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integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
NAD+ + (ADP-D-ribosyl)n-(EF-2)
nicotinamide + (ADP-D-ribosyl)n+1-(EF-2)
-
in native conformation, CRM66 shows limited ability to modify EF-2 covalently. Upon activation with urea and dithiothreitol CRM66 loses ADP-ribosylation activity entirely, yet it retains the ability to bind NAD+. Replacement of Tyr-426 with histidine in CRM66 completely restores cytotoxicity and ADP-ribosyltransferase activity
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
NAD+ + (ADP-D-ribosyl)n-actin
nicotinamide + (ADP-D-ribosyl)n+1-actin
VahC is shown to ADP-ribosylate Arg-177 of actin. VahC activity causes depolymerization of actin filaments, which induces caspase-mediated apoptosis in HeLa Tet-Off cells
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?
NAD+ + (ADP-D-ribosyl)n-apolipoprotein
nicotinamide + (ADP-D-ribosyl)n+1-apolipoprotein
-
-
-
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?
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-beta-transducin repeat-containing protein
nicotinamide + (ADP-D-ribosyl)n+1-beta-transducin repeat-containing protein + H+
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-
-
-
?
NAD+ + (ADP-D-ribosyl)n-biotin
nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+
NAD+ + (ADP-D-ribosyl)n-Crk-I
nicotinamide + (ADP-D-ribosyl)n+1-Crk-I
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Crk-II
nicotinamide + (ADP-D-ribosyl)n+1-Crk-II
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-His6HRas
nicotinamide + (ADP-D-ribosyl)n+1-His6HRas
-
the enzyme preferentially ADP-ribosylates membrane-associated His6HRas relative to its cytosolic His6HRasDELTACAAX with a C-terminal deletion
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?
NAD+ + (ADP-D-ribosyl)n-immunoglobulin A
nicotinamide + (ADP-D-ribosyl)n+1-immunoglobulin A
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-immunoglobulin G
nicotinamide + (ADP-D-ribosyl)n+1-immunoglobulin G
-
preferentially IgG3
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-
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
the enzyme prevents poly-ubiquitination of NEMO protein
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-
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
NAD+ + (ADP-D-ribosyl)n-P2X7 ion channel
nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-peptide LL-37
nicotinamide + (ADP-D-ribosyl)n+1-peptide LL-37 + H+
up to four of the five arginine residues present in peptide LL-37 can be ADP-ribosylated on the same peptide when incubated at a high NAD concentration
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?
NAD+ + (ADP-D-ribosyl)n-Rab2
nicotinamide + (ADP-D-ribosyl)n+1-Rab2
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-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab3
nicotinamide + (ADP-D-ribosyl)n+1-Rab3
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5 + H+
-
the enzyme ADP-ribosylates Rab5 at Gln79
-
-
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
NAD+ + (ADP-D-ribosyl)n-Rap1A
nicotinamide + (ADP-D-ribosyl)n+1-Rap1A
-
-
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-
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
NAD+ + (ADP-D-ribosyl)n-Ras protein
nicotinamide + (ADP-D-ribosyl)n+1-Ras protein
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-
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-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
NAD+ + (ADP-D-ribosyl)n-serine/arginine-rich protein-specific kinase 2
nicotinamide + (ADP-D-ribosyl)n+1-serine/arginine-rich protein-specific kinase 2 + H+
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?
NAD+ + (ADP-D-ribosyl)n-soybean trypsin inhibitor
nicotinamide + (ADP-D-ribosyl)n+1-soybean trypsin inhibitor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-soybean-trypsin-inhibitor
nicotinamide + (ADP-D-ribosyl)n+1-soybean-trypsin-inhibitor
-
-
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?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Btk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Btk + H+
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-
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-
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Csk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Csk + H+
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-
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-
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Hck
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Hck + H+
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-
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?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Lyn
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Lyn + H+
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-
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?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Src
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Src + H+
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-
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?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Syk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Syk + H+
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-
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?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Tec
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Tec + H+
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?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Yes1
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Yes1 + H+
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-
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?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
NAD+ + Galphai3C20
nicotinamide + N-(ADP-D-ribosyl)-Galphai3C20
-
-
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-
?
NAD+ + GTPase RhoA
nicotinamide + (ADP-D-ribosyl)-GTPase RhoA
-
the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
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-
?
NAD+ + GTPase RhoB
nicotinamide + (ADP-D-ribosyl)-GTPase RhoB
-
the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
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-
?
NAD+ + GTPase RhoC
nicotinamide + (ADP-D-ribosyl)-GTPase RhoC
-
the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
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?
NAD+ + H2O
nicotinamide + ADP-ribose
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?
NAD+ + histone H1
nicotinamide + (ADP-D-ribosyl)-histone H1
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-
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?
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
NAD+ + lymphocyte function-associated antigen LFA-1
nicotinamide + ?
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?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
NAD+ + p53
nicotinamide + (ADP-D-ribosyl)-p53
NAD+ + poly(ADP-ribose) polymerase-1
nicotinamide + (ADP-ribosyl)-poly(ADP-ribose) polymerase-1
-
the 40 kDa CD fragment of avian PARP-1 efficiently catalyzes a covalent auto-poly-(ADP-ribosyl)ation reaction via an intermolecular mechanism that is completely independent of DNA
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?
NAD+ + Rab31
nicotinamide + (ADP-D-ribosyl)-Rab31 + H+
-
the enzyme ADP-ribosylates Rab31 at Gln64
-
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
NAD+ + Ras
nicotinamide + (ADP-D-ribosyl)-Ras
-
interaction requires residue Leu428
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-
?
NAD+ + Ras GTPase
nicotinamide + (ADP-D-ribosyl)-Ras GTPase
-
-
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-
?
NAD+ + Ras2p
nicotinamide + (ADP-D-ribosyl)-Ras2p + H+
-
Ras2p is a yeast protein, activity absolutely requires the yeast protein Bmh1p
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-
?
NAD+ + RhoA
nicotinamide (ADP-D-ribosyl)-RhoA
NAD+ + RhoB
nicotinamide (ADP-D-ribosyl)-RhoB
NAD+ + RhoC
nicotinamide (ADP-D-ribosyl)-RhoC
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
NAD+ + soybean trypsin inhibitor
nicotinamide + (ADP-D-ribosyl)-soybean trypsin inhibitor
-
the exoenzyme modifies the substrate at an arginine residue
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-
?
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
NAD+ + vimentin
nicotinamide + (ADP-D-ribosyl)-vimentin
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-
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?
NAD+ + wild-type exoenzyme C3
nicotinamide + (ADP-D-ribosyl)-wild-type exoenzyme C3
-
activity of the recombinant mutant Q217E exoenzyme C3, modification at Arg86
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-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein
nicotinamide + ?
additional information
?
-
integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
the extracellular domain of integrin alpha7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 muscle cells, integrin alpha7 N-terminal ADP-ribosylation inhibits the binding of integrin alpha7beta1 to laminin activation status of integrin alpha7beta1 in intact myotubes, overview
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?
integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
the extracellular domain of integrin alpha7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 muscle cells, integrin alpha7 ADP-ribosylation inhibits the binding of integrin alpha7beta1 to laminin, binding site, overview
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone H1
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
the enzyme is a DNA repair enzyme
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of 21000-24000 Da platelet membrane proteins
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
Cryptothecodinium cohnii
-
poly(ADP-ribosyl)ation of histone
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone H1
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
linking a long negatively charged polymer to a protein, PARP catalyzes the polymerization of ADP-ribose units from donor NAD+ molecules on target proteins, resulting in the attachment of PAR, each residue in PAR contains an adenine moiety capable of base stacking and hydrogen bonding, as well as two phosphate groups that carry negative charges, substrate structure, overview
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of topoisomerase I
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
auto-poly(ADP-ribosyl)ation
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of high mobility group proteins
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of DNA ligase
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of endonuclease
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of topoisomerase II
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of terminal deoxynucleotidyltransferase
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone H1
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
catalyzes poly(ADP-ribosyl)ation of the synthetase itself, automodification
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of ADP-ribosyltransferase
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
linking a long negatively charged polymer to a protein, PARP-1 catalyzes the polymerization of ADP-ribose units from donor NAD+ molecules on target proteins, resulting in the attachment of PAR, each residue in PAR contains an adenine moiety capable of base stacking and hydrogen bonding, as well as two phosphate groups that carry negative charges, substrate structure, overview
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
agmatine as ADPribose acceptor is used
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
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-
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ADPRT domain of ExoT is active in vivo and contributes to the pathogenesis of Pseudomonas aeruginosa infections
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
exoenzyme S is an ADP-ribosyltransferase produced and directly translocated into eukaryotic cells by the opportunistic pathogen Pseudomonas aeruginosa. Factors expressed by growing epithelial cells are required for the bacterial contact-dependent translocation of ExoS. As normal epithelial cells differentiate into polarized confluent monolayers, expression of these factors is altered, and cells in turn become more resistant to the effects of ExoS
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS can modify multiple GTPases of the Ras superfamily in vivo. ExoS modulates the activity of several of GTP-binding proteins, such as Ras, Rap1, Rap2, Ral, Rac1, RhoA and Cdc42. It is suggested that ExoS is the major ADP-ribosyltransferase protein modulating small GTPase function encoded by Pseudomonas aeruginosa
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT modifies and inactivates host cell proteins involved in maintaining the actin cytoskeleton in vivo by two independent mechanisms. ADP-ribosylation activity of ExoT induces an irreversible disruption of actin microfilaments of infected Hela cells
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
intracellular expression of the amino terminus of ExoS in eukaryotic cells stimulates actin reorganization without cytotoxicity, which involves small-molecular-weight GTPases of the Rho subfamily
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
intracellular Ras is modified by bacterially translocated ExoS, inhibition of target cell proliferation correlates with the efficiency of Ras modification
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS has polysubstrate specificity and can ADP-ribosylate numerous host proteins, e.g. monomeric GTPase or vimentin. ExoS also undergoes auto-ADP-ribosylation. Ras has multiple alternative sites for ADP-ribosylation
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS is a type III cytotoxin which modulates two eukaryotic signalling pathways. The N-terminus (residues 1-234) is a GTPase activating protein for RhoGTPases, while the C-terminus (residues 232-453) encodes an ADP-ribosyltransferase
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?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS has polysubstrate specificity and can ADP-ribosylate numerous host proteins, e.g. monomeric GTPase or vimentin. ExoS also undergoes auto-ADP-ribosylation. Ras has multiple alternative sites for ADP-ribosylation
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS has polysubstrate specificity and can ADP-ribosylate numerous host proteins, e.g. monomeric GTPase or vimentin. ExoS also undergoes auto-ADP-ribosylation. Ras has multiple alternative sites for ADP-ribosylation
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-biotin
nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-biotin
nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
ADP-ribosylation of p21ras does not alter interactions with guanidine nucleotides. Possible function of the enzyme in pathogenesis
-
-
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
ADP-ribosylation affects Rab4 function in membrane recycling
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
ADP-ribosylation of Rab5 by ExoS affects endocytosis. Interaction of Rab5 with endosome antigen 1 is markedly diminished after Rab5 ADP-ribosylation by ExoS
-
-
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
ADP-ribosylation of RalA by ExoS interferes with RalA activation and binding to its downstream effector in J774A.1 macrophages and suggests the potential of ExoS ADPRT activity to interfere with filiopodium formation through the inactivation of RalA and downstream effects mediated through the exocyst complex
-
-
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
ADP-ribosylation of Ras at Arg41 disrupts Ras-Cdc25 interactions, which inhibits the rate-limiting step in Ras signal transduction, the activation of Ras by its guanine nucleotide exchange factor
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
-
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
a non-G-protein substrate with peptidyl-prolyl isomerase activity, from several human epithelial cells, modification at Arg55 and Arg69, but not at Arg148, of cyclophilin A, i.e. CpA, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, activity with CpA mutants, overview
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
a non-G-protein substrate with peptidyl-prolyl isomerase activity, from several human epithelial cells, modification at Arg55 and Arg69, but not at Arg148, of cyclophilin A, i.e. CpA, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, activity with CpA mutants, overview
-
-
?
NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
-
-
-
?
NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
-
-
-
?
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
-
?
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B
-
-
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
-
-
-
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
-
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B
-
-
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
-
ADP-ribosylated-moesin is a poor target for phosphorylation by protein kinase C and Rho kinase, which shows that ADP-ribosylation directly inhibits ERM phosphorylation
-
-
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
-
modification of Arg553, Arg560 and Arg563, activity with wild-type and mutant moesins, overview
-
-
?
NAD+ + p53
nicotinamide + (ADP-D-ribosyl)-p53
-
-
-
-
?
NAD+ + p53
nicotinamide + (ADP-D-ribosyl)-p53
-
PARP-1 interacts with and poly(ADP-ribosyl)ates p53, which participates in DNA recombination
-
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
-
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
-
-
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
-
-
-
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
-
-
-
?
NAD+ + RhoA
nicotinamide (ADP-D-ribosyl)-RhoA
-
-
-
-
?
NAD+ + RhoA
nicotinamide (ADP-D-ribosyl)-RhoA
-
-
-
-
?
NAD+ + RhoB
nicotinamide (ADP-D-ribosyl)-RhoB
-
-
-
-
?
NAD+ + RhoB
nicotinamide (ADP-D-ribosyl)-RhoB
-
-
-
-
?
NAD+ + RhoC
nicotinamide (ADP-D-ribosyl)-RhoC
-
weak activity
-
-
?
NAD+ + RhoC
nicotinamide (ADP-D-ribosyl)-RhoC
-
weak activity
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4
-
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4
three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModA
-
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModA
three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModB
-
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModB
three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
-
-
?
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
-
-
-
-
?
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
-
PARP-1 interacts with and poly(ADP-ribosyl)ates topoisomerase I, which participates in DNA recombination, I-SceI-meganuclease-mediated cleavage terminates the interaction, overview
-
-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein
nicotinamide + ?
-
-
-
-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein
nicotinamide + ?
-
-
-
-
?
additional information
?
-
-
cuts produced in vivo on DNA during DNA repair activate the enzyme, which then synthesiszes poly(ADP-ribose) on histone H1, in particular, and contributes to the opening of the 25 nm chromatin fiber, resulting in the increased accessibility of DNA to excision repair enzymes
-
-
?
additional information
?
-
-
the enzyme modifies eukaryotic 21000-24000 Da GTP-binding proteins
-
-
?
additional information
?
-
-
transcriptional regulation mechanism, overview
-
-
?
additional information
?
-
-
the enzyme also shows NAD+-hydrolase activity
-
-
?
additional information
?
-
-
ADP-ribosylation seems to be involved in regulation of differentiation, the enzyme may be centrally involved in tumorigenic cell transformation, the enzyme appears to be a central controller of cell processes: higher activities shift the cell towards proliferation, low activities shift the cell towards differentiation, role of the enzyme in DNA repair
-
-
?
additional information
?
-
-
role of the enzyme in DNA repair, the unmodified polymerase molecules bind tightly to DNA strand breaks: auto-poly(ADP-ribosyl)ation of the protein then effects its release and allows access to lesions for DNA repair enzymes
-
-
?
additional information
?
-
-
mechanistic basis for the physiological function of PARP-1 in the dynamics of the local modulation of chromatin structure. PARP-1 activation upon binding to base-unpaired regions and stem-loops structures in DNA leads to a local PAR modification of histones and non-histone proteins at genomic sites where such DNA structures are formed. Subsequent PARP-1 automodification results in its dissociation from DNA leading to an enzymatic self-inactivation thus ensuring a transient character of chromatin ADP-ribosylation. In combination with the PAR-glycohydrolase degradation of ADP-ribose polymers on acceptor proteins, PARP-1 interaction with DNA secondary structures provides a mechanism for local and transient chromatin modification by PAR during physiological nuclear processes
-
-
?
additional information
?
-
-
PARP-1 inhibits the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP. Inhibition of TonEBP/OREBP transcriptional activity by PARP-1 does not require PARP-1 catalytic activity, functional interaction anaylsis, overview
-
-
?
additional information
?
-
-
the enzyme is involved in pathogenesis of Parkinson's disease, analysis of polymorphisms, overview
-
-
?
additional information
?
-
-
the enzyme shows DNA-binding activity, and is physically associated with the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP
-
-
?
additional information
?
-
-
the enzyme has the ability to ADP-ribosylate itself
-
-
?
additional information
?
-
-
raft association focuses ART2.2 on specific targets that constitutively or inducibly assoiate with lipid rafts
-
-
?
additional information
?
-
-
ART1 is an arginine-specific transferase
-
-
?
additional information
?
-
-
PARP-1 is involved in modulation of NO-derived injury and response to genotoxic damage
-
-
?
additional information
?
-
-
PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
-
-
?
additional information
?
-
-
PARP-1 plays fundamental roles in the recruitment and modulation of enzymatic and regulatory factors involved in transcription, DNA replication, repair and recombination, the enzyme antagonizes topoisomerase I-dependent recombination stimulation by P53
-
-
?
additional information
?
-
-
PARP-1 responds to DNA damage by transferring 50 to 200 molecules of ADP-ribose to various nuclear proteins, including transcription factors, histones and PARP-1 itself, interaction between ATM and PARP-1 in response to DNA damage and sensitization of ATM deficient cells through PARP inhibition, ATM and PARP-1 are two of the most important players in the cell's response to DNA damage, PARP-1 is needed for optimal activation of ATM, overview
-
-
?
additional information
?
-
-
role for PARP-1 in DNA double-strand break repair, the enzyme is not required for homologous recombination itself, it regulates the process through its involvement in the repair of DNA single-strand breaks, PARP-1 binds to DNA breaks to facilitate DNA repair, but the role of PARP-1 in DNA repair appears to not be critical since PARP-1 knockout mice are viable, fertile and do not develop early onset tumors, DNA binding and auto-modification of PARP-1 attracts the DNA repair proteins
-
-
?
additional information
?
-
-
the enzyme is involved in endothelial cell dysfunction
-
-
?
additional information
?
-
-
transcriptional regulation mechanism, overview
-
-
?
additional information
?
-
-
PARP-1 protein has an N-terminal DNA binding domain containing two large zinc fingers that bind to both DNA single-strand breaks and DNA double-strand breaks, DNA binding by PARP-1 triggers its activity and it adds poly(ADP-ribose) polymers to itself and to surrounding histones, overview
-
-
?
additional information
?
-
-
the enzyme itself is a target for P2X7-triggered ectodomain shedding at F239/S240
-
-
?
additional information
?
-
-
the enzyme is involved in endothelial cell dysfunction
-
-
?
additional information
?
-
-
PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
-
-
?
additional information
?
-
-
narE possesses ADP-ribosylating and NAD-glycohydrolase activities
-
-
?
additional information
?
-
-
exoenzyme S and 14-3-3 interact in a direct fashion, interaction involves the conserved amphiphatic groove of 14-3-3
-
-
?
additional information
?
-
-
exoenzyme S is an important adhesin
-
-
?
additional information
?
-
-
ExoS is a virulence factor of the pathogen
-
-
?
additional information
?
-
-
Pseudomonas aeruginosa inhibits mammalian cytokinesis in a type III secretion system and exotoxin T-dependent manner, the ADP-ribosyl transferase domain inhibits late steps of cytokinesis by blocking syntaxin-2 localization to the midbody, an event essential for completion of cytokinesis, e.g. in Madin-Darby canine kidney cells, mechanism, overview
-
-
?
additional information
?
-
-
the bacterial enzyme shows the ability to mediate cell death in the host and is a toxin, residues 426-428 are required for this activity
-
-
?
additional information
?
-
-
exoenzyme S is a bifunctional type III secretion, TTS, effector protein, with GTPase-activating and ADP-ribosyltransferase activities
-
-
?
additional information
?
-
-
ExoS is a bifunctional toxin with an N-terminal Rho GTPase activating protein, GAP, domain, and a C-terminal ADP-ribosyltransferase domain which transfers ADP-ribose from NAD onto substrates such as the Ras GTPases and vimentin
-
-
?
additional information
?
-
-
ExoT is a bifunctional type III secretion system effector protein that contains an N-terminal GTPase-activating protein domain and a C-terminal ADP-ribosyl transferase domain
-
-
?
additional information
?
-
-
ExoS is a toxin playing a pivotal role during Pseudomonas aeruginosa infections, it is a virulence factor causing growth inhibition in Saccharomyces cerevisiae. Exoenzyme S ADP-ribosylates identical targets in both human and yeast
-
-
?
additional information
?
-
-
ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
-
-
?
additional information
?
-
-
ExoS is a bi-functional type III cytotoxin that possesses Rho GTPase activating protein and ADP-ribosyltransferase activities, no activity with Rab4 protein, overview
-
-
?
additional information
?
-
-
exoenzyme S is a bifunctional type III secretion, TTS, effector protein, with GTPase-activating and ADP-ribosyltransferase activities
-
-
?
additional information
?
-
-
ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
-
-
?
additional information
?
-
-
ExoS is a bi-functional type III cytotoxin that possesses Rho GTPase activating protein and ADP-ribosyltransferase activities, no activity with Rab4 protein, overview
-
-
?
additional information
?
-
the enzyme also targets deoxyguanosine
-
-
?
additional information
?
-
-
the enzyme also targets deoxyguanosine
-
-
?
additional information
?
-
the enzyme also targets deoxyguanosine
-
-
?
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integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
the extracellular domain of integrin alpha7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 muscle cells, integrin alpha7 N-terminal ADP-ribosylation inhibits the binding of integrin alpha7beta1 to laminin activation status of integrin alpha7beta1 in intact myotubes, overview
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-beta-transducin repeat-containing protein
nicotinamide + (ADP-D-ribosyl)n+1-beta-transducin repeat-containing protein + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
the enzyme prevents poly-ubiquitination of NEMO protein
-
-
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
ADP-ribosylation of p21ras does not alter interactions with guanidine nucleotides. Possible function of the enzyme in pathogenesis
-
-
?
NAD+ + (ADP-D-ribosyl)n-P2X7 ion channel
nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
ADP-ribosylation affects Rab4 function in membrane recycling
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
ADP-ribosylation of Rab5 by ExoS affects endocytosis. Interaction of Rab5 with endosome antigen 1 is markedly diminished after Rab5 ADP-ribosylation by ExoS
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5 + H+
-
the enzyme ADP-ribosylates Rab5 at Gln79
-
-
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
ADP-ribosylation of RalA by ExoS interferes with RalA activation and binding to its downstream effector in J774A.1 macrophages and suggests the potential of ExoS ADPRT activity to interfere with filiopodium formation through the inactivation of RalA and downstream effects mediated through the exocyst complex
-
-
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
ADP-ribosylation of Ras at Arg41 disrupts Ras-Cdc25 interactions, which inhibits the rate-limiting step in Ras signal transduction, the activation of Ras by its guanine nucleotide exchange factor
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Btk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Btk + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Csk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Csk + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Hck
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Hck + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Lyn
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Lyn + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Src
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Src + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Syk
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Syk + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Tec
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Tec + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-tyrosine kinase Yes1
nicotinamide + (ADP-D-ribosyl)n+1-tyrosine kinase Yes1 + H+
-
-
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
-
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
-
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
-
ADP-ribosylated-moesin is a poor target for phosphorylation by protein kinase C and Rho kinase, which shows that ADP-ribosylation directly inhibits ERM phosphorylation
-
-
?
NAD+ + p53
nicotinamide + (ADP-D-ribosyl)-p53
-
-
-
-
?
NAD+ + Rab31
nicotinamide + (ADP-D-ribosyl)-Rab31 + H+
-
the enzyme ADP-ribosylates Rab31 at Gln64
-
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
NAD+ + Ras
nicotinamide + (ADP-D-ribosyl)-Ras
-
interaction requires residue Leu428
-
-
?
NAD+ + Ras GTPase
nicotinamide + (ADP-D-ribosyl)-Ras GTPase
-
-
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
-
-
-
-
?
NAD+ + vimentin
nicotinamide + (ADP-D-ribosyl)-vimentin
-
-
-
-
?
additional information
?
