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Volumn 312, Issue 4, 2001, Pages 675-685

The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9

Author keywords

Cdk9; Phosphorylation; Pin1; RNA polymerase II; Spt5

Indexed keywords

CYCLIN DEPENDENT KINASE; ISOMERASE; PEPTIDYL PROLYL ISOMERASE PIN 1; PROTEIN HSPT 5; PROTEIN SPT 5; RECOMBINANT PROTEIN; RNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 0035965126     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4991     Document Type: Article
Times cited : (51)

References (48)
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  • 11
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    • Inhibitors of transcription such as 5,6-dichloro-1-β-D-ribofuranosyl benzimidazole (DRB) and isoquinoline sulfonamide derivatives (H-8 and H-7*), promote the dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II largest subunit
    • (1994) J. Biol. Chem. , vol.269 , pp. 13331-13336
    • Dubois, M.F.1    Nguyen, V.T.2    Bellier, S.3    Bensaude, O.4
  • 24
    • 0032771752 scopus 로고    scopus 로고
    • A hyperphosphorylated form of RNA polymerase II is the major interphase antigen of the phosphoprotein antibody MPM-2 and interacts with the peptidyl-prolyl isomerase Pin1
    • (1999) J. Cell Sci. , vol.112 , pp. 2493-2500
    • Albert, A.1    Lavoie, S.2    Vincent, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.