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Information on EC 2.4.2.30 - NAD+ ADP-ribosyltransferase and Organism(s) Mus musculus
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2.4.2.30 NAD+ ADP-ribosyltransferaseIUBMB Comments
The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20--30 units.
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Word Map
- 2.4.2.30
-
polyadp-ribose
- caspase-3
- agonist
- bcl-2
- camp
- cyclase
- g-proteins
-
adp-ribosylation
- phospholipase
- ovarian
- necrosis
- endothelial
-
toxin-sensitive
- leukemia
- adenylate
- cholera
- cyclin
-
gtp-binding
- inositol
- bordetella
- guanine
-
annexin
- gtp
- erk
-
pro-apoptotic
-
anti-apoptotic
- mapks
- chromatin
-
apoptosis-inducing
- phosphoinositide
-
muscarinic
-
tunel
-
phorbol
-
adenylyl
- forskolin
-
receptor-mediated
-
protein-coupled
- pkc
-
heterotrimeric
-
caspase-dependent
-
acellular
-
forskolin-stimulated
- survivin
- aif
-
sub-g1
- xiap
- rad51
- carbachol
-
brca1/2
- molecular biology
- drug development
- pharmacology
- toxoid
- analysis
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
parp, pertussis toxin, parp-1, poly(adp-ribose) polymerase, parp1, poly (adp-ribose) polymerase, poly(adp-ribose) polymerase-1, c3 exoenzyme, adprt, exoenzyme s, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(adenosine diphosphoribose)transferase, nicotinamide adenine dinucleotide-protein
-
-
-
-
193-kDa vault protein
-
-
-
-
adenosine diphosphate ribosyltransferase
-
-
-
-
ADP-ribosyltransferase
ADP-ribosyltransferase (polymerizing)
-
-
-
-
ADPRT
-
-
-
-
C3 exoenzyme
-
-
-
-
exoenzyme C3
-
-
-
-
exoenzyme S
-
-
-
-
msPARP
-
-
-
-
NAD(+) ADP-ribosyltransferase
-
-
-
-
NAD+:ADP-ribosyltransferase (polymerizing)
-
-
-
-
NAD-protein ADP-ribosyltransferase
-
-
-
-
pADPRT
-
-
-
-
PARP
-
-
-
-
PARP-related/IalphaI-related H5/proline-rich
-
-
-
-
PH5P
-
-
-
-
poly(ADP-ribose) polymerase
poly(ADP-ribose) synthase
-
-
-
-
poly(ADP-ribose) transferase
-
-
-
-
poly(ADP-ribosyl)transferase
-
-
-
-
poly[ADP-ribose] synthetase
-
-
-
-
TANK1
-
-
-
-
TANK2
-
-
-
-
Tankyrase-like protein
-
-
-
-
Tankyrase-related protein
-
-
-
-
TRF1-interacting ankyrin-related ADP-ribose polymerase
-
-
-
-
VPARP
-
-
-
-
additional information
-
the enzyme belongs to the family of PARP-like poly(ADP-ribosyl)transferases, pARTs
ADP-ribosyltransferase
-
-
-
-
poly(ADP-ribose) polymerase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
mechanism and physiological function, overview
-
NAD+ + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the pART catalytic domain is found associated in Lego-like fashion with a variety of domains, including nucleic acid-binding, protein-protein interaction, and ubiquitylation domains
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
NAD+:poly(ADP-D-ribosyl)-acceptor ADP-D-ribosyl-transferase
The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20--30 units.
CAS REGISTRY NUMBER
COMMENTARY
58319-92-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NAD+ + (ADP-D-ribosyl)n-P2X7 ion channel
nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
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
-
-
?
NAD+ + p53
nicotinamide + (ADP-D-ribosyl)-p53
-
PARP-1 interacts with and poly(ADP-ribosyl)ates p53, which participates in DNA recombination
-
-
?
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
-
-
?
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-P2X7 ion channel
nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+
-
-
-
-
?
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
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
PARP inhibitors promote ATM activation through induction of double strand breaks
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
DNA binding by PARP-1 triggers its activity and it adds poly(ADP-ribose) polymers to itself and to surrounding histones, overview
-
additional information
-
PARP-1 is activated in response to DNA damage and participates in DNA repair, genomic integrity and cell death
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
PARP-1 in lung repair during recovery after hyperoxia, that is induced by 5-bromo-2-deoxyuridine, overview
-
transfectants expressing either ART2.2 with its native anchor (RT2.2-GPI) or ART2.2 with a grafted transmembrane anchor
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme loss induces higher levels of cytokine production and downregulates ex-vivo apoptosis of splenocytes
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PARP2_MOUSE
559
0
63397
Swiss-Prot
other Location (Reliability: 4)
PARP1_MOUSE
1013
0
113100
Swiss-Prot
other Location (Reliability: 3)
TNKS1_MOUSE
1320
0
140944
Swiss-Prot
Mitochondrion (Reliability: 3)
TNKS2_MOUSE
1166
0
126744
Swiss-Prot
other Location (Reliability: 5)
Q3TM68_MOUSE
1014
0
112696
TrEMBL
other Location (Reliability: 2)
Q3TIV3_MOUSE
1014
0
112711
TrEMBL
other Location (Reliability: 2)
Q3UJ03_MOUSE
1014
0
112708
TrEMBL
other Location (Reliability: 2)
Q3TF18_MOUSE
1014
0
112707
TrEMBL
other Location (Reliability: 2)
Q921K2_MOUSE
1014
0
112721
TrEMBL
other Location (Reliability: 2)
Q3TX36_MOUSE
1014
0
112794
TrEMBL
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
additional information
-
structural and functional organizations of PARP-1 and PARP-2, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PARP, DNA and amino acid sequence determination, exon compositions, phylogenetic analysis, identification of two subgroups of the family of PARP-like poly(ADP-ribosyl)transferases, depending on the active site residues, overview
-
gene parp-1, expression in LMV cells and subclones, derived from the parental line LLC-MK2 from rhesus monkey Macaca mulatta kidney, stably expressing the estradiol-inducible transcriptional transactivation factor Gal4ERVP
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
establishment of an immortalized PARP-1-/- murine endothelial cell line HYKO6 as a tool to study PARP-1-mediated endothelial cell dysfunction
molecular biology
-
establishment of an immortalized PARP-1-/- murine endothelial cell line HYKO6 as a tool to study PARP-1-mediated endothelial cell dysfunction
pharmacology
-
the enzyme inhibition is a possible tool in cancer therapy both in prophylactic and therapeutic treatment, e.g. by targeting BRCA2 tumors with PARP inhibitors, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bannas, P.; Adriouch, S.; Kahl, S.; Braasch, F.; Haag, F.; Koch-Nolte, F.