-
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
the enzyme is a DNA repair enzyme
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ADPRT domain of ExoT is active in vivo and contributes to the pathogenesis of Pseudomonas aeruginosa infections
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
exoenzyme S is an ADP-ribosyltransferase produced and directly translocated into eukaryotic cells by the opportunistic pathogen Pseudomonas aeruginosa. Factors expressed by growing epithelial cells are required for the bacterial contact-dependent translocation of ExoS. As normal epithelial cells differentiate into polarized confluent monolayers, expression of these factors is altered, and cells in turn become more resistant to the effects of ExoS
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS can modify multiple GTPases of the Ras superfamily in vivo. ExoS modulates the activity of several of GTP-binding proteins, such as Ras, Rap1, Rap2, Ral, Rac1, RhoA and Cdc42. It is suggested that ExoS is the major ADP-ribosyltransferase protein modulating small GTPase function encoded by Pseudomonas aeruginosa
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT modifies and inactivates host cell proteins involved in maintaining the actin cytoskeleton in vivo by two independent mechanisms. ADP-ribosylation activity of ExoT induces an irreversible disruption of actin microfilaments of infected Hela cells
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
intracellular expression of the amino terminus of ExoS in eukaryotic cells stimulates actin reorganization without cytotoxicity, which involves small-molecular-weight GTPases of the Rho subfamily
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
intracellular Ras is modified by bacterially translocated ExoS, inhibition of target cell proliferation correlates with the efficiency of Ras modification
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
-
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
-
-
?
NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
-
-
-
?
NAD+ + Galphai
nicotinamide + (ADP-D-ribosyl)-Galphai + H+
-
-
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
-
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
-
-
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
-
-
-
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
-
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4
three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModA
three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
Tequatrovirus T4 ModB
three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
-
-
?
additional information
?
-
-
cuts produced in vivo on DNA during DNA repair activate the enzyme, which then synthesiszes poly(ADP-ribose) on histone H1, in particular, and contributes to the opening of the 25 nm chromatin fiber, resulting in the increased accessibility of DNA to excision repair enzymes
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-
?
additional information
?
-
-
the enzyme modifies eukaryotic 21000-24000 Da GTP-binding proteins
-
-
?
additional information
?
-
-
transcriptional regulation mechanism, overview
-
-
?
additional information
?
-
-
ADP-ribosylation seems to be involved in regulation of differentiation, the enzyme may be centrally involved in tumorigenic cell transformation, the enzyme appears to be a central controller of cell processes: higher activities shift the cell towards proliferation, low activities shift the cell towards differentiation, role of the enzyme in DNA repair
-
-
?
additional information
?
-
-
role of the enzyme in DNA repair, the unmodified polymerase molecules bind tightly to DNA strand breaks: auto-poly(ADP-ribosyl)ation of the protein then effects its release and allows access to lesions for DNA repair enzymes
-
-
?
additional information
?
-
-
mechanistic basis for the physiological function of PARP-1 in the dynamics of the local modulation of chromatin structure. PARP-1 activation upon binding to base-unpaired regions and stem-loops structures in DNA leads to a local PAR modification of histones and non-histone proteins at genomic sites where such DNA structures are formed. Subsequent PARP-1 automodification results in its dissociation from DNA leading to an enzymatic self-inactivation thus ensuring a transient character of chromatin ADP-ribosylation. In combination with the PAR-glycohydrolase degradation of ADP-ribose polymers on acceptor proteins, PARP-1 interaction with DNA secondary structures provides a mechanism for local and transient chromatin modification by PAR during physiological nuclear processes
-
-
?
additional information
?
-
-
PARP-1 inhibits the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP. Inhibition of TonEBP/OREBP transcriptional activity by PARP-1 does not require PARP-1 catalytic activity, functional interaction anaylsis, overview
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-
?
additional information
?
-
-
the enzyme is involved in pathogenesis of Parkinson's disease, analysis of polymorphisms, overview
-
-
?
additional information
?
-
-
the enzyme has the ability to ADP-ribosylate itself
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-
?
additional information
?
-
-
raft association focuses ART2.2 on specific targets that constitutively or inducibly assoiate with lipid rafts
-
-
?
additional information
?
-
-
PARP-1 is involved in modulation of NO-derived injury and response to genotoxic damage
-
-
?
additional information
?
-
-
PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
-
-
?
additional information
?
-
-
PARP-1 plays fundamental roles in the recruitment and modulation of enzymatic and regulatory factors involved in transcription, DNA replication, repair and recombination, the enzyme antagonizes topoisomerase I-dependent recombination stimulation by P53
-
-
?
additional information
?
-
-
PARP-1 responds to DNA damage by transferring 50 to 200 molecules of ADP-ribose to various nuclear proteins, including transcription factors, histones and PARP-1 itself, interaction between ATM and PARP-1 in response to DNA damage and sensitization of ATM deficient cells through PARP inhibition, ATM and PARP-1 are two of the most important players in the cell's response to DNA damage, PARP-1 is needed for optimal activation of ATM, overview
-
-
?
additional information
?
-
-
role for PARP-1 in DNA double-strand break repair, the enzyme is not required for homologous recombination itself, it regulates the process through its involvement in the repair of DNA single-strand breaks, PARP-1 binds to DNA breaks to facilitate DNA repair, but the role of PARP-1 in DNA repair appears to not be critical since PARP-1 knockout mice are viable, fertile and do not develop early onset tumors, DNA binding and auto-modification of PARP-1 attracts the DNA repair proteins
-
-
?
additional information
?
-
-
the enzyme is involved in endothelial cell dysfunction
-
-
?
additional information
?
-
-
transcriptional regulation mechanism, overview
-
-
?
additional information
?
-
-
the enzyme itself is a target for P2X7-triggered ectodomain shedding at F239/S240
-
-
?
additional information
?
-
-
the enzyme is involved in endothelial cell dysfunction
-
-
?
additional information
?
-
-
PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
-
-
?
additional information
?
-
-
exoenzyme S and 14-3-3 interact in a direct fashion, interaction involves the conserved amphiphatic groove of 14-3-3
-
-
?
additional information
?
-
-
exoenzyme S is an important adhesin
-
-
?
additional information
?
-
-
ExoS is a virulence factor of the pathogen
-
-
?
additional information
?
-
-
Pseudomonas aeruginosa inhibits mammalian cytokinesis in a type III secretion system and exotoxin T-dependent manner, the ADP-ribosyl transferase domain inhibits late steps of cytokinesis by blocking syntaxin-2 localization to the midbody, an event essential for completion of cytokinesis, e.g. in Madin-Darby canine kidney cells, mechanism, overview
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-
?
additional information
?
-
-
the bacterial enzyme shows the ability to mediate cell death in the host and is a toxin, residues 426-428 are required for this activity
-
-
?
additional information
?
-
-
ExoS is a toxin playing a pivotal role during Pseudomonas aeruginosa infections, it is a virulence factor causing growth inhibition in Saccharomyces cerevisiae. Exoenzyme S ADP-ribosylates identical targets in both human and yeast
-
-
?
additional information
?
-
-
ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
-
-
?
additional information
?
-
-
ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
-
-
?
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(1E,4E)-1,5-di(pyridin-3-yl)penta-1,4-dien-3-one
i.e. NSC149286
(2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanamide
-
(beta,beta-dimethylacryl)shikonin
64% inhibition at 0.01 mM; 64% inhibition at 0.01 mM
0469-0796
-
restores yeast growth after treatment with ExoS
1(2H)-phthalazinone
-
IC50: 0.012 mM
1,2-benzopyrone
-
IC50: 2.8 mM
1,3-benzodiazine
-
IC50: 2.0 mM
1,3-dihydroxynaphthalene
-
IC50: 1.3 mM
1,4-benzoquinone
-
IC50: 0.4 mM
1,4-naphthalenedione
-
IC50: 0.25 mM
1,5-dihydroxyisoquinoline
-
IC50: 0.00039 mM
1,8-naphthalimide
-
IC50: 0.0014 mM
1-hydroxy-2-methyl-4-aminonaphthalene
-
IC50: 1.3 mM
1-hydroxyisoquinoline
-
IC50: 0.007 mM
1-Indanone
-
IC50: 0.81 mM
1-methylnicotinamide chloride
2,3-benzodiazine
-
IC50: 0.15 mM
2,3-dichloro-1,4-naphthoquinone
-
IC50: 0.26 mM
2,3-dihydro-1,4-phthalazinedione
-
IC50: 0.03 mM
2,3-dihydro-5-hydroxy-1,4-phthalazinedione
-
0.001 mM, 95% inhibition of the 116000 Da enzyme
2,4(1H,3H)-quinazolinedione
-
IC50: 0.0081 mM
2,6-difluorobenzamide
-
IC50: 0.18 mM
2-(3-hydroxypropyl)-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-4-one
-
-
2-(3-hydroxypropyl)-5,6,7,8-tetrahydro[1]benzothieno[2,3-d]pyrimidin-4(3H)-one
-
-
2-(4-[4-[(2,4-dimethoxyphenyl)amino]quinazolin-2-yl]piperazin-1-yl)ethanol
-
2-acetamidobenzamide
-
IC50: 1.0 mM
2-amino-3-chloro-1,4-naphthoquinone
-
IC50: 0.82 mM
2-bromobenzamide
-
IC50: 2.9 mM
2-chlorobenzamide
-
IC50: 1.0 mM
2-fluorobenzamide
-
IC50: 0.12 mM
2-Hydroxy-1,4-naphthoquinone
-
IC50: 0.33 mM
2-hydroxybenzamide
-
IC50: 0.82 mM
2-mercapto-4(3H)-quinazolinone
-
IC50: 0.044 mM
2-Methoxybenzamide
-
IC50: 0.2 mM
2-methyl-1,4-benzopyrone
-
IC50: 0.045 mM
2-methyl-1,4-naphthoquinone
-
IC50: 0.42 mM
2-methyl-3-phytyl-1,4-naphthoquinone
-
IC50: 0.52 mM
2-methyl-4(3H)-quinazolinone
-
IC50: 0.056 mM
2-methylbenzamide
-
IC50: 1.5 mM
2-methylchromone
-
IC50: 0.045 mM
2-nitro-6(5H)-phenanthridione
-
IC50: 0.00035 mM
2-phenylchromone
-
IC50: 0.022 mM
