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This family has three members in humans (ARH1-3): ARH1, also termed [Protein ADP-ribosylarginine] hydrolase, cleaves ADP-ribose-L-arginine, ARH2, which is predicted to be enzymatically inactive, and ARH3, which cleaves primarily ADP-ribose-L-serine, but was shown to also hydrolyse poly(ADP-ribose), 1''-O-acetyl-ADP-ribose and alpha-nicotinamide adenine dinucleotide.
In enzymology, an ADP—thymidine kinase (EC 2.7.1.118) is an enzyme that catalyzes the chemical reaction ADP + thymidine ⇌ {\displaystyle \rightleftharpoons } AMP + thymidine 5'-phosphate Thus, the two substrates of this enzyme are ADP and thymidine , whereas its two products are AMP and thymidine 5'-phosphate .
ADP-ribosylation is the addition of one or more ADP-ribose moieties to a protein. [1] [2] It is a reversible post-translational modification that is involved in many cellular processes, including cell signaling, DNA repair, gene regulation and apoptosis. [3] [4] Improper ADP-ribosylation has been implicated in some forms of cancer. [5]
ADP (company), an American provider of human resources management software and services; AdP, a German self-help organisation for patients who have undergone pancreatectomy; Association of Directory Publishers, an international trade organization for print and online directory publishers
Agua del Pueblo (AdP) is a private, non-profit, non-denominational and Guatemalan organization.AdP has completed more than 500 integrated rural water, sanitation, and community development projects serving more than 1,000 communities and their 500,000 Guatemalan residents.
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(ADP-ribosyl)hydrolase 3 (ARH3) is an enzyme that in humans is encoded by the ADPRHL2 gene (also called ADPRS). This enzyme reverses the proteins’ post-translational addition of ADP-ribose to serine residues as part of the DNA damage response The enzyme is also known to cleave poly(ADP-ribose) polymers, 1''-O-acetyl-ADP-ribose and alpha-NAD +
Function. ADP-ribosylation factor 3 (ARF3) is a member of the human ARF gene family. These genes encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D.