메뉴 건너뛰기




Volumn 2, Issue 3, 2001, Pages 169-178

Themes and variations on ubiquitylation

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA;

EID: 0035292759     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/35056563     Document Type: Review
Times cited : (1284)

References (107)
  • 1
  • 2
    • 0028109693 scopus 로고
    • Conjugates of ubiquitin cross-reactive protein distribute in a cytoskeletal pattern
    • Loeb, K. R. & Haas, A. L. Conjugates of ubiquitin cross-reactive protein distribute in a cytoskeletal pattern. Mol. Cell. Biol. 14, 8408-8419 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8408-8419
    • Loeb, K.R.1    Haas, A.L.2
  • 3
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • Jentsch, S. & Pyrowolakis, G. Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 10, 335-342 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 4
    • 0034595239 scopus 로고    scopus 로고
    • Ubiquitin-like proteins: New wines in new bottles
    • Yeh, E. T., Gong, L. & Kamitani, T. Ubiquitin-like proteins: new wines in new bottles. Gene 248, 1-14 (2000).
    • (2000) Gene , vol.248 , pp. 1-14
    • Yeh, E.T.1    Gong, L.2    Kamitani, T.3
  • 5
    • 0033636785 scopus 로고    scopus 로고
    • The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome
    • Kleijnen, M. F. et al. The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. Mol. Cell 6, 409-419 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 409-419
    • Kleijnen, M.F.1
  • 6
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse, J. M., Scheffner, M., Beaudenon, S. & Howley, P. M. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl Acad. Sci. USA. 92, 2563-2567 (1995).
    • (1995) Proc. Natl Acad. Sci. USA. , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 7
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro, C. A. & Weissman, A. M. RING finger proteins: mediators of ubiquitin ligase activity. Cell 102, 549-552 (2000).
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 8
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley, D., Bartel, B. & Varshavsky, A. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature 338, 394-401 (1989).
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 9
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson, K. D. Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. Semin. Cell. Dev. Biol. 11, 141-148 (2000).
    • (2000) Semin. Cell. Dev. Biol. , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 10
    • 0028577266 scopus 로고
    • Human ubiquitin-activating enzyme, E1. Indication of potential nuclear and cytoplasmic subpopulations using epitope-tagged cDNA constructs
    • Handley-Gearhart, P. M., Stephen, A. G., Trausch-Azar, J. S., Ciechanover, A. & Schwartz, A. L. Human ubiquitin-activating enzyme, E1. Indication of potential nuclear and cytoplasmic subpopulations using epitope-tagged cDNA constructs. J. Biol. Chem. 269, 33171-33178 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 33171-33178
    • Handley-Gearhart, P.M.1    Stephen, A.G.2    Trausch-Azar, J.S.3    Ciechanover, A.4    Schwartz, A.L.5
  • 11
    • 0029047641 scopus 로고
    • Ubiquitin-activating enzyme, E1, is phosphorylated in mammalian cells by the protein kinase Cdc2
    • Nagai, Y. et al. Ubiquitin-activating enzyme, E1, is phosphorylated in mammalian cells by the protein kinase Cdc2. J. Cell Sci. 108, 2145-2152 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 2145-2152
    • Nagai, Y.1
  • 13
    • 0021139080 scopus 로고
    • Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85
    • Finley, D., Ciechanover, A. & Varshavsky, A. Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85. Cell 37, 43-55 (1984). This is a landmark study that provided the first evidence of a role for the ubiquitin-conjugating system in cellular function.
    • (1984) Cell , vol.37 , pp. 43-55
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 14
    • 0032512737 scopus 로고    scopus 로고
    • An essential domain within Cdc34p is required for binding to a complex containing Cdc4p and Cdc53p in Saccharomyces cerevisiae
    • Mathias, N., Steussy, C. N. & Goebl, M. G. An essential domain within Cdc34p is required for binding to a complex containing Cdc4p and Cdc53p in Saccharomyces cerevisiae. J. Biol. Chem. 273, 4040-4045 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 4040-4045
    • Mathias, N.1    Steussy, C.N.2    Goebl, M.G.3
  • 15
    • 0033485869 scopus 로고    scopus 로고
    • The E2-E3 interaction in the N-end rule pathway: The RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain
    • Xie, Y. & Varshavsky, A. The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain. EMBO J. 18, 6832-6844 (1999). This study establishes a role for the RING finger in the activity of the N-end rule E3.