2-trichloromethyl-4(3H)-quinazolinone
-
IC50: 2.2 mM
2-[[3-(dimethylamino)-2-oxopropyl]amino]-5,6-dihydrophenanthridin-6-one
potent inhibitor
2H-benz[c]isoquinolin-1-one
-
IC50: 0.0003 mM
2H-benz[de]isoquinoline-1,3-dione
-
IC50: 0.0014 mM
3,4-dihydro-1(2H)-naphthalenone
-
IC50: 0.31 mM
3,5-dibromosalicylamide
-
IC50: 0.56 mM
3,5-dimethoxybenzamide
-
IC50: 1.2 mM
3,5-dinitrobenzamide
-
IC50: 2.5 mM
3-(4-methoxy-6,7-dihydro-5H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
-
-
3-(4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl)propanoic acid
-
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-(pyridin-2-yl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-phenylethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-(pyridin-2-yl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylpropyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(4-sulfamoylphenyl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(pyridin-2-yl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoic acid
-
-
3-(4-oxo-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
-
inhibitor with micromolar potency
3-(N,N-dimethylamino)benzamide
-
IC50: 0.12 mM
3-Acetamidobenzamide
-
IC50: 0.012 mM
3-acetamidosalicylamide
-
IC50: 2.0 mM
3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole
-
i.e. Trp-P-1, 94% inhibition at 5 mM, IC50: 0.22 mM
3-amino-1-methyl-5H-pyrido[4,3-b]indole
-
i.e. Trp-P-2, 34% activation at 1 mM, 7% inhibition at 5 mM, IC50: 2.2 mM
3-aminobenzoic acid
-
1 mM, 12% inhibition
3-bromobenzamide
-
IC50: 0.055 mM
3-Chlorobenzamide
-
IC50: 0.22 mM
3-Fluorobenzamide
-
IC50: 0.2 mM
3-Guanidinobenzamide
-
0.1 mM, 71% inhibition of the 116000 Da enzyme
3-isobutyl-1-methylxanthine
-
IC50: 3.1 mM
3-Methylbenzamide
-
IC50: 0.19 mM
3-nitrobenzamide
-
IC50: 0.16 mM
3-nitrophthalhydrazide
-
IC50: 0.072 mM
3-nitrosalicylamide
-
IC50: 1.6 mM
4,4'-(methylmino)dibenzamide
26% inhibition at 0.01 mM
4,4'-thiodibenzamide
30% inhibition at 0.01 mM
4,5,7,9-tetrahydro-2H-purine-2,8(3H)-dithione
i.e. NSC29193
4,8-dihydroxy-2-quinolinecarboxylic acid
-
IC50: 0.19 mM
4-(2-fluorophenoxy)benzamide
-
4-(2-phenoxyethoxy)benzamide
-
4-(4-aminophenoxy)benzamide
-
4-(4-carbamoylphenoxy)benzoic acid
-
4-(4-formylphenoxy)benzamide
-
4-(4-hydroxyphenoxy)benzamide
-
4-(4-methoxyphenoxy)benzamide
-
4-(4-nitrobenzoyl)benzamide
24% inhibition at 0.01 mM
4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanoic acid
-
-
4-(pyridin-2-yloxy)benzamide
49% inhibition at 0.01 mM
4-amino-1,8-naphthalimide
-
IC50: 0.00018 mM
4-aminophthalhydrazide
-
IC50: 0.29 mM
4-bromobenzamide
-
IC50: 2.2 mM
4-carbamoylphenyl benzoate
-
4-chlorobenzamide
-
IC50: 0.3 mM
4-chromanone
-
IC50: 0.72 mM
4-fluorobenzamide
-
IC50: 0.2 mM
4-hydroxy-2-methylquinoline
-
IC50: 0.074 mM
4-hydroxy-2-quinolinecarboxylic acid
-
IC50: 0.67 mM
4-Hydroxycoumarin
-
IC50: 0.57 mM
4-hydroxypyridine
-
IC50: 2.3 mM
4-hydroxyquinazoline
-
IC50: 0.0095 mM
4-hydroxyquinoline
-
IC50: 0.08 mM
4-methylbenzamide
-
IC50: 1.8 mM
4-nitro-7-[(1-oxo-1lambda(5)-pyridin-2-yl)sulfanyl]-2,1,3-benzoxadiazole
i.e. NSC228155
4-nitrophthalhydrazide
-
IC50: 0.51 mM
4-[(2-bromophenyl)methoxy]benzamide
-
4-[(2-fluorophenyl)methoxy]benzamide
-
4-[(3,5-dimethylphenyl)methoxy]benzamide
-
4-[(3-bromophenyl)methoxy]benzamide
-
4-[(3-fluorophenyl)methoxy]benzamide
-
4-[(4-cyanophenyl)thio]benzamide
16% inhibition at 0.01 mM
4-[(4-fluorophenyl)methoxy]benzamide
-
4-[(4-methylphenyl)methoxy]benzamide
-
4-[(naphthalen-1-yl)methoxy]benzamide
-
4-[(propan-2-yl)oxy]benzamide
-
4-[(pyridin-2-yl)methoxy]benzamide
-
4-[1-[4-(propan-2-yl)phenyl]ethoxy]benzamide
16% inhibition at 0.01 mM
4-[4-(1-aminoethenyl)phenoxy]benzamide
4-[8-fluoro-6-oxo-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-2-yl]butanoic acid
-
4-[[4-(aminocarbonyl)benzyl]oxy]benzamide
-
4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]-N,N-dimethylpiperidine-1-carboxamide
-
activates in presence of Mg2+, inhibits in absence of Mg2+
4296-1011
-
restores yeast growth after treatment with ExoS
5-acetamidosalicylamide
-
IC50: 0.045 mM
5-aminosalicylamide
-
IC50: 0.1 mM
5-bromodeoxyuridine
-
IC50: 0.015 mM
5-Bromouracil
-
IC50: 0.16 mM
5-Bromouridine
-
IC50: 0.21 mM
5-chlorosalicylamide
-
IC50: 0.19 mM
5-Chlorouracil
-
IC50: 0.27 mM
5-hydroxy-1,4-naphthoquinone
-
IC50: 0.25 mM
5-Hydroxy-2-methyl-1,4-naphthoquinone
-
IC50: 0.7 mM
5-Iodouracil
-
IC50: 0.071 mM
5-iodouridine
-
IC50: 0.043 mM
5-methyluracil
-
IC50: 0.29 mM
5-Nitrouracil
-
IC50: 0.43 mM
6(5H)-phenanthridinone
-
IC50: 0.0003 mM
6-aminocoumarin
-
IC50: 0.85 mM
6-aminonicotinamide
-
IC50: 1.1 mM
8-acetamidocarsalam
-
IC50: 1.4 mM
8-fluoro-2-[3-(piperidin-1-yl)propanesulfonyl]-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-6-one
-
8-fluoro-2-[3-(piperidin-1-yl)propyl]-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-6-one
-
8-Methylnicotinamide
-
IC50: 7.8 mM
acetophenone
-
IC50: 2.3 mM
ADP-D-ribose
-
5 mM, remaining activity: 7.3%
all-trans-retinal
-
IC50: 0.45 mM
Alpha-NAD+
-
0.5 mM, 40% inhibition of the 116000 Da enzyme, 44% inhibition of the 90000 Da enzyme
alpha-picolinamide
-
IC50: 0.25 mM
AMP
-
1 mM, remaining activity: 3.6%
benzoyleneurea
-
IC50: 0.0081 mM
bergapten
69% inhibition at 0.01 mM; 69% inhibition at 0.01 mM
carbonylsalicylamide
-
IC50: 0.46 mM
carsalam
-
5 mM, 88% inhibition in presence of Mg2+, 68% inhibition in absence of Mg2+
Chlorthenoxazin
-
IC50: 0.0085 mM
chromone-2-carboxylic acid
-
IC50: 0.56 mM
cyclohexanecarboxamide
-
IC50: 0.62 mM
deoxyshikonin
67% inhibition at 0.01 mM; 67% inhibition at 0.01 mM
diosmin
-
restores yeast growth after treatment with ExoS
DMSO
at 2% (v/v) DMSO isoform ARTD10 loses more than half of its activity; at 2% (v/v) DMSO isoform ARTD7 loses its activity completely
E216-5303
-
restores yeast growth after treatment with ExoS
EB-47
i.e. 5'-deoxy-5'-[4-[2-[(2,3-dihydro-1-oxo-1H-isoindol-4-yl)amino]-2-oxoethyl]-1-piperazinyl]-5'-oxoadenosine dihydrochloride; i.e. 5'-deoxy-5'-[4-[2-[(2,3-dihydro-1-oxo-1H-isoindol-4-yl)amino]-2-oxoethyl]-1-piperazinyl]-5'-oxoadenosine dihydrochloride
EDTA
-
5 mM, 41% inhibition in presence of Mg2+, 2% inhibition in absence of Mg2+
embelin
57% inhibition at 0.01 mM; 57% inhibition at 0.01 mM
everninic acid
-
restores yeast growth after treatment with ExoS
exosin
-
a small molecule inhibitor, that modulates ExoS ADP-ribosyltransferase activity in vitro, suggesting the inhibition is direct. Exosin and two of its analogues display a significant protective effect against Pseudomonas infection in vivo, competitive against NAD+
flavokawain B
-
restores yeast growth after treatment with ExoS
gambogic acid
75% inhibition at 0.01 mM; 75% inhibition at 0.01 mM
gamma-linolenic acid
-
IC50: 0.12 mM
gossypol
75% inhibition at 0.01 mM; 75% inhibition at 0.01 mM
GTP(gammaS)
-
in presence of Mg2+
hypoxanthine
-
IC50: 1.7 mM
Isonicotinamide
-
IC50: 0.99 mM
Isonicotinate hydrazide
-
IC50: 4.8 MM
Isoquinoline
-
5 mM, 47% inhibition in presence of Mg2+, 34% inhibition in absence of Mg2+
linoleic acid
-
IC50: 0.048 mM
linolenic acid
-
IC50: 0.11 mM
m-acetamidoacetophenone
-
IC50: 0.93 mM
m-aminoacetophenone
-
IC50: 1.9 mM
m-hydroxyacetophenone
-
IC50: 0.6 mM
m-phthalamide
-
IC50: 0.05 mM
menadione
55% inhibition at 0.01 mM; 55% inhibition at 0.01 mM
menadione sodium bisulfite
-
IC50: 0.72 mM
methyl (2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanoate
-
myricetin
78% inhibition at 0.01 mM; 78% inhibition at 0.01 mM
N-(2-chloroethyl)1,8-naphthalamide
-
IC50: above 1.8 mM
N-(6-oxo-5,6-dihydrophenanthrolin-2-yl)-(N,N-dimethylamino)acetamide
-
0.1 mM, remaining activity: 36.2%
N-(acridin-9-yl)-4-nitrobenzamide
-
N-hydroxynaphthalimide sodium salt
-
IC50: 0.45 mM
N-[(1R)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(1S)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxybutan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxypropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[1-[4-(1H-imidazol-1-yl)phenyl]ethyl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[2-oxo-4-(phenylamino)-3,8a-dihydro-2H-chromen-3-yl]acetamide
-
N-[[1-(1H-pyrazolo[3,4-d]pyrimidin-4-yl)piperidin-3-yl]methyl]methanesulfonamide
-
novobiocin
-
IC50: 2.2 mM, 5 mM, 90% inhibition in presence of Mg2+, 59% inhibition in absence of Mg2+
oleic acid
-
IC50: 0.082 mM
palmitoleic acid
-
IC50: 0.095 mM
phenanthridinone
-
5 mM, remaining activity: 35.1%
phenantridinone
i.e. 6(5H)-phenantridinone; i.e. 6(5H)-phenantridinone
phthalamide
-
IC50: 1.0 mM
Phthalazine
-
5 mM, 91% inhibition in presence of Mg2+, 79% inhibition in absence of Mg2+
PJ34
-
potent PARP inhibitor
Plumbagin
67% inhibition at 0.01 mM; 67% inhibition at 0.01 mM
Pyrazinamide
-
IC50: 0.13 mM
Quinazoline
-
5 mM, 63% inhibition in presence of Mg2+, 50% inhibition in absence of Mg2+
reserpine
-
IC50: 0.79 mM
thiobenzamide
-
IC50: 0.62 mM
Thionicotinamide
-
IC50: 1.8 mM
TIQ-A
i.e. 4H-thieno[2,3-c]isoquinolin-5-one; i.e. 4H-thieno[2,3-c]isoquinolin-5-one
trans-decahydro-1-naphthalenone
-
IC50: 4.3 mM
trimethylpsoralen
61% inhibition at 0.01 mM; 61% inhibition at 0.01 mM
vitamin K1
-
IC50: 0.0019 mM
vitamin K3
-
IC50: 0.42 mM
xanthurenic acid
-
5 mM, 88% inhibition in presence of Mg2+, 65% inhibition in absence of Mg2+
Zinc acetate
-
0.1 mM, remaining activity: 0.5%
1-methylnicotinamide chloride
-
IC50: 3.8 mM
1-methylnicotinamide chloride
-
IC50: 1.7 mM
2-Aminobenzamide
-
IC50: 0.65 mM
2-Aminobenzamide
-
IC50: 0.1 mM
3-aminobenzamide
-
IC50: 0.33 mM
3-aminobenzamide
-
IC50: 0.0054
3-aminobenzamide
-
1 mM, remaining activity: 3.9%
3-aminobenzamide
-
1 mM, 98% inhibition
3-aminobenzamide
-
1 mM, 99% inhibition
3-aminobenzamide
10 mM, 47% inhibition; 10 mM, 47% inhibition
3-Aminophthalhydrazide
-
IC50: 0.023 mM
3-Aminophthalhydrazide
-
0.1 mM, 98% inhibition of the 116000 Da enzyme
3-Hydroxybenzamide
-
IC50: 0.0091 mM
3-Hydroxybenzamide
-
0.1 mM, 89% inhibition of the 116000 Da enzyme
3-Methoxybenzamide
-
IC50: 0.017 mM
3-Methoxybenzamide
-
IC50: 0.0034 mM
3-Methoxybenzamide
-
0.01 mM, 85% inhibition of the 116000 Da enzyme, 84% inhibition of the 90000 Da enzyme; 1 mM, 96% inhibition of the 116000 Da enzyme, 95% inhibition of the 90000 Da enzyme
3-Methoxybenzamide
-
1 mM, 98% inhibition
4-Aminobenzamide
-
IC50: 1.8 mM
4-Aminobenzamide
-
IC50: 0.4 mM
4-hydroxybenzamide
-
IC50: 0.28 mM
4-hydroxybenzamide
27% inhibition at 0.01 mM
4-methoxybenzamide
-
IC50: 1.1 mM
4-[4-(1-aminoethenyl)phenoxy]benzamide
OUL35, potent inhibitor of ARTD10
4-[4-(1-aminoethenyl)phenoxy]benzamide
-
5-Methylnicotinamide
-
IC50: 0.35 mM
5-Methylnicotinamide
-
IC50: 0.07
5-Methylnicotinamide
Cryptothecodinium cohnii
-
0.15 mM, 31% inhibition
Benzamide
-
IC50: 0.22 mM
Benzamide
-
