ERCC8 (gene)

ERCC8 (gene)

Excision repair cross-complementing rodent repair deficiency, complementation group 8, also known as ERCC8, is a human gene.cite web | title = Entrez Gene: ERCC8 excision repair cross-complementing rodent repair deficiency, complementation group 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1161| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a WD repeat protein, which interacts with Cockayne syndrome type B (CSB) protein and with p44 protein, a subunit of the RNA polymerase II transcription factor IIH. Mutations in this gene have been identified in patients with hereditary disease Cockayne syndrome (CS). The CS cells are abnormally sensitive to ultraviolet radiation and are defective in the repair of transcriptionally active genes. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.cite web | title = Entrez Gene: ERCC8 excision repair cross-complementing rodent repair deficiency, complementation group 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1161| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=van Gool AJ, van der Horst GT, Citterio E, Hoeijmakers JH |title=Cockayne syndrome: defective repair of transcription? |journal=EMBO J. |volume=16 |issue= 14 |pages= 4155–62 |year= 1997 |pmid= 9250659 |doi=
*cite journal | author=Henning KA, Li L, Iyer N, "et al." |title=The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH. |journal=Cell |volume=82 |issue= 4 |pages= 555–64 |year= 1995 |pmid= 7664335 |doi=
*cite journal | author=Itoh T, Shiomi T, Shiomi N, "et al." |title=Rodent complementation group 8 (ERCC8) corresponds to Cockayne syndrome complementation group A. |journal=Mutat. Res. |volume=362 |issue= 2 |pages= 167–74 |year= 1996 |pmid= 8596535 |doi=
*cite journal | author=Bregman DB, Halaban R, van Gool AJ, "et al." |title=UV-induced ubiquitination of RNA polymerase II: a novel modification deficient in Cockayne syndrome cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 21 |pages= 11586–90 |year= 1996 |pmid= 8876179 |doi=
*cite journal | author=Selby CP, Sancar A |title=Human transcription-repair coupling factor CSB/ERCC6 is a DNA-stimulated ATPase but is not a helicase and does not disrupt the ternary transcription complex of stalled RNA polymerase II. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1885–90 |year= 1997 |pmid= 8999876 |doi=
*cite journal | author=Nakatsu Y, Asahina H, Citterio E, "et al." |title=XAB2, a novel tetratricopeptide repeat protein involved in transcription-coupled DNA repair and transcription. |journal=J. Biol. Chem. |volume=275 |issue= 45 |pages= 34931–7 |year= 2001 |pmid= 10944529 |doi= 10.1074/jbc.M004936200
*cite journal | author=Kamiuchi S, Saijo M, Citterio E, "et al." |title=Translocation of Cockayne syndrome group A protein to the nuclear matrix: possible relevance to transcription-coupled DNA repair. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 1 |pages= 201–6 |year= 2002 |pmid= 11782547 |doi= 10.1073/pnas.012473199
*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=Groisman R, Polanowska J, Kuraoka I, "et al." |title=The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. |journal=Cell |volume=113 |issue= 3 |pages= 357–67 |year= 2003 |pmid= 12732143 |doi=
*cite journal | author=Cao H, Williams C, Carter M, Hegele RA |title=CKN1 (MIM 216400): mutations in Cockayne syndrome type A and a new common polymorphism. |journal=J. Hum. Genet. |volume=49 |issue= 1 |pages= 61–3 |year= 2004 |pmid= 14661080 |doi= 10.1007/s10038-003-0107-2
*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=Ridley AJ, Colley J, Wynford-Thomas D, Jones CJ |title=Characterisation of novel mutations in Cockayne syndrome type A and xeroderma pigmentosum group C subjects. |journal=J. Hum. Genet. |volume=50 |issue= 3 |pages= 151–4 |year= 2005 |pmid= 15744458 |doi= 10.1007/s10038-004-0228-2
*cite journal | author=Sarker AH, Tsutakawa SE, Kostek S, "et al." |title=Recognition of RNA polymerase II and transcription bubbles by XPG, CSB, and TFIIH: insights for transcription-coupled repair and Cockayne Syndrome. |journal=Mol. Cell |volume=20 |issue= 2 |pages= 187–98 |year= 2006 |pmid= 16246722 |doi= 10.1016/j.molcel.2005.09.022
*cite journal | author=Groisman R, Kuraoka I, Chevallier O, "et al." |title=CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome. |journal=Genes Dev. |volume=20 |issue= 11 |pages= 1429–34 |year= 2006 |pmid= 16751180 |doi= 10.1101/gad.378206
*cite journal | author=Fousteri M, Vermeulen W, van Zeeland AA, Mullenders LH |title=Cockayne syndrome A and B proteins differentially regulate recruitment of chromatin remodeling and repair factors to stalled RNA polymerase II in vivo. |journal=Mol. Cell |volume=23 |issue= 4 |pages= 471–82 |year= 2006 |pmid= 16916636 |doi= 10.1016/j.molcel.2006.06.029
*cite journal | author=Saijo M, Hirai T, Ogawa A, "et al." |title=Functional TFIIH is required for UV-induced translocation of CSA to the nuclear matrix. |journal=Mol. Cell. Biol. |volume=27 |issue= 7 |pages= 2538–47 |year= 2007 |pmid= 17242193 |doi= 10.1128/MCB.01288-06
*cite journal | author=D'Errico M, Parlanti E, Teson M, "et al." |title=The role of CSA in the response to oxidative DNA damage in human cells. |journal=Oncogene |volume=26 |issue= 30 |pages= 4336–43 |year= 2007 |pmid= 17297471 |doi= 10.1038/sj.onc.1210232

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