    • (1999) EMBO J. , vol.18 , pp. 6832-6844
    • Xie, Y.1    Varshavsky, A.2
  • 16
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • Sommer, T. & Jentsch, S. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365, 176-179 (1993). This study describes Ubc6 and provided the first suggestion of a linkage between the ubiquitin-conjugating system and the degradation of proteins from the endoplasmic reticulum.
    • (1993) Nature , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 17
    • 0032526948 scopus 로고    scopus 로고
    • A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors
    • Hauser, H. P., Bardroff, M., Pyrowolakis, G. & Jentsch, S. A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors. J. Cell Biol. 141, 1415-1422 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 1415-1422
    • Hauser, H.P.1    Bardroff, M.2    Pyrowolakis, G.3    Jentsch, S.4
  • 18
    • 0033591363 scopus 로고    scopus 로고
    • Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IκBα
    • Gonen, H. et al. Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IκBα. J. Biol. Chem. 274, 14823-14830 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 14823-14830
    • Gonen, H.1
  • 19
    • 0032524621 scopus 로고    scopus 로고
    • Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7
    • Schwarz, S. E. Rosa, J. L. & Scheffner, M. Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. J. Biol. Chem. 273, 12148-12154 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 12148-12154
    • Schwarz, S.E.1    Rosa, J.L.2    Scheffner, M.3
  • 20
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas, A. L. & Siepmann, T. J. Pathways of ubiquitin conjugation. FASEB J. 11, 1257-1268 (1997).
    • (1997) FASEB J. , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 21
    • 0032741446 scopus 로고    scopus 로고
    • Structure of an E6AP-UbcH7 complex: Insights into ubiquitination by the E2-E3 enzyme cascade
    • Huang, L. et al. Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science 286, 1321-1326 (1999).
    • (1999) Science , vol.286 , pp. 1321-1326
    • Huang, L.1
  • 22
    • 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. & Pavletich, N. P. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102, 533-539 (2000). References 21 and 22 describe the crystal structures of a HECT domain and a RING finger protein with an E2.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 23
    • 0033548432 scopus 로고    scopus 로고
    • Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction
    • Nuber, U. & Scheffner, M. Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction. J. Biol. Chem. 274, 7576-7582 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 7576-7582
    • Nuber, U.1    Scheffner, M.2
  • 24
    • 0031037265 scopus 로고    scopus 로고
    • Crystal structure of a class I ubiquitin conjugating enzyme (Ubc7) from Saccharomyces cerevisiae at 2.9 angstroms resolution
    • Cook, W. J., Martin, P. D., Edwards, B. F., Yamazaki, R. K. & Chau, V. Crystal structure of a class I ubiquitin conjugating enzyme (Ubc7) from Saccharomyces cerevisiae at 2.9 angstroms resolution. Biochemistry 36, 1621-1627 (1997).
    • (1997) Biochemistry , vol.36 , pp. 1621-1627
    • Cook, W.J.1    Martin, P.D.2    Edwards, B.F.3    Yamazaki, R.K.4    Chau, V.5
  • 25
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., Huibregtse, J. M., Vierstra, R. D. & Howley, P. M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495-505 (1993). This is a seminal paper describing the characterization of E6-AP, the first described member of the HECT domain family of E3s.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 26
    • 0033603339 scopus 로고    scopus 로고
    • Identification of HHR23a as a substrate for E6-associated protein-mediated ubiquitination
    • Kumar, S., Talis, A. L. & Howley, P. M. Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination. J. Biol. Chem. 274, 18785-18792 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 18785-18792
    • Kumar, S.1    Talis, A.L.2    Howley, P.M.3
  • 27
    • 0031012849 scopus 로고    scopus 로고
    • UBE3A/E6-AP mutations cause Angelman syndrome
    • Kishino, T., Lalande, M. & Wagstaff, J. UBE3A/E6-AP mutations cause Angelman syndrome. Nature Genet. 15, 70-73 (1997).
    • (1997) Nature Genet. , vol.15 , pp. 70-73
    • Kishino, T.1    Lalande, M.2    Wagstaff, J.3
  • 28
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay, B. K., Williamson, M. P. & Sudol, M. The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14, 231-241 (2000).
