메뉴 건너뛰기




Volumn 6, Issue 11, 2015, Pages 849-852

Molecular mechanism for the substrate recognition of USP7

Author keywords

[No Author keywords available]

Indexed keywords

DEUBIQUITINASE; DNA METHYLTRANSFERASE 1; HISTONE H2A; HISTONE H3; MINICHROMOSOME MAINTENANCE PROTEIN; PHOSPHATIDYLINOSITOL 3, 4, 5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN MDM2; PROTEIN P21; PROTEIN P53; SCAFFOLD PROTEIN; TRANSCRIPTION FACTOR FOXO; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR; UNCLASSIFIED DRUG; PROTEIN BINDING; UBIQUITIN THIOLESTERASE; USP7 PROTEIN, HUMAN;

EID: 84945472205     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-015-0192-y     Document Type: Letter
Times cited : (17)

References (10)
  • 1
    • 84874035038 scopus 로고    scopus 로고
    • Regulation of alphaherpesvirus infections by the ICP0 family of proteins
    • COI: 1:CAS:528:DC%2BC3sXltVyqsrs%3D, PID: 23239572
    • Boutell C, Everett RD (2013) Regulation of alphaherpesvirus infections by the ICP0 family of proteins. J Gen Virol 94:465–481
    • (2013) J Gen Virol , vol.94 , pp. 465-481
    • Boutell, C.1    Everett, R.D.2
  • 2
    • 84929178504 scopus 로고    scopus 로고
    • Molecular mechanism for USP7-mediated DNMT1 stabilization by acetylation
    • COI: 1:CAS:528:DC%2BC2MXhtF2ktrfP, PID: 25960197
    • Cheng J, Yang H, Fang J, Ma L, Gong R, Wang P, Li Z, Xu Y (2015) Molecular mechanism for USP7-mediated DNMT1 stabilization by acetylation. Nat Commun 6:7023
    • (2015) Nat Commun , vol.6 , pp. 7023
    • Cheng, J.1    Yang, H.2    Fang, J.3    Ma, L.4    Gong, R.5    Wang, P.6    Li, Z.7    Xu, Y.8
  • 3
    • 0032889557 scopus 로고    scopus 로고
    • The ability of herpes simplex virus type 1 immediate-early protein Vmw110 to bind to a ubiquitin-specific protease contributes to its roles in the activation of gene expression and stimulation of virus replication
    • COI: 1:CAS:528:DyaK1cXotFSksLo%3D, PID: 9847347
    • Everett RD, Meredith M, Orr A (1999) The ability of herpes simplex virus type 1 immediate-early protein Vmw110 to bind to a ubiquitin-specific protease contributes to its roles in the activation of gene expression and stimulation of virus replication. J Virol 73:417–426
    • (1999) J Virol , vol.73 , pp. 417-426
    • Everett, R.D.1    Meredith, M.2    Orr, A.3
  • 4
    • 80053594090 scopus 로고    scopus 로고
    • Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase
    • COI: 1:CAS:528:DC%2BC3MXht12gtrrE, PID: 21981925
    • Faesen AC, Dirac AM, Shanmugham A, Ovaa H, Perrakis A, Sixma TK (2011) Mechanism of USP7/HAUSP activation by its C-terminal ubiquitin-like domain and allosteric regulation by GMP-synthetase. Mol Cell 44:147–159
    • (2011) Mol Cell , vol.44 , pp. 147-159
    • Faesen, A.C.1    Dirac, A.M.2    Shanmugham, A.3    Ovaa, H.4    Perrakis, A.5    Sixma, T.K.6
  • 5
    • 84859475181 scopus 로고    scopus 로고
    • M phase phosphorylation of the epigenetic regulator UHRF1 regulates its physical association with the deubiquitylase USP7 and stability
    • COI: 1:CAS:528:DC%2BC38Xlt1agt70%3D, PID: 22411829
    • Ma H, Chen H, Guo X, Wang Z, Sowa ME, Zheng L, Hu S, Zeng P, Guo R, Diao J et al (2012) M phase phosphorylation of the epigenetic regulator UHRF1 regulates its physical association with the deubiquitylase USP7 and stability. Proc Natl Acad Sci USA 109:4828–4833
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 4828-4833
    • Ma, H.1    Chen, H.2    Guo, X.3    Wang, Z.4    Sowa, M.E.5    Zheng, L.6    Hu, S.7    Zeng, P.8    Guo, R.9    Diao, J.10
  • 6
    • 79955938866 scopus 로고    scopus 로고
    • The multifaceted roles of USP7: new therapeutic opportunities
    • COI: 1:CAS:528:DC%2BC3MXmtVGhs7k%3D, PID: 21468693
    • Nicholson B, Suresh Kumar KG (2011) The multifaceted roles of USP7: new therapeutic opportunities. Cell Biochem Biophys 60:61–68
    • (2011) Cell Biochem Biophys , vol.60 , pp. 61-68
    • Nicholson, B.1    Suresh Kumar, K.G.2
  • 7
    • 84923585238 scopus 로고    scopus 로고
    • Deubiquitinases and the new therapeutic opportunities offered to cancer
    • COI: 1:CAS:528:DC%2BC2MXkvFShtbY%3D, PID: 25605410
    • Pfoh R, Lacdao IK, Saridakis V (2015) Deubiquitinases and the new therapeutic opportunities offered to cancer. Endocr Relat Cancer 22:T35–54
    • (2015) Endocr Relat Cancer , vol.22 , pp. T35-T54
    • Pfoh, R.1    Lacdao, I.K.2    Saridakis, V.3
  • 8
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • COI: 1:CAS:528:DC%2BD1MXos1Ghtbc%3D, PID: 19489724
    • Reyes-Turcu FE, Ventii KH, Wilkinson KD (2009) Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu Rev Biochem 78:363–397
    • (2009) Annu Rev Biochem , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 10
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • COI: 1:CAS:528:DC%2BD1MXhtVSgtr3F, PID: 19615732
    • Sowa ME, Bennett EJ, Gygi SP, Harper JW (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138:389–403
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.