ADPRHL2

ADPRHL2

ADP-ribosylhydrolase like 2, also known as ADPRHL2, is a human gene.cite web | title = Entrez Gene: ADPRHL2 ADP-ribosylhydrolase like 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54936| accessdate = ]

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References

Further reading

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*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Glowacki G, Braren R, Firner K, "et al." |title=The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse. |journal=Protein Sci. |volume=11 |issue= 7 |pages= 1657–70 |year= 2003 |pmid= 12070318 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Oka S, Kato J, Moss J |title=Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase. |journal=J. Biol. Chem. |volume=281 |issue= 2 |pages= 705–13 |year= 2006 |pmid= 16278211 |doi= 10.1074/jbc.M510290200
*cite journal | author=Kernstock S, Koch-Nolte F, Mueller-Dieckmann J, "et al." |title=Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase. |journal=Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |volume=62 |issue= Pt 3 |pages= 224–7 |year= 2006 |pmid= 16511307 |doi= 10.1107/S1744309106003435
*cite journal | author=Gregory SG, Barlow KF, McLay KE, "et al." |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727
*cite journal | author=Mueller-Dieckmann C, Kernstock S, Lisurek M, "et al." |title=The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=103 |issue= 41 |pages= 15026–31 |year= 2006 |pmid= 17015823 |doi= 10.1073/pnas.0606762103
*cite journal | author=Ono T, Kasamatsu A, Oka S, Moss J |title=The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=103 |issue= 45 |pages= 16687–91 |year= 2006 |pmid= 17075046 |doi= 10.1073/pnas.0607911103

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