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 29
    • 0034235434 scopus 로고    scopus 로고
    • Ubiquitination and endocytosis of plasma membrane proteins: Role of Nedd4/Rsp5p family of ubiquitin-protein ligases
    • Rotin, D., Staub, O. & Haguenauer-Tsapis, R. Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4/Rsp5p family of ubiquitin-protein ligases. J. Membr. Biol. 176, 1-17 (2000).
    • (2000) J. Membr. Biol. , vol.176 , pp. 1-17
    • Rotin, D.1    Staub, O.2    Haguenauer-Tsapis, R.3
  • 30
    • 0034717801 scopus 로고    scopus 로고
    • Apical membrane targeting of Nedd4 is mediated by an association of its C2 domain with annexin XIIIb
    • Plant, P. J. et al. Apical membrane targeting of Nedd4 is mediated by an association of its C2 domain with annexin XIIIb. J. Cell Biol. 149, 1473-1484 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 1473-1484
    • Plant, P.J.1
  • 31
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • Hoppe, T. et al. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102, 577-586 (2000).
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1
  • 32
    • 0028982263 scopus 로고
    • Ubiquitin-mediated processing of NF-κB transcriptional activator precursor p105. Reconstitution of a cell-free system and identification of the ubiquitin-carrier protein, E2, and a novel ubiquitin-protein ligase, E3, involved in conjugation
    • Orian, A. et al. Ubiquitin-mediated processing of NF-κB transcriptional activator precursor p105. Reconstitution of a cell-free system and identification of the ubiquitin-carrier protein, E2, and a novel ubiquitin-protein ligase, E3, involved in conjugation. J. Biol. Chem. 270, 21707-21714 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 21707-21714
    • Orian, A.1
  • 33
    • 0032441479 scopus 로고    scopus 로고
    • Ubiquitin and the control of protein fate in the secretory and endocytic pathways
    • Bonifacino, J. S. & Weissman, A. M. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu. Rev. Cell. Dev. Biol. 14, 19-57 (1998).
    • (1998) Annu. Rev. Cell. Dev. Biol. , vol.14 , pp. 19-57
    • Bonifacino, J.S.1    Weissman, A.M.2
  • 35
    • 0033961923 scopus 로고    scopus 로고
    • RING for destruction?
    • Freemont, P. S. RING for destruction? Curr. Biol. 10, R84-R87 (2000).
    • (2000) Curr. Biol. , vol.10
    • Freemont, P.S.1
  • 36
    • 0033597443 scopus 로고    scopus 로고
    • Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase
    • Kamura, T. et al. Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase. Science 284, 657-661 (1999).
    • (1999) Science , vol.284 , pp. 657-661
    • Kamura, T.1
  • 37
    • 0033120027 scopus 로고    scopus 로고
    • ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity
    • Ohta, T., Michel, J. J., Schottelius, A. J. & Xiong, Y. ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. Mol. Cell 3, 535-541 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 535-541
    • Ohta, T.1    Michel, J.J.2    Schottelius, A.J.3    Xiong, Y.4
  • 38
    • 0033120593 scopus 로고    scopus 로고
    • Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of IκBα
    • Tan, P. et al. Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of IκBα. Mol. Cell 3, 527-533 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 527-533
    • Tan, P.1
  • 39
    • 0033596977 scopus 로고    scopus 로고
    • Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1
    • Skowyra, D. et al. Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1. Science 284, 662-665 (1999).
    • (1999) Science , vol.284 , pp. 662-665
    • Skowyra, D.1
  • 40
    • 20244389988 scopus 로고    scopus 로고
    • Cdc53/cullin and the essential hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme cdc34
    • Seol, J. H. et al. Cdc53/cullin and the essential hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme cdc34. Genes Dev. 13, 1614-1626 (1999). References 36-40 all describe the characterization of a small RING finger protein as an integral component of SCF E3s.
    • (1999) Genes Dev. , vol.13 , pp. 1614-1626
    • Seol, J.H.1
  • 41
    • 0033613222 scopus 로고    scopus 로고
    • RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination
    • Lorick, K. L. et al. RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. Proc. Natl Acad. Sci. USA 96, 11364-11369 (1999). This study suggests a general role for RING fingers in ubiquitylation.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11364-11369
    • Lorick, K.L.1
  • 42
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H. & Weissman, A. M. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem. 275, 8945-8951 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 43
    • 0034624678 scopus 로고    scopus 로고
    • Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase
    • Honda, R. & Yasuda, H. Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase. Oncogene 19, 1473-1476 (2000).