IC50: 0.0033 mM
Benzamide
Cryptothecodinium cohnii
-
0.15 mM, 48% inhibition
Caffeine
-
IC50: 1.4 mM
Caffeine
-
1 mM, 86% inhibition of the 116000 Da enzyme, 57% inhibition of the 90000 Da enzyme
Caffeine
-
1 mM, 23% inhibition
KCl
-
0.05 mM, remaining activity: 6.8%
KCl
-
100 mM, 85% inhibition of the 90000 Da enzyme
nicotinamide
-
IC50: 0.21 mM
nicotinamide
-
IC50: 0.031 mM
nicotinamide
-
0.05 mM, remaining activity: 27.3%
nicotinamide
Cryptothecodinium cohnii
-
0.15 mM, 25% inhibition
nicotinamide
-
1 mM, 96% inhibition of the 116000 Da enzyme, 95% inhibition of the 90000 Da enzyme
nicotinamide
-
1 mM, 91% inhibition
nicotinamide
-
1 mM, 93% inhibition
nicotinamide
10 mM, 14% inhibition; 10 mM, 14% inhibition
olaparib
i.e. 4-[(3-[(4-cyclopropylcarbonyl)piperazin-4-yl]carbonyl)-4-fluorophenyl]methyl(2H)phthalazin-1-one; i.e. 4-[(3-[(4-cyclopropylcarbonyl)piperazin-4-yl]carbonyl)-4-fluorophenyl]methyl(2H)phthalazin-1-one
Theobromine
-
IC50: 0.11 mM
Theobromine
-
1 mM, 76% inhibition
theophylline
-
IC50: 0.0046
theophylline
Cryptothecodinium cohnii
-
0.15 mM, 62% inhibition
theophylline
-
1 mM, 68% inhibition of the 116000 Da enzyme, 39% inhibition of the 90000 Da enzyme
theophylline
-
1 mM, 72% inhibition
thymidine
-
IC50: 0.18 mM
thymidine
Cryptothecodinium cohnii
-
0.15 mM, 39% inhibition
thymidine
-
1 mM, 94% inhibition of the 116000 Da enzyme, 88% inhibition of the 90000 Da enzyme
thymidine
-
1 mM, 70% inhibition
Zn2+
-
ZnCl2, IC50: 0.077 mM
Zn2+
0.5 mM, 47% inhibition; 0.5 mM, 50% inhibition
additional information
-
comparison of the effects of heterocyclic amines acting as potent carcinogens on PARP-1 and the arginine-specific mono-ADP-ribosyltransferase A, MART-A, EC 2.4.2.31, overview
-
additional information
-
PARP inhibitors promote ATM activation through induction of double strand breaks
-
additional information
-
identification of small molecule inhibitors of Pseudomonas aeruginosa exoenzyme S using a yeast phenotypic screening, overview
-
additional information
-
phenanthroline has no or a slightly activating effect
-
additional information
phenanthroline has no or a slightly activating effect
-
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0.02
(1E,4E)-1,5-di(pyridin-3-yl)penta-1,4-dien-3-one
Bordetella pertussis
at pH 7.5 and 25°C
0.0038
(2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanamide
Homo sapiens
pH and temperature not specified in the publication
0.012
1(2H)-phthalazinone
Bos taurus
-
IC50: 0.012 mM
2.8
1,2-benzopyrone
Bos taurus
-
IC50: 2.8 mM
2
1,3-benzodiazine
Bos taurus
-
IC50: 2.0 mM
1.3
1,3-dihydroxynaphthalene
Bos taurus
-
IC50: 1.3 mM
0.4
1,4-benzoquinone
Bos taurus
-
IC50: 0.4 mM
0.25
1,4-naphthalenedione
Bos taurus
-
IC50: 0.25 mM
0.00039
1,5-dihydroxyisoquinoline
Bos taurus
-
IC50: 0.00039 mM
0.0014
1,8-naphthalimide
Bos taurus
-
IC50: 0.0014 mM
1.3
1-hydroxy-2-methyl-4-aminonaphthalene
Bos taurus
-
IC50: 1.3 mM
0.007
1-hydroxyisoquinoline
Bos taurus
-
IC50: 0.007 mM
0.81
1-Indanone
Bos taurus
-
IC50: 0.81 mM
1.7 - 3.8
1-methylnicotinamide chloride
0.15
2,3-benzodiazine
Bos taurus
-
IC50: 0.15 mM
0.26
2,3-dichloro-1,4-naphthoquinone
Bos taurus
-
IC50: 0.26 mM
0.03
2,3-dihydro-1,4-phthalazinedione
Bos taurus
-
IC50: 0.03 mM
0.0081
2,4(1H,3H)-quinazolinedione
Bos taurus
-
IC50: 0.0081 mM
0.18
2,6-difluorobenzamide
Bos taurus
-
IC50: 0.18 mM
0.0524
2-(3-hydroxypropyl)-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-4-one
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.169
2-(3-hydroxypropyl)-5,6,7,8-tetrahydro[1]benzothieno[2,3-d]pyrimidin-4(3H)-one
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
1
2-acetamidobenzamide
Bos taurus
-
IC50: 1.0 mM
0.82
2-amino-3-chloro-1,4-naphthoquinone
Bos taurus
-
IC50: 0.82 mM
0.1 - 0.65
2-Aminobenzamide
2.9
2-bromobenzamide
Bos taurus
-
IC50: 2.9 mM
1
2-chlorobenzamide
Bos taurus
-
IC50: 1.0 mM
0.12
2-fluorobenzamide
Bos taurus
-
IC50: 0.12 mM
0.33
2-Hydroxy-1,4-naphthoquinone
Bos taurus
-
IC50: 0.33 mM
0.82
2-hydroxybenzamide
Bos taurus
-
IC50: 0.82 mM
0.044
2-mercapto-4(3H)-quinazolinone
Bos taurus
-
IC50: 0.044 mM
0.2
2-Methoxybenzamide
Bos taurus
-
IC50: 0.2 mM
0.045
2-methyl-1,4-benzopyrone
Bos taurus
-
IC50: 0.045 mM
0.42
2-methyl-1,4-naphthoquinone
Bos taurus
-
IC50: 0.42 mM
0.52
2-methyl-3-phytyl-1,4-naphthoquinone
Bos taurus
-
IC50: 0.52 mM
0.056
2-methyl-4(3H)-quinazolinone
Bos taurus
-
IC50: 0.056 mM
1.5
2-methylbenzamide
Bos taurus
-
IC50: 1.5 mM
0.045
2-methylchromone
Bos taurus
-
IC50: 0.045 mM
0.00035
2-nitro-6(5H)-phenanthridione
Bos taurus
-
IC50: 0.00035 mM
0.022
2-phenylchromone
Bos taurus
-
IC50: 0.022 mM
2.2
2-trichloromethyl-4(3H)-quinazolinone
Bos taurus
-
IC50: 2.2 mM
0.0003
2H-benz[c]isoquinolin-1-one
Bos taurus
-
IC50: 0.0003 mM
0.0014
2H-benz[de]isoquinoline-1,3-dione
Bos taurus
-
IC50: 0.0014 mM
0.31
3,4-dihydro-1(2H)-naphthalenone
Bos taurus
-
IC50: 0.31 mM
0.56
3,5-dibromosalicylamide
Bos taurus
-
IC50: 0.56 mM
1.2
3,5-dimethoxybenzamide
Bos taurus
-
IC50: 1.2 mM
2.5
3,5-dinitrobenzamide
Bos taurus
-
IC50: 2.5 mM
0.294
3-(4-methoxy-6,7-dihydro-5H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.0479
3-(4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.1
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-(pyridin-2-yl)ethyl]propanamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.0152
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-phenylethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0013
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-(pyridin-2-yl)ethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0009
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0022
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylpropyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0144
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(4-sulfamoylphenyl)ethyl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.135
3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.019
3-(4-oxo-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.12
3-(N,N-dimethylamino)benzamide
Bos taurus
-
IC50: 0.12 mM
0.012
3-Acetamidobenzamide
Bos taurus
-
IC50: 0.012 mM
2
3-acetamidosalicylamide
Bos taurus
-
IC50: 2.0 mM
0.22
3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole
Bos taurus
-
i.e. Trp-P-1, 94% inhibition at 5 mM, IC50: 0.22 mM
2.2
3-amino-1-methyl-5H-pyrido[4,3-b]indole
Bos taurus
-
i.e. Trp-P-2, 34% activation at 1 mM, 7% inhibition at 5 mM, IC50: 2.2 mM
0.0054 - 0.33
3-aminobenzamide
0.023
3-Aminophthalhydrazide
Bos taurus
-
IC50: 0.023 mM
0.055
3-bromobenzamide
Bos taurus
-
IC50: 0.055 mM
0.22
3-Chlorobenzamide
Bos taurus
-
IC50: 0.22 mM
0.2
3-Fluorobenzamide
Bos taurus
-
IC50: 0.2 mM
0.0091
3-Hydroxybenzamide
Bos taurus
-
IC50: 0.0091 mM
3.1
3-isobutyl-1-methylxanthine
Bos taurus
-
IC50: 3.1 mM
0.0034 - 0.017
3-Methoxybenzamide
0.19
3-Methylbenzamide
Bos taurus
-
IC50: 0.19 mM
0.16
3-nitrobenzamide
Bos taurus
-
IC50: 0.16 mM
0.072
3-nitrophthalhydrazide
Bos taurus
-
IC50: 0.072 mM
1.6
3-nitrosalicylamide
Bos taurus
-
IC50: 1.6 mM
0.0068
4,5,7,9-tetrahydro-2H-purine-2,8(3H)-dithione
Bordetella pertussis
at pH 7.5 and 25°C
0.19
4,8-dihydroxy-2-quinolinecarboxylic acid
Bos taurus
-
IC50: 0.19 mM
0.0017
4-(2-fluorophenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0019
4-(2-phenoxyethoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0013
4-(4-aminophenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00018
4-(4-carbamoylphenoxy)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00071
4-(4-formylphenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0018
4-(4-hydroxyphenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0014
4-(4-methoxyphenoxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0249
4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.0014
4-(benzyloxy)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00018
4-amino-1,8-naphthalimide
Bos taurus
-
IC50: 0.00018 mM
0.4 - 1.8
4-Aminobenzamide
0.29
4-aminophthalhydrazide
Bos taurus
-
IC50: 0.29 mM
2.2
4-bromobenzamide
Bos taurus
-
IC50: 2.2 mM
0.00072
4-butoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
0.0073
4-carbamoylphenyl benzoate
Homo sapiens
pH and temperature not specified in the publication
0.3
4-chlorobenzamide
Bos taurus
-
IC50: 0.3 mM
0.72
4-chromanone
Bos taurus
-
IC50: 0.72 mM
0.0035
4-ethoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
0.2
4-fluorobenzamide
Bos taurus
-
IC50: 0.2 mM
0.074
4-hydroxy-2-methylquinoline
Bos taurus
-
IC50: 0.074 mM
0.67
4-hydroxy-2-quinolinecarboxylic acid
Bos taurus
-
IC50: 0.67 mM
0.28
4-hydroxybenzamide
Bos taurus
-
IC50: 0.28 mM
0.57
4-Hydroxycoumarin
Bos taurus
-
IC50: 0.57 mM
2.3
4-hydroxypyridine
Bos taurus
-
IC50: 2.3 mM
0.0095
4-hydroxyquinazoline
Bos taurus
-
IC50: 0.0095 mM
0.08
4-hydroxyquinoline
Bos taurus
-
IC50: 0.08 mM
0.0028 - 1.1
4-methoxybenzamide
1.8
4-methylbenzamide
Bos taurus
-
IC50: 1.8 mM
0.003
4-nitro-7-[(1-oxo-1lambda(5)-pyridin-2-yl)sulfanyl]-2,1,3-benzoxadiazole
Bordetella pertussis
at pH 7.5 and 25°C
0.51
4-nitrophthalhydrazide
Bos taurus
-
IC50: 0.51 mM
0.0011
4-phenoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
0.0038
4-[(2-bromophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00023
4-[(2-fluorophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0045
4-[(3,5-dimethylphenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0022
4-[(3-bromophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0033
4-[(3-fluorophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0079
4-[(4-fluorophenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0093
4-[(4-methylphenyl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0014
4-[(naphthalen-1-yl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0013
4-[(propan-2-yl)oxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00135
4-[(pyridin-2-yl)methoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.000329 - 0.00033
4-[4-(1-aminoethenyl)phenoxy]benzamide
0.002
4-[[4-(aminocarbonyl)benzyl]oxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.006
4296-1011
Pseudomonas aeruginosa
-
pH 6.0, 30°C
0.045
5-acetamidosalicylamide
Bos taurus
-
IC50: 0.045 mM
0.1
5-aminosalicylamide
Bos taurus
-
IC50: 0.1 mM
0.015
5-bromodeoxyuridine
Bos taurus
-
IC50: 0.015 mM
0.16
5-Bromouracil
Bos taurus
-
IC50: 0.16 mM
0.21
5-Bromouridine
Bos taurus
-
IC50: 0.21 mM
0.19
5-chlorosalicylamide
Bos taurus
-
IC50: 0.19 mM
0.27
5-Chlorouracil
Bos taurus
-
IC50: 0.27 mM
0.25
5-hydroxy-1,4-naphthoquinone
Bos taurus
-
IC50: 0.25 mM
0.7
5-Hydroxy-2-methyl-1,4-naphthoquinone
Bos taurus
-
IC50: 0.7 mM
0.071
5-Iodouracil
Bos taurus
-
IC50: 0.071 mM
0.043
5-iodouridine
Bos taurus
-
IC50: 0.043 mM
0.07 - 0.35
5-Methylnicotinamide
0.29
