메뉴 건너뛰기




Volumn 26, Issue 6, 2007, Pages 891-898

E3-Independent Monoubiquitination of Ubiquitin-Binding Proteins

Author keywords

PROTEINS

Indexed keywords

BINDING PROTEIN; PROTEIN NFZ; PROTEIN UBA; PROTEIN UBM; PROTEIN UBZ; PROTEIN UIM; SMALL INTERFERING RNA; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 34250375116     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2007.05.014     Document Type: Article
Times cited : (135)

References (24)
  • 1
    • 0029741379 scopus 로고    scopus 로고
    • Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin
    • Bastiaens P.I., Majoul I.V., Verveer P.J., Soling H.D., and Jovin T.M. Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin. EMBO J. 15 (1996) 4246-4253
    • (1996) EMBO J. , vol.15 , pp. 4246-4253
    • Bastiaens, P.I.1    Majoul, I.V.2    Verveer, P.J.3    Soling, H.D.4    Jovin, T.M.5
  • 4
    • 0038362292 scopus 로고    scopus 로고
    • When ubiquitin meets ubiquitin receptors: a signalling connection
    • Di Fiore P.P., Polo S., and Hofmann K. When ubiquitin meets ubiquitin receptors: a signalling connection. Nat. Rev. Mol. Cell Biol. 4 (2003) 491-497
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 491-497
    • Di Fiore, P.P.1    Polo, S.2    Hofmann, K.3
  • 6
    • 27144529182 scopus 로고    scopus 로고
    • Ubiquitylation and cell signaling
    • Haglund K., and Dikic I. Ubiquitylation and cell signaling. EMBO J. 24 (2005) 3353-3359
    • (2005) EMBO J. , vol.24 , pp. 3353-3359
    • Haglund, K.1    Dikic, I.2
  • 7
    • 33646064427 scopus 로고    scopus 로고
    • Structural complexity in ubiquitin recognition
    • Harper W., and Schulman B.A. Structural complexity in ubiquitin recognition. Cell 124 (2006) 1133-1136
    • (2006) Cell , vol.124 , pp. 1133-1136
    • Harper, W.1    Schulman, B.A.2
  • 12
    • 33750555919 scopus 로고    scopus 로고
    • Ubiquitin-binding domains
    • Hurley J.H., Lee S., and Prag G. Ubiquitin-binding domains. Biochem. J. 399 (2006) 361-372
    • (2006) Biochem. J. , vol.399 , pp. 361-372
    • Hurley, J.H.1    Lee, S.2    Prag, G.3
  • 13
    • 18544383164 scopus 로고    scopus 로고
    • Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4
    • Katz M., Shtiegman K., Tal-Or P., Yakir L., Mosesson Y., Harari D., Machluf Y., Asao H., Jovin T., Sugamura K., and Yarden Y. Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4. Traffic 3 (2002) 740-751
    • (2002) Traffic , vol.3 , pp. 740-751
    • Katz, M.1    Shtiegman, K.2    Tal-Or, P.3    Yakir, L.4    Mosesson, Y.5    Harari, D.6    Machluf, Y.7    Asao, H.8    Jovin, T.9    Sugamura, K.10    Yarden, Y.11
  • 14
    • 3242878438 scopus 로고    scopus 로고
    • Analysis of the role of ubiquitin-interacting motifs in ubiquitin binding and ubiquitylation
    • Miller S.L., Malotky E., and O'Bryan J.P. Analysis of the role of ubiquitin-interacting motifs in ubiquitin binding and ubiquitylation. J. Biol. Chem. 279 (2004) 33528-33537
    • (2004) J. Biol. Chem. , vol.279 , pp. 33528-33537
    • Miller, S.L.1    Malotky, E.2    O'Bryan, J.P.3
  • 15
    • 0033548432 scopus 로고    scopus 로고
    • Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction
    • Nuber U., and Scheffner M. Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction. J. Biol. Chem. 274 (1999) 7576-7582
    • (1999) J. Biol. Chem. , vol.274 , pp. 7576-7582
    • Nuber, U.1    Scheffner, M.2
  • 16
    • 0037046805 scopus 로고    scopus 로고
    • The ubiquitin-interacting motifs target the endocytic adaptor protein epsin for ubiquitination
    • Oldham C.E., Mohney R.P., Miller S.L., Hanes R.N., and O'Bryan J.P. The ubiquitin-interacting motifs target the endocytic adaptor protein epsin for ubiquitination. Curr. Biol. 12 (2002) 1112-1116
    • (2002) Curr. Biol. , vol.12 , pp. 1112-1116
    • Oldham, C.E.1    Mohney, R.P.2    Miller, S.L.3    Hanes, R.N.4    O'Bryan, J.P.5
  • 17
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: structures, functions, mechanisms
    • Pickart C.M., and Eddins M.J. Ubiquitin: structures, functions, mechanisms. Biochim. Biophys. Acta 1695 (2004) 55-72
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 18
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: polymeric protein signals
    • Pickart C.M., and Fushman D. Polyubiquitin chains: polymeric protein signals. Curr. Opin. Chem. Biol. 8 (2004) 610-616
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 22
    • 34250316712 scopus 로고    scopus 로고
    • Verveer, P.J., Rocks, O., Harpur, A.G., and Bastiaens, P.I.H. (2006). Imaging protein interactions by FRET Microscopy. Cold Spring Harbor Protocols. 10.1101/pdb.ip15.
  • 24
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng N., Wang P., Jeffrey P.D., and Pavletich N.P. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102 (2000) 533-539
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.