    • (2000) Oncogene , vol.19 , pp. 1473-1476
    • Honda, R.1    Yasuda, H.2
  • 44
    • 0033529537 scopus 로고    scopus 로고
    • The RING finger of c-Cbl mediates desensitization of the epidermal growth factor receptor
    • Waterman, H., Levkowitz, G., Alroy, I. & Yarden, Y. The RING finger of c-Cbl mediates desensitization of the epidermal growth factor receptor. J. Biol. Chem. 274, 22151-22154 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 22151-22154
    • Waterman, H.1    Levkowitz, G.2    Alroy, I.3    Yarden, Y.4
  • 45
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine kinase negative regulator c-Cbl as a RING-type, E2- Dependent ubiquitin-protein ligase
    • Joazeiro, C. A. et al. The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. Science 286, 309-312 (1999).
    • (1999) Science , vol.286 , pp. 309-312
    • Joazeiro, C.A.1
  • 46
    • 0033615732 scopus 로고    scopus 로고
    • Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7
    • Yokouchi, M. et al. Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7. J. Biol. Chem. 274, 31707-31712 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 31707-31712
    • Yokouchi, M.1
  • 47
    • 0032933351 scopus 로고    scopus 로고
    • Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins
    • Hu, G. & Fearon, E. R. Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins. Mol. Cell. Biol. 19, 724-732 (1999). References 42-47 demonstrate a role for the RING finger in a variety of known and suspected E3s.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 724-732
    • Hu, G.1    Fearon, E.R.2
  • 48
    • 0032549115 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the anaphase-promoting complex from yeast: Identification of a subunit related to cullins
    • Zachariae, W. et al. Mass spectrometric analysis of the anaphase-promoting complex from yeast: identification of a subunit related to cullins. Science 279, 1216-1219 (1998).
    • (1998) Science , vol.279 , pp. 1216-1219
    • Zachariae, W.1
  • 49
    • 0032478697 scopus 로고    scopus 로고
    • The cancer-predisposing mutation C61G disrupts homodimer formation in the NH2-terminal BRCA1 RING finger domain
    • Brzovic, P. S., Meza, J., King, M. C. & Klevit, R. E. The cancer-predisposing mutation C61G disrupts homodimer formation in the NH2-terminal BRCA1 RING finger domain. J. Biol. Chem. 273, 7795-7799 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 7795-7799
    • Brzovic, P.S.1    Meza, J.2    King, M.C.3    Klevit, R.E.4
  • 50
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • Yang, Y., Fang, S., Jensen, J. P., Weissman, A. M. & Ashwell, J. D. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science 288, 874-877 (2000).
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 51
    • 0034282432 scopus 로고    scopus 로고
    • The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7
    • Hwang, H. K. et al. The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7. J. Biol. Chem. 275, 26661-26664 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26661-26664
    • Hwang, H.K.1
  • 52
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson's disease gene product, Parkin, in a ubiquitin-protein ligase
    • Shimura, H. et al. Familial Parkinson's disease gene product, Parkin, in a ubiquitin-protein ligase. Nature Genet. 25, 302-305 (2000).
    • (2000) Nature Genet. , vol.25 , pp. 302-305
    • Shimura, H.1
  • 53
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang, Y. et al. Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc. Natl Acad. Sci. USA 97, 13354-13359 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13354-13359
    • Zhang, Y.1
  • 54
    • 0033930277 scopus 로고    scopus 로고
    • The APC11 RING-H2 finger mediates E2-dependent ubiquitination
    • Leverson, J. D. et al. The APC11 RING-H2 finger mediates E2-dependent ubiquitination. Mol. Biol. Cell 11, 2315-2325 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2315-2325
    • Leverson, J.D.1
  • 55
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies, R. J. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell. Dev. Biol. 15, 435-467 (1999).