5-methyluracil
Bos taurus
-
IC50: 0.29 mM
0.43
5-Nitrouracil
Bos taurus
-
IC50: 0.43 mM
0.0003
6(5H)-phenanthridinone
Bos taurus
-
IC50: 0.0003 mM
0.85
6-aminocoumarin
Bos taurus
-
IC50: 0.85 mM
1.1
6-aminonicotinamide
Bos taurus
-
IC50: 1.1 mM
1.4
8-acetamidocarsalam
Bos taurus
-
IC50: 1.4 mM
7.8
8-Methylnicotinamide
Bos taurus
-
IC50: 7.8 mM
2.3
acetophenone
Bos taurus
-
IC50: 2.3 mM
0.45
all-trans-retinal
Bos taurus
-
IC50: 0.45 mM
0.25
alpha-picolinamide
Bos taurus
-
IC50: 0.25 mM
0.0081
benzoyleneurea
Bos taurus
-
IC50: 0.0081 mM
1.4
Caffeine
Bos taurus
-
IC50: 1.4 mM
0.46
carbonylsalicylamide
Bos taurus
-
IC50: 0.46 mM
0.0085
Chlorthenoxazin
Bos taurus
-
IC50: 0.0085 mM
0.56
chromone-2-carboxylic acid
Bos taurus
-
IC50: 0.56 mM
0.62
cyclohexanecarboxamide
Bos taurus
-
IC50: 0.62 mM
0.003
diosmin
Pseudomonas aeruginosa
-
pH 6.0, 30°C
0.023
E216-5303
Pseudomonas aeruginosa
-
pH 6.0, 30°C
0.00118
EB-47
Homo sapiens
isoform ARDT10, pH and temperature not specified in the publication
0.021
everninic acid
Pseudomonas aeruginosa
-
pH 6.0, 30°C
0.022
flavone
Bos taurus
-
IC50: 0.022 mM
0.12
gamma-linolenic acid
Bos taurus
-
IC50: 0.12 mM
1.7
hypoxanthine
Bos taurus
-
IC50: 1.7 mM
0.99
Isonicotinamide
Bos taurus
-
IC50: 0.99 mM
4.8
Isonicotinate hydrazide
Bos taurus
-
IC50: 4.8 mM
0.048
linoleic acid
Bos taurus
-
IC50: 0.048 mM
0.11
linolenic acid
Bos taurus
-
IC50: 0.11 mM
0.93
m-acetamidoacetophenone
Bos taurus
-
IC50: 0.93 mM
1.9
m-aminoacetophenone
Bos taurus
-
IC50: 1.9 mM
0.6
m-hydroxyacetophenone
Bos taurus
-
IC50: 0.6 mM
0.05
m-phthalamide
Bos taurus
-
IC50: 0.05 mM
0.72
menadione sodium bisulfite
Bos taurus
-
IC50: 0.72 mM
0.0022
methyl (2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanoate
Homo sapiens
pH and temperature not specified in the publication
1.8
N-(2-chloroethyl)1,8-naphthalamide
Bos taurus
-
IC50: above 1.8 mM
0.0858
N-(acridin-9-yl)-4-nitrobenzamide
Aeromonas hydrophila
25°C, pH not specified in the publication
0.45
N-hydroxynaphthalimide sodium salt
Bos taurus
-
IC50: 0.45 mM
0.1
N-[(1R)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.1
N-[(1S)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.001
N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0096
N-[(2S)-1-hydroxybutan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0111
N-[(2S)-1-hydroxypropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0132
N-[1-[4-(1H-imidazol-1-yl)phenyl]ethyl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.086
N-[2-oxo-4-(phenylamino)-3,8a-dihydro-2H-chromen-3-yl]acetamide
Aeromonas hydrophila
25°C, pH not specified in the publication
0.031 - 0.21
nicotinamide
4.7
norharman
Bos taurus
-
IC50: 4.7 mM
2.2
novobiocin
Bos taurus
-
IC50: 2.2 mM, 5 mM, 90% inhibition in presence of Mg2+, 59% inhibition in absence of Mg2+
0.000925 - 0.00204
olaparib
0.082
oleic acid
Bos taurus
-
IC50: 0.082 mM
0.095
palmitoleic acid
Bos taurus
-
IC50: 0.095 mM
0.000745 - 0.00114
phenantridinone
1
phthalamide
Bos taurus
-
IC50: 1.0 mM
0.13
Pyrazinamide
Bos taurus
-
IC50: 0.13 mM
0.79
reserpine
Bos taurus
-
IC50: 0.79 mM
0.02
suramin
Aeromonas hydrophila
25°C, pH not specified in the publication
0.11
Theobromine
Bos taurus
-
IC50: 0.11 mM
0.046
theophylline
Bos taurus
-
IC50: 0.046 mM
0.62
thiobenzamide
Bos taurus
-
IC50: 0.62 mM
1.8
Thionicotinamide
Bos taurus
-
IC50: 1.8 mM
0.000232
TIQ-A
Homo sapiens
isoform ARDT7, pH and temperature not specified in the publication
4.3
trans-decahydro-1-naphthalenone
Bos taurus
-
IC50: 4.3 mM
0.157
V8 protease
Aeromonas hydrophila
25°C, pH not specified in the publication
-
0.0019
vitamin K1
Bos taurus
-
IC50: 0.0019 mM
0.42
vitamin K3
Bos taurus
-
IC50: 0.42 mM
0.077
Zn2+
Bos taurus
-
ZnCl2, IC50: 0.077 mM
1.7
1-methylnicotinamide chloride
Bos taurus
-
IC50: 1.7 mM
3.8
1-methylnicotinamide chloride
Bos taurus
-
IC50: 3.8 mM
0.1
2-Aminobenzamide
Bos taurus
-
IC50: 0.1 mM
0.65
2-Aminobenzamide
Bos taurus
-
IC50: 0.65 mM
0.0054
3-aminobenzamide
Bos taurus
-
IC50: 0.0054
0.33
3-aminobenzamide
Bos taurus
-
IC50: 0.33 mM
0.0034
3-Methoxybenzamide
Bos taurus
-
IC50: 0.0034 mM
0.017
3-Methoxybenzamide
Bos taurus
-
IC50: 0.017 mM
0.4
4-Aminobenzamide
Bos taurus
-
IC50: 0.4 mM
1.8
4-Aminobenzamide
Bos taurus
-
IC50: 1.8 mM
0.0028
4-methoxybenzamide
Homo sapiens
pH and temperature not specified in the publication
1.1
4-methoxybenzamide
Bos taurus
-
IC50: 1.1 mM
0.000329
4-[4-(1-aminoethenyl)phenoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.00033
4-[4-(1-aminoethenyl)phenoxy]benzamide
Homo sapiens
pH and temperature not specified in the publication
0.07
5-Methylnicotinamide
Bos taurus
-
IC50: 0.07 mM
0.35
5-Methylnicotinamide
Bos taurus
-
IC50: 0.35 mM
0.0033
Benzamide
Bos taurus
-
IC50: 0.0033 mM
0.22
Benzamide
Bos taurus
-
IC50: 0.22 mM
0.031
nicotinamide
Bos taurus
-
IC50: 0.031 mM
0.21
nicotinamide
Bos taurus
-
IC50: 0.21 mM
0.000925
olaparib
Homo sapiens
isoform ARDT7, pH and temperature not specified in the publication
0.00204
olaparib
Homo sapiens
isoform ARDT10, pH and temperature not specified in the publication
0.000745
phenantridinone
Homo sapiens
isoform ARDT10, pH and temperature not specified in the publication
0.00114
phenantridinone
Homo sapiens
isoform ARDT7, pH and temperature not specified in the publication
0.043
thymidine
Bos taurus
-
IC50: 0.043 mM
0.18
thymidine
Bos taurus
-
IC50: 0.18 mM
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E213A
kcat highly decreased compared to wild-type, Km similar to wild-type
E215A
kcat highly decreased compared to wild-type, Km (ADP-D-ribosyl)n-actin similar to wild-type, Km (NAD+) increased compared to wild-type
N86A
kcat moderately decreased compared to wild-type, Km decreased compared to wild-type
S178A
kcat decreased compared to wild-type, Km increased compared to wild-type
Y77A
kcat decreased compared to wild-type, Km increased compared to wild-type
Y82A
kcat decreased compared to wild-type, Km increased compared to wild-type
C19A
-
ADP-ribosyltransferase activity is 118% of the wild-type activity
E185Q
-
no ADP-ribosyltransferase activity
Q183E
-
no ADP-ribosyltransferase activity
R155E
-
ADP-ribosyltransferase activity is 0.2% of the wild-type activity
R59K
-
ADP-ribosyltransferase activity is 1.1% of the wild-type activity
R59K/R97K
-
no ADP-ribosyltransferase activity
R97K
-
ADP-ribosyltransferase activity is 1.9% of the wild-type activity
T178A
-
ADP-ribosyltransferase activity is 1.3% of the wild-type activity
T178A/Q183E
-
no ADP-ribosyltransferase activity
Y151V
-
ADP-ribosyltransferase activity is 1.6% of the wild-type activity
Y180T
-
no ADP-ribosyltransferase activity
C19A
-
ADP-ribosyltransferase activity is 118% of the wild-type activity
-
R155E
-
ADP-ribosyltransferase activity is 0.2% of the wild-type activity
-
R59K
-
ADP-ribosyltransferase activity is 1.1% of the wild-type activity
-
R59K/R97K
-
no ADP-ribosyltransferase activity
-
R97K
-
ADP-ribosyltransferase activity is 1.9% of the wild-type activity
-
D187A
-
catalytically inactive
E219Q
-
site-directed mutagenesis, inactive mutant
Q217E
-
site-directed mutagenesis, the point mutation alters the asparagine-specificity of the enzyme to an arginie-specificity, the mutant does not show ADP-ribosyltransferase activity towards RhoA, but is still capable of NAD-binding and possesses NAD+ glycohydrolase activity, the mutant exoenzyme C3 is capable of ADP-ribosylation of poly-arginine, but not poly-asparagine, and shows high activity with Arg residues of soybean trypsin inhibitor
R151A
-
site-directed mutagenesis, the mutation does not alter the enzyme activity or its potential as substrate for the C3 mutant Q217E
R61A
-
site-directed mutagenesis, the mutation does not alter the enzyme activity or its potential as substrate for the C3 mutant Q217E
R86A
-
site-directed mutagenesis, the mutation does not alter the enzyme activity but its potential as substrate for the C3 mutant Q217E, which cannot ADP-ribosylate this mutant
I163A
the enzyme shows wild type activity
DELTA106-288
-
mutant enzyme has NADase activity, lack of transferase activity
DELTA24288
-
signal sequences necessary for export from the ER (at the amino terminus) and addition of a GPI-anchor (at the carboxyl terminus) are deleted. The resulting mutants retain the catalytic properties of the mature wild-type ART1. Their NADase activities relative to transferase activities are very low, and nicotinamide release is enhanced in the presence of the ADP-ribose acceptor, agmatine
DELTA24293
-
signal sequences necessary for export from the ER (at the amino terminus) and addition of a GPI-anchor (at the carboxyl terminus) are deleted. The resulting mutants retain the catalytic properties of the mature wild-type ART1. Their NADase activities relative to transferase activities are very low, and nicotinamide release is enhanced in the presence of the ADP-ribose acceptor, agmatine
E111D
-
catalytic activity close to wild-type
E120D
-
catalytic activity highly decreased
A425K
-
site-directed mutagenesis, phenotypic analysis
D424A
-
site-directed mutagenesis, phenotypic analysis
D424A/D427A
-
site-directed mutagenesis, reduced interaction with 14-3-3, phenotypic analysis
D424A/L426A/D427A/L428A
-
site-directed mutagenesis, the mutant shows a highly reduced expression level, phenotypic analysis
D427A
-
site-directed mutagenesis, the mutant shows a reduced expression level, phenotypic analysis
DELTAN222/E381A
-
possesses 0.02% of the ADP-ribosyltransferase activity of DELTAN222. KM-value for (ADP-D-ribosyl)n-soybean-trypsin-inhibitor is 8.7fold higher than the KM-value for DELTAN222
DELTAN222/E381D
-
possesses 0.6% of the ADP-ribosyltransferase activity of DELTAN222. KM-value for (ADP-D-ribosyl)n-soybean-trypsin-inhibitor is 7.9fold higher than the KM-value for DELTAN222
DELTAN222/E381S
-
possesses 0.01% of the ADP-ribosyltransferase activity of DELTAN222. KM-value for (ADP-D-ribosyl)n-soybean-trypsin-inhibitor is 4.7fold higher than the KM-value for DELTAN222
DELTAN222/E387A
-
possesses 31% of the ADP-ribosyltransferase activity of DELTAN222
DELTAN222/E399A
-
possesses 28% of the ADP-ribosyltransferase activity of DELTAN222
DELTAN222/E414A
-
possesses 20% of the ADP-ribosyltransferase activity of DELTAN222
E379D
-
mutation inhibits expression of ADP-ribosyltransferase activity, but has little effect on the expression of NAD glycohydrolase activity
G421A
-
site-directed mutagenesis, phenotypic analysis
L422A
-
site-directed mutagenesis, phenotypic analysis
L423A
-
site-directed mutagenesis, phenotypic analysis
L426A
-
site-directed mutagenesis, phenotypic analysis
L426A/D427A
-
site-directed mutagenesis, the mutant shows a highly reduced expression level and slightly reduced cytotoxicity, no interaction with 14-3-3, phenotypic analysis
