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유전체항상성연구단
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Repair, Removal, and Shutdown: It All Hinges on RNA Polymerase II Ubiquitylation

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dc.contributor.authorKook Son-
dc.contributor.authorOrlando D. Scha¨ rer-
dc.date.available2020-07-06T06:43:29Z-
dc.date.created2020-04-20-
dc.date.issued2020-03-
dc.identifier.issn0092-8674-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/7160-
dc.description.abstract© 2020 Elsevier Inc.Two papers, by Nakazawa and Vidaković, show how ubiquitylation of a single lysine residue in RNA polymerase II serves as a master switch to regulate transcription, RNA polymerase II degradation, and transcription-coupled nucleotide excision repair in response to DNA damage. © 2020 Elsevier Inc.Two papers, by Nakazawa and Vidaković, show how ubiquitylation of a single lysine residue in RNA polymerase II serves as a master switch to regulate transcription, RNA polymerase II degradation, and transcription-coupled nucleotide excision repair in response to DNA damage-
dc.description.uri1-
dc.language영어-
dc.publisherCELL PRESS-
dc.titleRepair, Removal, and Shutdown: It All Hinges on RNA Polymerase II Ubiquitylation-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000520925300004-
dc.identifier.scopusid2-s2.0-85081687048-
dc.identifier.rimsid71709-
dc.contributor.affiliatedAuthorKook Son-
dc.contributor.affiliatedAuthorOrlando D. Scha¨ rer-
dc.identifier.doi10.1016/j.cell.2020.02.053-
dc.identifier.bibliographicCitationCELL, v.180, no.6, pp.1039 - 1041-
dc.citation.titleCELL-
dc.citation.volume180-
dc.citation.number6-
dc.citation.startPage1039-
dc.citation.endPage1041-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
Appears in Collections:
Center for Genomic Integrity(유전체 항상성 연구단) > 1. Journal Papers (저널논문)
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