    • (1999) Annu. Rev. Cell. Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 56
    • 0032852311 scopus 로고    scopus 로고
    • The anaphase-promoting complex: New subunits and regulators
    • Page, A. M. & Hieter, P. The anaphase-promoting complex: new subunits and regulators. Annu. Rev. Biochem. 68, 583-609 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 583-609
    • Page, A.M.1    Hieter, P.2
  • 57
    • 0033995119 scopus 로고    scopus 로고
    • Proteolysis and the cell cycle: With this RING I do thee destroy
    • Tyers, M. & Jorgensen, P. Proteolysis and the cell cycle: with this RING I do thee destroy. Curr. Opin. Genet. Dev. 10, 54-64 (2000).
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 54-64
    • Tyers, M.1    Jorgensen, P.2
  • 58
    • 0030602813 scopus 로고    scopus 로고
    • SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
    • Bai, C. et al. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86, 263-274 (1996).
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1
  • 59
    • 0033638333 scopus 로고    scopus 로고
    • Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins
    • Zhou, P., Bogacki, R., McReynolds, L. & Howley, P. M. Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins. Mol. Cell 6, 751-756 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 751-756
    • Zhou, P.1    Bogacki, R.2    McReynolds, L.3    Howley, P.M.4
  • 60
    • 0034604341 scopus 로고    scopus 로고
    • Met30-mediated inactivation of the transcription factor Met4
    • Met30-mediated inactivation of the transcription factor Met4. Cell 102, 303-314 (2000).
    • (2000) Cell , vol.102 , pp. 303-314
    • Kaiser, P.1    Flick, K.2    Wittenberg, C.3    Reed, S.I.4
  • 61
    • 0033565672 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity
    • Lisztwan, J., Imbert, G., Wirbelauer, C., Gstaiger, M. & Krek, W. The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity. Genes Dev. 13, 1822-1833 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1822-1833
    • Lisztwan, J.1    Imbert, G.2    Wirbelauer, C.3    Gstaiger, M.4    Krek, W.5
  • 62
    • 0033607291 scopus 로고    scopus 로고
    • Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex
    • Iwai, K. et al. Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex. Proc. Natl Acad. Sci. USA 96, 12436-12441 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12436-12441
    • Iwai, K.1
  • 63
    • 0033776536 scopus 로고    scopus 로고
    • Ubiquitination of hypoxia-inducible factor requires direct binding to the β-domain of the von Hippel-Lindau protein
    • Ohh, M. et al. Ubiquitination of hypoxia-inducible factor requires direct binding to the β-domain of the von Hippel-Lindau protein. Nature Cell Biol. 2, 423-427 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 423-427
    • Ohh, M.1
  • 64
    • 0034682783 scopus 로고    scopus 로고
    • Hypoxia inducible factor-α binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein
    • Cockman, M. E. et al. Hypoxia inducible factor-α binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein. J. Biol. Chem. 275, 25733-25741 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 25733-25741
    • Cockman, M.E.1
  • 65
    • 0034641615 scopus 로고    scopus 로고
    • Activation of HIF1α ubiquitination by a reconstituted von hippel-lindau (VHL) tumor suppressor complex
    • Kamura, T. et al. Activation of HIF1α ubiquitination by a reconstituted von hippel-lindau (VHL) tumor suppressor complex. Proc. Natl Acad. Sci. USA 97, 10430-10435 (2000). References 61-65 establish the VHL-CBC complex as an E3 and show that HIF1α is a substrate.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10430-10435
    • Kamura, T.1
  • 66
    • 0032535364 scopus 로고    scopus 로고
    • The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras. WD-40 repeat, and ankyrin repeat families
    • Kamura, T. et al. The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras. WD-40 repeat, and ankyrin repeat families. Genes Dev. 12, 3872-3881 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 3872-3881
    • Kamura, T.1
  • 67
    • 0033616143 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: Their diversity and emerging roles
    • Chung, C. H. & Baek, S. H. Deubiquitinating enzymes: their diversity and emerging roles. Biochem. Biophys. Res. Commun. 266, 633-640 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 633-640
    • Chung, C.H.1    Baek, S.H.2
  • 68
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • Papa, F. R. & Hochstrasser, M. The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature 366, 313-319 (1993).
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.R.1    Hochstrasser, M.2
  • 69
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • Lam, Y. A., Xu, W., DeMartino, G. N. & Cohen, R. E. Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 385, 737-740 (1997).