L426A/D427A/L428A
-
site-directed mutagenesis, the mutant shows a highly reduced expression level and cytotoxicity, no interaction with 14-3-3, phenotypic analysis
L428A
-
site-directed mutagenesis, reduced interaction with 14-3-3, the mutant shows highly reduced cytotoxicity, phenotypic analysis
Q420A
-
site-directed mutagenesis, phenotypic analysis
R146K
-
site-directed mutagenesis, the mutation within the active site for the RhoGAP domain
R146K/E379/381D
-
inactive mutant, does not inhibit Pseudomonas aeruginosa internalization into ExoS-transfected HeLa cells in contrast to the wild-type enzyme
S419I
-
site-directed mutagenesis, phenotypic analysis
Y426H
-
in native conformation, CRM66 shows limited ability to modify EF-2 covalently. Upon activation with urea and dithiothreitol CRM66 loses ADP-ribosylation activity entirely, yet it retains the ability to bind NAD+. Replacement of Tyr-426 with histidine in CRM66 completely restores cytotoxicity and ADP-ribosyltransferase activity
R146K
-
site-directed mutagenesis, the mutation within the active site for the RhoGAP domain
-
R146K/E379/381D
-
inactive mutant, does not inhibit Pseudomonas aeruginosa internalization into ExoS-transfected HeLa cells in contrast to the wild-type enzyme
-
E189A
-
about 5200fold decrease in NAD+ hydrolysis activity
E189I
-
20000fold decrease in NAD+ hydrolysis activity
E189S
-
about 5200fold decrease in NAD+ hydrolysis activity
Q187A/E189A
-
50000fold decrease in NAD+ hydrolysis activity
E118A
Tequatrovirus T4
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
E163A
Tequatrovirus T4
mutation reduces toxicity of ModA to a minor extent
E165A
Tequatrovirus T4
mutation in ModA reduces the toxicity to colony growth
E171A
Tequatrovirus T4
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
E173A
Tequatrovirus T4
mutation largly abolishes enzyme activity
F127A
Tequatrovirus T4
mutation in ModA reduces the toxicity to colony growth
I176A
Tequatrovirus T4
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
L71A
Tequatrovirus T4
mutation largly abolishes enzyme activity
N128A
Tequatrovirus T4
mutation reduces toxicity of ModA to a minor extent
N130A
Tequatrovirus T4
mutant enzyme with toxicity close to that of wild-type enzyme
Q116A
Tequatrovirus T4
mutation reduces toxicity of ModA to a minor extent
Q164A
Tequatrovirus T4
mutation reduces toxicity of ModA to a minor extent
Q172A
Tequatrovirus T4
mutant enzyme with toxicity close to that of wild-type enzyme
R72A
Tequatrovirus T4
mutation in ModA reduces the toxicity to colony growth
R73A
Tequatrovirus T4
mutation largly abolishes enzyme activity
S109A
Tequatrovirus T4
mutation in ModA reduces the toxicity to colony growth
S111A
Tequatrovirus T4
mutant enzyme with toxicity close to that of wild-type enzyme
Y131A
Tequatrovirus T4
mutation largly abolishes enzyme activity
E118A
Tequatrovirus T4 ModA
-
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
-
E173A
Tequatrovirus T4 ModA
-
mutation largly abolishes enzyme activity
-
Q116A
Tequatrovirus T4 ModA
-
mutation reduces toxicity of ModA to a minor extent
-
R72A
Tequatrovirus T4 ModA
-
mutation in ModA reduces the toxicity to colony growth
-
Y131A
Tequatrovirus T4 ModA
-
mutation largly abolishes enzyme activity
-
E118A
Tequatrovirus T4 ModB
-
mutation reduces the toxicity of the enzyme and still allows small colonies to grow
-
E173A
Tequatrovirus T4 ModB
-
mutation largly abolishes enzyme activity
-
Q116A
Tequatrovirus T4 ModB
-
mutation reduces toxicity of ModA to a minor extent
-
R72A
Tequatrovirus T4 ModB
-
mutation in ModA reduces the toxicity to colony growth
-
Y131A
Tequatrovirus T4 ModB
-
mutation largly abolishes enzyme activity
-
Q127D/E129D
the mutant shows drastically diminished activity compared to the wild type enzyme
Q127D/E129D
-
the mutant shows drastically diminished activity compared to the wild type enzyme
-
G888W
inactive
R7K
inactive
R7K
-
catalytic activity highly decreased
DELTAN222
-
carboxyl-terminal 222 amino acids of exoenzyme S, catalyzes the ADP-ribosylation of soybean trypsin inhibitor at a rate sixfold greater than rHisExoS. Relative to rHisExoS, DN222 has a similar affinity for NAD, a threefold greater affinity for soybean trypsin inhibitor, and a four- to eight-fold greater turnover number for the ADP-ribosylation of soybean trypsin inhibitor. DN222 does not chromatograph as an aggregate, which shows that the amino-terminal 99 amino acids of exoenzyme S are responsible for the aggregation phenotype
DELTAN222
-
the carboxy-terminal 222 amino acids, catalytic domain
E381D
-
mutant deficient in ADP-ribosyltransferase activity, possesses pI heterogeneity that is different than that of auto-ADP-ribosylated wild-type ExoS
E381D
-
mutation inhibits expression of both ADP-ribosyltransferase activity and NAD glycohydrolase activity
E381D
-
site-directed mutagenesis, the mutation within the active site for the ADPr domain
E381D
-
mutant deficient in ADP-ribosyltransferase activity, possesses pI heterogeneity that is different than that of auto-ADP-ribosylated wild-type ExoS
-
E381D
-
site-directed mutagenesis, the mutation within the active site for the ADPr domain
-
Q158A/E160A
the mutant shows reduced activity compared to the wild type enzyme
Q158A/E160A
-
the mutant shows reduced activity compared to the wild type enzyme
-
F129A
Tequatrovirus T4
mutation in ModA reduces the toxicity to colony growth
F129A
Tequatrovirus T4
mutation largly abolishes enzyme activity
additional information
-
phenotypes of isozyme-deficient mutant mice, overview
additional information
-
analysis of polymorphisms of PARP-1 promoter sequence in Parkinson patients, variations in the regulatory region are probably involved in increased risk for the disease, overview
additional information
-
stable expression of the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP, amino acids 1-547, in HEK-293 cells increases the expression of the enzyme
additional information
-
construction of parp-1-knockout mice
additional information
-
downregulatory effect of PARP-1 on the p53-dependent regulation of recombination between SV40 minichromosomes in primate cell lines conditionally expressing exogenous PARP-1 in a wild-type p53-positive or -negative background, respectively, overview
additional information
-
effects of ADP-ribosylation of integrin alpha7 on the expression of the monoclonal anti-integrin antibody 9EG7 epitope in intact differentiated C2C12 cells in presence or absene of NAD+ and Mn2+, overview
additional information
-
establishment of an immortalized PARP-1-/- murine endothelial cell line HYKO6 by transfection of primary cells with a plasmid containing the SV40 genome, expression of epitopes for detection by antibodies, phenotype, overview
additional information
-
knockout mice show increased inflammatory response in PARP-1 -/- compared to wild-type animals, characterized by neutrophil infiltration and increased IL-6 levels in broncho-alveolar lavages, the lesions are reversible, since the extent of the hyperplastic regions is reduced after 21 days of recovery and do not result in fibrosis, phenotype, overview
additional information
-
PARP-1 knockout mice are much less sensitive to inflammatory stress as a result of a diminished release of pro-inflammatory mediators, including nitric oxide, parp-1 knockout mice show reduced NO-induced oxidative injury and response to genotoxic damage during carcinogenesis and inflammation
additional information
-
PARP-1 knockout mice are viable, fertile and do not develop early onset tumors, cells isolated from these mice show an increased level of homologous recombination
additional information
-
phenotypes of isozyme-deficient mutant mice, overview
additional information
-
establishment of an immortalized PARP-1-/- murine endothelial cell line HYKO6 by transfection of primary cells with a plasmid containing the SV40 genome, expression of epitopes for detection by antibodies, phenotype, overview
-
additional information
-
knockout mice show increased inflammatory response in PARP-1 -/- compared to wild-type animals, characterized by neutrophil infiltration and increased IL-6 levels in broncho-alveolar lavages, the lesions are reversible, since the extent of the hyperplastic regions is reduced after 21 days of recovery and do not result in fibrosis, phenotype, overview
-
additional information
-
enzyme is comprised of an N-terminal domain with GTPase activating protein activity towards Rho family GTPases and a C-terminal ADP ribosyl-transferase (ADPRT) domain with minimal activity towards a synthetic substrate in vitro. Deletion of a majority of the ADPRT domain (residues 234 to 438) or point mutations of the ADPRT catalytic site (residues 383 to 385) leads to distinct changes in host cell morphology and substantially reduces the ability of ExoT to inhibit in vitro epithelial wound healing over a 24-h period. In contrast, only subtle effects on the efficiency of ExoT-induced bacterial internalization are observed in the ADPRT mutant forms
additional information
-
the recombinant deletion protein N223-53 which contains the catalytic domain of Exo53, comprising its 223 carboxyl-terminal residues catalyzes the FAS-dependent ADP-ribosylation of soybean trypsin inhibitor at 0.4% and of the Ras protein at 1.0% of the rates of catalysis by N222-49 (a protein comprising the 222 carboxyl-terminal residues of ExoS, which represent its catalytic domain). N223-53 possesesses binding affinities for NAD+ and SBTI similar to those of N222-49 but shows a lower rate for the ADP-ribosylation of SBTI
additional information
-
the recombinant deletion protein N223-53 which contains the catalytic domain of Exo53, comprising its 223 carboxyl-terminal residues catalyzes the FAS-dependent ADP-ribosylation of soybean trypsin inhibitor at 0.4% and of the Ras protein at 1.0% of the rates of catalysis by N222-49 (a protein comprising the 222 carboxyl-terminal residues of ExoS, which represent its catalytic domain). N223-53 possesesses binding affinities for NAD+ and SBTI similar to those of N222-49 but shows a lower velocity rate for the ADP-ribosylation of SBTI
additional information
-
construction of a truncated ExoS mutant DELTA51-72
additional information
-
construction of an enzyme-deficient strain 388DELTAexoS
additional information
-
construction of an enzyme-deficient strain 388DELTAexoS
-
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Drosophila melanogaster (P35875)
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Faraone Mennella, M.R.; Castellano, S.; De Luca, P.; Discenza, A.; Gambacorta, A.; Nicolaus, B.; Farina, B.
