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Results 1 - 10 of 170 > >>
EC Number
Substrates
Commentary Substrates
Organism
Products
Commentary (Products)
Reversibility
integrin alpha7 + NAD+
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
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
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integrin alpha7 + NAD+
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
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
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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
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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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the enzyme modifies eukaryotic 21000-24000 Da GTP-binding proteins
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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
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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
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raft association focuses ART2.2 on specific targets that constitutively or inducibly assoiate with lipid rafts
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ART1 is an arginine-specific transferase
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narE possesses ADP-ribosylating and NAD-glycohydrolase activities
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Results 1 - 10 of 170 > >>