    • (1997) Nature , vol.385 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    DeMartino, G.N.3    Cohen, R.E.4
  • 70
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl, M. et al. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-644 (1999).
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1
  • 71
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence, J., Sadis, S., Haas, A. L. & Finley, D. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol. Cell. Biol. 15, 1265-1273 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 72
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann, R. M. & Pickart, C. M. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell 96, 645-653 (1999).
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 73
    • 0030800865 scopus 로고    scopus 로고
    • Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities
    • Baily, V., Lauder, S., Prakash, S. & Prakash, L. Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities. J. Biol. Chem. 272, 23360-23365 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 23360-23365
    • Baily, V.1    Lauder, S.2    Prakash, S.3    Prakash, L.4
  • 74
    • 0034600851 scopus 로고    scopus 로고
    • Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair
    • Ulrich, H. D. & Jentsch, S. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. EMBO J. 19, 3388-3397 (2000).
    • (2000) EMBO J. , vol.19 , pp. 3388-3397
    • Ulrich, H.D.1    Jentsch, S.2
  • 75
    • 0034616943 scopus 로고    scopus 로고
    • Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain
    • Spence, J. et al. Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain. Cell 102, 67-76 (2000). This is provocative study that demonstrates a role for K63-linked multi-ubiquitin chains in regulating translation.
    • (2000) Cell , vol.102 , pp. 67-76
    • Spence, J.1
  • 76
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng, L. et al. Activation of the IκB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103, 351-361 (2000).
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1
  • 77
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V. et al. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243, 1576-1583 (1989).
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1
  • 78
    • 0030070803 scopus 로고    scopus 로고
    • Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of IκBα
    • Baldi, L., Brown, K., Franzoso, G. & Siebenlist, U. Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of IκBα. J. Biol. Chem. 271, 376-379 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 376-379
    • Baldi, L.1    Brown, K.2    Franzoso, G.3    Siebenlist, U.4
  • 79
    • 0028303252 scopus 로고
    • Activation-dependent ubiquitination a T cell antigen receptor subunit on multiple intracellular lysines
    • Hou, D., Cenciarelli, C., Jensen, J. P., Nguyen, H. B. & Weissman, A. M. Activation-dependent ubiquitination a T cell antigen receptor subunit on multiple intracellular lysines. J. Biol. Chem. 269, 14244-14247 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 14244-14247
    • Hou, D.1    Cenciarelli, C.2    Jensen, J.P.3    Nguyen, H.B.4    Weissman, A.M.5
  • 80
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • Treier, M., Staszewski, L. M. & Bohmann, D. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78, 787-793 (1994).
    • (1994) Cell , vol.78 , pp. 787-793
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 81
    • 0032531925 scopus 로고    scopus 로고
    • A novel site for ubiquitination: The N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein
    • Breitschopf, K., Bengal, E., Ziv, T., Admon, A. & Ciechanover, A. A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein. EMBO J. 17, 5964-5973 (1998).
    • (1998) EMBO J. , vol.17 , pp. 5964-5973
    • Breitschopf, K.1    Bengal, E.2    Ziv, T.3    Admon, A.4    Ciechanover, A.5
  • 82
    • 0033623850 scopus 로고    scopus 로고
    • Cp1 ubiquitination
    • Cp1 ubiquitination. Mol. Cell 5, 403-410 (2000). This study provides strong evidence for ubiquitin-independent proteasomal degradation of a protein that is known to ubiquitylated.
    • (2000) Mol. Cell , vol.5 , pp. 403-410
    • Sheaff, R.J.1
  • 83
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • van Nocker, S. et al. The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol. 16, 6020-6028 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6020-6028
    • Van Nocker, S.1
  • 84
    • 0033208984 scopus 로고    scopus 로고
    • ER protein quality control and proteasome-mediated protein degradation
    • Brodsky, J. L. & McCracken, A. A. ER protein quality control and proteasome-mediated protein degradation. Semin. Cell Dev. Biol. 10, 507-513 (1999).
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 507-513
    • Brodsky, J.L.1    McCracken, A.A.2
  • 85
    • 0033609306 scopus 로고    scopus 로고
    • Mutations in serines 15 and 20 of human p53 impair its apoptotic activity
    • Unger, T. et al. Mutations in serines 15 and 20 of human p53 impair its apoptotic activity. Oncogene 18, 3205-3212 (1999).
