메뉴 건너뛰기




Volumn 111, Issue 23, 2014, Pages 8434-8439

Pivotal role for the ubiquitin Y59-E51 loop in lysine 48 polyubiquitination

Author keywords

E2 ubiquitin conjugating enzyme; E3 ubiquitin ligase; Receptor ubiquitin

Indexed keywords

CDC34 ENZYME; LYSINE; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN Y59 E51; UNCLASSIFIED DRUG;

EID: 84902143589     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1407849111     Document Type: Article
Times cited : (26)

References (12)
  • 3
    • 77949548466 scopus 로고    scopus 로고
    • Priming and extending: A UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate
    • Wu K, Kovacev J, Pan Z-Q (2010) Priming and extending: A UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate. Mol Cell 37(6):784-796.
    • (2010) Mol Cell , vol.37 , Issue.6 , pp. 784-796
    • Wu, K.1    Kovacev, J.2    Pan, Z.-Q.3
  • 4
    • 35148869981 scopus 로고    scopus 로고
    • Human Cdc34 employs distinct sites to coordinate attachment of ubiquitin to a substrate and assembly of polyubiquitin chains
    • DOI 10.1128/MCB.00812-07
    • Gazdoiu S, Yamoah K, Wu K, Pan Z-Q (2007) Human Cdc34 employs distinct sites to coordinate attachment of ubiquitin to a substrate and assembly of polyubiquitin chains. Mol Cell Biol 27(20):7041-7052. (Pubitemid 47549743)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.20 , pp. 7041-7052
    • Gazdoiu, S.1    Yamoah, K.2    Wu, K.3    Pan, Z.-Q.4
  • 5
    • 84889047749 scopus 로고    scopus 로고
    • Multimodal mechanism of action for the Cdc34 acidic loop: A case study for why ubiquitin-conjugating enzymes have loops and tails
    • Ziemba A, et al. (2013) Multimodal mechanism of action for the Cdc34 acidic loop: A case study for why ubiquitin-conjugating enzymes have loops and tails. J Biol Chem 288(48):34882-34896.
    • (2013) J Biol Chem , vol.288 , Issue.48 , pp. 34882-34896
    • Ziemba, A.1
  • 6
    • 0026734774 scopus 로고
    • Iodination of tyrosine 59 of ubiquitin selectively blocks ubiquitin's acceptor activity in diubiquitin synthesis catalyzed by E2(25K)
    • Pickart CM, Haldeman MT, Kasperek EM, Chen Z (1992) Iodination of tyrosine 59 of ubiquitin selectively blocks ubiquitin's acceptor activity in diubiquitin synthesis catalyzed by E2(25K). J Biol Chem 267(20):14418-14423.
    • (1992) J Biol Chem , vol.267 , Issue.20 , pp. 14418-14423
    • Pickart, C.M.1    Haldeman, M.T.2    Kasperek, E.M.3    Chen, Z.4
  • 7
    • 77955990685 scopus 로고    scopus 로고
    • Catalysis of lysine 48-specific ubiquitin chain assembly by residues in E2 and ubiquitin
    • Rodrigo-Brenni MC, Foster SA, Morgan DO (2010) Catalysis of lysine 48-specific ubiquitin chain assembly by residues in E2 and ubiquitin. Mol Cell 39(4):548-559.
    • (2010) Mol Cell , vol.39 , Issue.4 , pp. 548-559
    • Rodrigo-Brenni, M.C.1    Foster, S.A.2    Morgan, D.O.3
  • 8
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 A resolution
    • Vijay-Kumar S, Bugg CE, Cook WJ (1987) Structure of ubiquitin refined at 1.8 A resolution. J Mol Biol 194(3):531-544.
    • (1987) J Mol Biol , vol.194 , Issue.3 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 9
    • 84896639811 scopus 로고    scopus 로고
    • E2 enzyme inhibition by stabilization of a low-affinity interface with ubiquitin
    • Huang H, et al. (2014) E2 enzyme inhibition by stabilization of a low-affinity interface with ubiquitin. Nat Chem Biol 10(2):156-163.
    • (2014) Nat Chem Biol , vol.10 , Issue.2 , pp. 156-163
    • Huang, H.1
  • 10
    • 84865781586 scopus 로고    scopus 로고
    • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
    • Plechanovová A, Jaffray EG, Tatham MH, Naismith JH, Hay RT (2012) Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489(7414):115-120.
    • (2012) Nature , vol.489 , Issue.7414 , pp. 115-120
    • Plechanovová, A.1    Jaffray, E.G.2    Tatham, M.H.3    Naismith, J.H.4    Hay, R.T.5
  • 11
    • 70350015537 scopus 로고    scopus 로고
    • A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1β
    • Xu M, Skaug B, Zeng W, Chen ZJ (2009) A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1β. Mol Cell 36(2):302-314.
    • (2009) Mol Cell , vol.36 , Issue.2 , pp. 302-314
    • Xu, M.1    Skaug, B.2    Zeng, W.3    Chen, Z.J.4
  • 12
    • 84875703570 scopus 로고    scopus 로고
    • Analyses of the effects of all ubiquitin point mutants on yeast growth rate
    • Roscoe BP, Thayer KM, Zeldovich KB, Fushman D, Bolon DNA (2013) Analyses of the effects of all ubiquitin point mutants on yeast growth rate. J Mol Biol 425(8):1363-1377.
    • (2013) J Mol Biol , vol.425 , Issue.8 , pp. 1363-1377
    • Roscoe, B.P.1    Thayer, K.M.2    Zeldovich, K.B.3    Fushman, D.4    Bolon, D.N.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.