Comparison of the ADP-ribosylating thermozyme from Sulfolobus solfataricus and the mesophilic poly(ADP-ribose) polymerases
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Saccharolobus solfataricus, Saccharolobus solfataricus (B3EWG9), Saccharolobus solfataricus MT-4 / DSM 5833
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Faraone-Mennella, M.R.; Piccialli, G.; De Luca, P.; Castellano, S.; Giordano, A.; Rigano, D.; De Napoli, L.; Farina, B.
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Saccharolobus solfataricus (B3EWG9), Saccharolobus solfataricus MT-4 / DSM 5833 (B3EWG9)
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Simon, N.; Vergis, J.; Ebrahimi, A.; Ventura, C.; O'Brien, A.; Barbieri, J.
Host cell cytotoxicity and cytoskeleton disruption by CerADPr, an ADP-ribosyltransferase of Bacillus cereus G9241
Biochemistry
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Bacillus cereus, Bacillus cereus G9241
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Meyer-Ficca, M.L.; Ihara, M.; Bader, J.J.; Leu, N.A.; Beneke, S.; Meyer, R.G.
Spermatid head elongation with normal nuclear shaping requires ADP-ribosyltransferase PARP11 (ARTD11) in mice
Biol. Reprod.
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Homo sapiens
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Venkannagari, H.; Fallarero, A.; Feijs, K.L.; Luescher, B.; Lehtioe, L.
Activity-based assay for human mono-ADP-ribosyltransferases ARTD7/PARP15 and ARTD10/PARP10 aimed at screening and profiling inhibitors
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Homo sapiens (Q460N3), Homo sapiens (Q53GL7), Homo sapiens
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Picchianti, M.; Russo, C.; Castagnini, M.; Biagini, M.; Soldaini, E.; Balducci, E.
NAD-dependent ADP-ribosylation of the human antimicrobial and immune-modulatory peptide LL-37 by ADP-ribosyltransferase-1
Innate Immun.
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Homo sapiens (Q53GL7), Homo sapiens
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Nicolae, C.M.; Aho, E.R.; Vlahos, A.H.; Choe, K.N.; De, S.; Karras, G.I.; Moldovan, G.L.
The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell nuclear antigen (PCNA) and is required for DNA damage tolerance
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Homo sapiens (Q53GL7)
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Krska, D.; Ravulapalli, R.; Fieldhouse, R.J.; Lugo, M.R.; Merrill, A.R.
C3larvin toxin, an ADP-ribosyltransferase from Paenibacillus larvae
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Paenibacillus larvae subsp. larvae (W2E3J5), Paenibacillus larvae subsp. larvae BRL-230010 (W2E3J5)
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Lyons, B.; Ravulapalli, R.; Lanoue, J.; Lugo, M.R.; Dutta, D.; Carlin, S.; Merrill, A.R.
Scabin, a Novel DNA-acting ADP-ribosyltransferase from Streptomyces scabies
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Streptomyces scabiei (C9Z6T8), Streptomyces scabiei, Streptomyces scabiei 87.22 (C9Z6T8)
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Pinto, A.F.; Ebrahimi, M.; Saleeb, M.; Forsberg, A.; Elofsson, M.; Schueler, H.
Identification of inhibitors of Pseudomonas aeruginosa exotoxin-S ADP-ribosyltransferase activity
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Pseudomonas aeruginosa, Pseudomonas aeruginosa PAK
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Menzel, S.; Rissiek, B.; Bannas, P.; Jakoby, T.; Miksiewicz, M.; Schwarz, N.; Nissen, M.; Haag, F.; Tholey, A.; Koch-Nolte, F.
Nucleotide-induced membrane-proximal proteolysis controls the substrate specificity of T cell ecto-ADP-ribosyltransferase ARTC2.2
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Mus musculus
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Lindgren, A.E.; Karlberg, T.; Ekblad, T.; Spjut, S.; Thorsell, A.G.; Andersson, C.D.; Nhan, T.T.; Hellsten, V.; Weigelt, J.; Linusson, A.; Schueler, H.; Elofsson, M.
Chemical probes to study ADP-ribosylation: synthesis and biochemical evaluation of inhibitors of the human ADP-ribosyltransferase ARTD3/PARP3
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Homo sapiens (Q9Y6F1), Homo sapiens
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Liu, T.; Wei, Y.; Liu, G.; Shi, B.; Giovanni, S.; Peterson, J.W.; Chopra, A.K.
A mutated cholera toxin without the ADP-ribosyltransferase activity induces cytokine production and inhibits apoptosis of splenocytes in mice possibly via toll-like receptor-4 signaling
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Mus musculus
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Verheugd, P.; Forst, A.H.; Milke, L.; Herzog, N.; Feijs, K.L.; Kremmer, E.; Kleine, H.; Luescher, B.
Regulation of NF-kappaB signalling by the mono-ADP-ribosyltransferase ARTD10
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Homo sapiens (Q53GL7)
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MacPherson, L.; Tamblyn, L.; Rajendra, S.; Bralha, F.; McPherson, J.; Matthews, J.
2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP, ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon receptor transactivation
Nucleic Acids Res.
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Homo sapiens (Q7Z3E1)
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Valeri, M.; Zurli, V.; Ayala, I.; Colanzi, A.; Lapazio, L.; Corda, D.; Soriani, M.; Pizza, M.; Rossi Paccani, S.
The Neisseria meningitidis ADP-ribosyltransferase NarE enters human epithelial cells and disrupts epithelial monolayer integrity
PLoS ONE
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Neisseria meningitidis (Q9JZ10)
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Ashok, Y.; Miettinen, M.; Oliveira, D.K.H.; Tamirat, M.Z.; Naereoja, K.; Tiwari, A.; Hottiger, M.O.; Johnson, M.S.; Lehtioe, L.; Pulliainen, A.T.
Discovery of compounds inhibiting the ADP-ribosyltransferase activity of pertussis toxin
ACS Infect. Dis.
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Bordetella pertussis (P04977), Bordetella pertussis, Bordetella pertussis Tohama I (P04977)
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Asokanathan, C.; Tierney, S.; Ball, C.R.; Buckle, G.; Day, A.; Tanley, S.; Bristow, A.; Markey, K.; Xing, D.; Yuen, C.T.
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Bordetella pertussis
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Venkannagari, H.; Verheugd, P.; Koivunen, J.; Haikarainen, T.; Obaji, E.; Ashok, Y.; Narwal, M.; Pihlajaniemi, T.; Luescher, B.; Lehtioe, L.
Small-molecule chemical probe rescues cells from mono-ADP-ribosyltransferase ARTD10/PARP10-induced apoptosis and sensitizes cancer cells to DNA damage
Cell Chem. Biol.
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Homo sapiens (Q53GL7), Homo sapiens
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Murthy, S.; Desantis, J.; Verheugd, P.; Maksimainen, M.M.; Venkannagari, H.; Massari, S.; Ashok, Y.; Obaji, E.; Nkizinkinko, Y.; Luescher, B.; Tabarrini, O.; Lehtioe, L.
4-(Phenoxy) and 4-(benzyloxy)benzamides as potent and selective inhibitors of mono-ADP-ribosyltransferase PARP10/ARTD10
Eur. J. Med. Chem.
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Homo sapiens (Q53GL7), Homo sapiens
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Pollard, D.J.; Berger, C.N.; So, E.C.; Yu, L.; Hadavizadeh, K.; Jennings, P.; Tate, E.W.; Choudhary, J.S.; Frankel, G.
Broad-spectrum regulation of nonreceptor tyrosine kinases by the bacterial ADP-ribosyltransferase EspJ
mBio
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Citrobacter rodentium
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Guo, T.; Zuo, Y.; Qian, L.; Liu, J.; Yuan, Y.; Xu, K.; Miao, Y.; Feng, Q.; Chen, X.; Jin, L.; Zhang, L.; Dong, C.; Xiong, S.; Zheng, H.
ADP-ribosyltransferase PARP11 modulates the interferon antiviral response by mono-ADP-ribosylating the ubiquitin E3 ligase beta-TrCP
Nat. Microbiol.
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1872-1884
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Homo sapiens
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Dhoonmoon, A.; Schleicher, E.M.; Clements, K.E.; Nicolae, C.M.; Moldovan, G.L.
Genome-wide CRISPR synthetic lethality screen identifies a role for the ADP-ribosyltransferase PARP14 in DNA replication dynamics controlled by ATR
Nucleic Acids Res.
48
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2020
Homo sapiens
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Ost, G.S.; Wirth, C.; Bogdanovic, X.; Kao, W.C.; Schorch, B.; Aktories, P.J.K.; Papatheodorou, P.; Schwan, C.; Schlosser, A.; Jank, T.; Hunte, C.; Aktories, K.
Inverse control of Rab proteins by Yersinia ADP-ribosyltransferase and glycosyltransferase related to clostridial glucosylating toxins
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eaaz2094
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Yersinia mollaretii
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Lugo, M.R.; Merrill, A.R.
An in-silico sequence-structure-function analysis of the N-terminal lobe in CT group bacterial ADP-ribosyltransferase toxins
Toxins
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365
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Bacillus cereus (Q8KNY0), Staphylococcus aureus (Q9ADS9), Paenibacillus larvae subsp. larvae (W2E3J5), Paenibacillus larvae subsp. larvae DSM 25719 (W2E3J5)
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