    • (1999) Oncogene , vol.18 , pp. 3205-3212
    • Unger, T.1
  • 86
    • 0033118933 scopus 로고    scopus 로고
    • DNA damage-inducible phosphorylation of p53 at N-terminal sites including a novel site, Ser20, requires tetramerization
    • Shieh, S. Y., Taya, Y. & Prives, C. DNA damage-inducible phosphorylation of p53 at N-terminal sites including a novel site, Ser20, requires tetramerization. EMBO J. 18, 1815-1823 (1999).
    • (1999) EMBO J. , vol.18 , pp. 1815-1823
    • Shieh, S.Y.1    Taya, Y.2    Prives, C.3
  • 87
    • 0033771948 scopus 로고    scopus 로고
    • Identification of a cryptic nucleolar-localization signal in MDM2
    • Lohrum, M. A., Ashcroft, M., Kubbutat, M. H. & Vousden, K. H. Identification of a cryptic nucleolar-localization signal in MDM2. Nature Cell Biol. 2, 179-181 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 179-181
    • Lohrum, M.A.1    Ashcroft, M.2    Kubbutat, M.H.3    Vousden, K.H.4
  • 88
    • 0034017956 scopus 로고    scopus 로고
    • Cooperative signals governing ARF-mdm2 interaction and nucleolar localization of the complex
    • Weber, J. D. et al. Cooperative signals governing ARF-mdm2 interaction and nucleolar localization of the complex. Mol. Cell. Biol. 20, 2517-2528 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2517-2528
    • Weber, J.D.1
  • 89
    • 0034603897 scopus 로고    scopus 로고
    • ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo
    • ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo. Oncogene 19, 2312-2323 (2000).
    • (2000) Oncogene , vol.19 , pp. 2312-2323
    • Midgley, C.A.1
  • 90
    • 0033521621 scopus 로고    scopus 로고
    • ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53. EMBO J. 18, 22-27 (1999).
    • (1999) EMBO J. , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 91
    • 0033963335 scopus 로고    scopus 로고
    • MdmX protects p53 from Mdm2-mediated degradation
    • Jackson, M. W. & Berberich, S. J. MdmX protects p53 from Mdm2-mediated degradation. Mol. Cell. Biol. 20, 1001-1007 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1001-1007
    • Jackson, M.W.1    Berberich, S.J.2
  • 92
    • 0033621415 scopus 로고    scopus 로고
    • Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein
    • Sharp, D. A., Kratowicz, S. A., Sank, M. J. & George, D. L. Stabilization of the MDM2 oncoprotein by interaction with the structurally related MDMX protein. J. Biol. Chem. 274, 38189-38196 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 38189-38196
    • Sharp, D.A.1    Kratowicz, S.A.2    Sank, M.J.3    George, D.L.4
  • 93
    • 0033051322 scopus 로고    scopus 로고
    • MDM2 interacts with MDMX through their RING finger domains
    • Tanimura, S. et al. MDM2 interacts with MDMX through their RING finger domains. FEBS Lett. 447, 5-9 (1999).
    • (1999) FEBS Lett. , vol.447 , pp. 5-9
    • Tanimura, S.1
  • 94
    • 0034705319 scopus 로고    scopus 로고
    • SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53
    • Buschmann, T., Fuchs, S. Y., Lee, C.-G., Pan, Z.-Q. & Ronai, Z. SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53. Cell 101, 753-762 (2000).
    • (2000) Cell , vol.101 , pp. 753-762
    • Buschmann, T.1    Fuchs, S.Y.2    Lee, C.-G.3    Pan, Z.-Q.4    Ronai, Z.5
  • 95
    • 0033536230 scopus 로고    scopus 로고
    • Mdm2 binds p73α without targeting degradation
    • Balint, E., Bates, S. & Vousden, K. H. Mdm2 binds p73α without targeting degradation. Oncogene 18, 3923-3929 (1999).
    • (1999) Oncogene , vol.18 , pp. 3923-3929
    • Balint, E.1    Bates, S.2    Vousden, K.H.3
  • 96
    • 0033602462 scopus 로고    scopus 로고
    • Inactivation of the p53-homologue p73 by the mdm2-oncoprotein
    • Dobbelstein, M., Wienzek, S., Konig, C. & Roth, J. Inactivation of the p53-homologue p73 by the mdm2-oncoprotein. Oncogene 18, 2101-2106 (1999).