Activity and specificity of toxin-related mouse T cell ecto-ADP-ribosyltransferase ART2.2 depends on its association with lipid rafts
Blood
105
3663-3670
2005
Mus musculus
Bourgeois, C.; Okazaki, I.; Cavanaugh, E.; Nightingale, M.; Moss, J.
Identification of regulatory domains in ADP-ribosyltransferase-1 that determine transferase and NAD glycohydrolase activities
J. Biol. Chem.
278
26351-26355
2003
Mus musculus
Pagano, A.; Metrailler-Ruchonnet, I.; Aurrand-Lions, M.; Lucattelli, M.; Donati, Y.; Barazzone-Argiroffo, C.
Poly(ADP-ribose) polymerase-1 (PARP-1) controls lung cell proliferation and repair after hyperoxia-induced lung damage
Am. J. Physiol. Lung Cell Mol. Physiol.
293
L619-L629
2007
Mus musculus, Mus musculus Sv129
Zhao, Z.; Gruszczynska-Biegala, J.; Zolkiewska, A.
ADP-ribosylation of integrin alpha7 modulates the binding of integrin alpha7beta1 to laminin
Biochem. J.
385
309-317
2005
Mus musculus
Otto, H.; Reche, P.A.; Bazan, F.; Dittmar, K.; Haag, F.; Koch-Nolte, F.
In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)
BMC Genomics
6
139
2005
Mus musculus, Homo sapiens (O95271), Homo sapiens (P09874), Homo sapiens (Q2NL67), Homo sapiens (Q460N5), Homo sapiens (Q8N5Y8), Homo sapiens (Q9NR21), Homo sapiens (Q9UGN5), Homo sapiens (Q9UKK3), Homo sapiens (Q9Y6F1)
Aguilar-Quesada, R.; Munoz-Gamez, J.A.; Martin-Oliva, D.; Peralta, A.; Valenzuela, M.T.; Matinez-Romero, R.; Quiles-Perez, R.; Menissier-de Murcia, J.; de Murcia, G.; de Almodovar, M.R.; Oliver, F.J.
Interaction between ATM and PARP-1 in response to DNA damage and sensitization of ATM deficient cells through PARP inhibition
BMC Mol. Biol.
8
29
2007
Mus musculus
Helleday, T.; Bryant, H.E.; Schultz, N.
Poly(ADP-ribose) polymerase (PARP-1) in homologous recombination and as a target for cancer therapy
Cell Cycle
4
1176-1178
2005
Mus musculus
Kim, M.Y.; Zhang, T.; Kraus, W.L.
Poly(ADP-ribosyl)ation by PARP-1: PAR-laying NAD+ into a nuclear signal
Genes Dev.
19
1951-1967
2005
Drosophila melanogaster, Mus musculus
Carrillo, A.; Monreal, Y.; Ramirez, P.; Suarez, E.; Parrilla, P.; Menissier-de Murcia, J.; de Murcia, G.; Alvarez-Vallina, L.; Yelamos, J.
Establishment of an immortalized PARP-1-/- murine endothelial cell line: a new tool to study PARP-1 mediated endothelial cell dysfunction
J. Cell. Biochem.
94
1163-1174
2005
Mus musculus, Mus musculus 129/Sv x C57BL/6
Siles, E.; Martinez-Lara, E.; Nunez, M.I.; Munoz-Gamez, J.A.; Martin-Oliva, D.; Valenzuela, M.T.; Peinado, M.A.; Ruiz de Almodovar, J.M.; Javier Oliver, F.
PARP-1-dependent 3-nitrotyrosine protein modification after DNA damage
J. Cell. Biochem.
96
709-715
2005
Mus musculus
Baumann, C.; Boehden, G.S.; Buerkle, A.; Wiesmueller, L.
Poly(ADP-RIBOSE) polymerase-1 (Parp-1) antagonizes topoisomerase I-dependent recombination stimulation by P53
Nucleic Acids Res.
34
1036-1049
2006
Mus musculus
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
J. Immunol.
195
2057-2066
2015
Mus musculus
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
Mol. Immunol.
75
21-27
2016
Mus musculus
EXTERNAL LINKS (specific for EC-Number 2.4.2.30)
Transporter Classification Database (TCDB): 1.I.1.1.3
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