From Wikipedia, the free encyclopedia
Poly(ADP-ribose) glycohydrolase ARH3 is an enzyme that in humans is encoded by the ADPRHL2 gene.[1][2][3]
[edit] References
- ^ Glowacki G, Braren R, Firner K, Nissen M, Kuhl M, Reche P, Bazan F, Cetkovic-Cvrlje M, Leiter E, Haag F, Koch-Nolte F (Jun 2002). "The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse". Protein Sci 11 (7): 1657–1670. doi:10.1110/ps.0200602. PMC 2373659. PMID 12070318. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2373659.
- ^ Oka S, Kato J, Moss J (Jan 2006). "Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase". J Biol Chem 281 (2): 705–713. doi:10.1074/jbc.M510290200. PMID 16278211.
- ^ "Entrez Gene: ADPRHL2 ADP-ribosylhydrolase like 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54936.
[edit] Further reading
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Strausberg RL, Feingold EA, Grouse LH et al (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Ota T, Suzuki Y, Nishikawa T et al (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–45. doi:10.1038/ng1285. PMID 14702039.
- Gerhard DS, Wagner L, Feingold EA et al (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Kernstock S, Koch-Nolte F, Mueller-Dieckmann J et al (2006). "Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase". Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (Pt 3): 224–227. doi:10.1107/S1744309106003435. PMC 2197168. PMID 16511307. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2197168.
- Gregory SG, Barlow KF, McLay KE et al (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–321. doi:10.1038/nature04727. PMID 16710414.
- Mueller-Dieckmann C, Kernstock S, Lisurek M et al (2006). "The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation". Proc. Natl. Acad. Sci. U.S.A. 103 (41): 15026–15031. doi:10.1073/pnas.0606762103. PMC 1622773. PMID 17015823. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1622773.
- Ono T, Kasamatsu A, Oka S, Moss J (2006). "The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases". Proc. Natl. Acad. Sci. U.S.A. 103 (45): 16687–16691. doi:10.1073/pnas.0607911103. PMC 1636516. PMID 17075046. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1636516.
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PDB gallery
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2foz: human ADP-ribosylhydrolase 3
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2fp0: human ADP-ribosylhydrolase 3
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2g4k: Anomalous substructure of human ADP-ribosylhydrolase 3
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