    • (1999) Oncogene , vol.18 , pp. 2101-2106
    • Dobbelstein, M.1    Wienzek, S.2    Konig, C.3    Roth, J.4
  • 97
    • 0032961828 scopus 로고    scopus 로고
    • MDM2 suppresses p73 function without promoting p73 degradation
    • Zeng, X. et al. MDM2 suppresses p73 function without promoting p73 degradation. Mol. Cell. Biol. 19, 3257-3256 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3257-13256
    • Zeng, X.1
  • 98
    • 0034730172 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system in Alzheimer's disease
    • Lam, Y. A. et al. Inhibition of the ubiquitin-proteasome system in Alzheimer's disease. Proc. Natl Acad. Sci. USA. 97, 9902-9906 (2000).
    • (2000) Proc. Natl Acad. Sci. USA. , vol.97 , pp. 9902-9906
    • Lam, Y.A.1
  • 100
    • 0034600951 scopus 로고    scopus 로고
    • Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission yeast
    • Osaka, F. et al. Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission yeast. EMBO J. 19, 3475-3484 (2000).
    • (2000) EMBO J. , vol.19 , pp. 3475-3484
    • Osaka, F.1
  • 101
    • 0034712842 scopus 로고    scopus 로고
    • A Nedd8 conjugation pathway is essential for proteolytic targeting of p27Kip1 by ubiquitination
    • Podust, V. N. et al. A Nedd8 conjugation pathway is essential for proteolytic targeting of p27Kip1 by ubiquitination. Proc. Natl Acad. Sci. USA 97, 4579-4584 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4579-4584
    • Podust, V.N.1
  • 102
    • 0034117282 scopus 로고    scopus 로고
    • Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha
    • Read, M. A. et al. Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha. Mol. Cell. Biol. 20, 2326-2333 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2326-2333
    • Read, M.A.1
  • 103
    • 0034595849 scopus 로고    scopus 로고
    • A dominant-negative UBC12 mutant sequesters NEDD8 and inhibits NEDD8 conjugation in vivo
    • Wada, H., Yeh, E. T. & Kamitani, T. A dominant-negative UBC12 mutant sequesters NEDD8 and inhibits NEDD8 conjugation in vivo. J. Biol. Chem. 275, 17008-17015 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 17008-17015
    • Wada, H.1    Yeh, E.T.2    Kamitani, T.3
  • 104
    • 0034644650 scopus 로고    scopus 로고
    • Conjugation of Nedd8 to CUL1 enhances the ability of the ROC1-CUL1 complex to promote ubiquitin polymerization
    • Wu, K., Chen, A. & Pan, Z. Q. Conjugation of Nedd8 to CUL1 enhances the ability of the ROC1-CUL1 complex to promote ubiquitin polymerization. J. Biol. Chem. 275, 32317-32324 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 32317-32324
    • Wu, K.1    Chen, A.2    Pan, Z.Q.3
  • 105
    • 0032522382 scopus 로고    scopus 로고
    • A novel protein modification pathway related to the ubiquitin system
    • Liakopoulos, D., Doenges, G., Matuschewski, K. & Jentsch, S. A novel protein modification pathway related to the ubiquitin system. EMBO J. 17, 2208-2214 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2208-2214
    • Liakopoulos, D.1    Doenges, G.2    Matuschewski, K.3    Jentsch, S.4
  • 106
    • 0033545860 scopus 로고    scopus 로고
    • Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function
    • Liakopoulos, D., Busgen, T., Brychzy, A., Jentsch, S. & Pause, A. Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function. Proc. Natl Acad. Sci. USA 96, 5510-5515 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 5510-5515
    • Liakopoulos, D.1    Busgen, T.2    Brychzy, A.3    Jentsch, S.4    Pause, A.5
  • 107
    • 0034255264 scopus 로고    scopus 로고
    • The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex
    • Gmachl, M., Gieffers, C., Podtelejnikov, A. V., Mann, M. & Peters, J. M. The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex. Proc. Natl Acad. Sci. USA 97, 8973-8978 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8973-8978
    • Gmachl, M.1    Gieffers, C.2    Podtelejnikov, A.V.3    Mann, M.4    Peters, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.