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Volumn 1695, Issue 1-3, 2004, Pages 55-72

Ubiquitin: Structures, functions, mechanisms

Author keywords

E1; E2; E3; Nedd8; Sumo; Ubc; Ubiquitin

Indexed keywords

BIOLOGICAL RESPONSE MODIFIER; BRCA1 PROTEIN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; LIGASE; PROTEIN MDM2; PROTEIN P53; PROTEIN SUBUNIT; UBIQUITIN; VON HIPPEL LINDAU PROTEIN;

EID: 9744227183     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2004.09.019     Document Type: Review
Times cited : (1142)

References (142)
  • 1
    • 0003096992 scopus 로고    scopus 로고
    • Polyubiquitin chains
    • J. Peters R. Harris D. Finley Plenum Press New York
    • C.M. Pickart Polyubiquitin chains J. Peters R. Harris D. Finley Ubiquitin and the Biology of the Cell 1998 Plenum Press New York 19 63
    • (1998) Ubiquitin and the Biology of the Cell , pp. 19-63
    • Pickart, C.M.1
  • 2
    • 0032053883 scopus 로고    scopus 로고
    • There's the Rub: A novel ubiquitin-like modification linked to cell cycle regulation
    • M. Hochstrasser There's the Rub: a novel ubiquitin-like modification linked to cell cycle regulation Genes Dev. 12 1998 901 907
    • (1998) Genes Dev. , vol.12 , pp. 901-907
    • Hochstrasser, M.1
  • 3
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • M. Hochstrasser Evolution and function of ubiquitin-like protein-conjugation systems Nat. Cell Biol. 2 2000 E153 E157
    • (2000) Nat. Cell Biol. , vol.2
    • Hochstrasser, M.1
  • 4
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • S. Jentsch, and G. Pyrowolakis Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 10 2000 335 342
    • (2000) Trends Cell Biol. , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 5
    • 0035167185 scopus 로고    scopus 로고
    • Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation
    • M.J. Rudolph, M.M. Wuebbens, K.V. Rajagopalan, and H. Schindelin Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation Nat. Struct. Biol. 8 2001 42 46
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 42-46
    • Rudolph, M.J.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 6
    • 0035170874 scopus 로고    scopus 로고
    • Solution structure of ThiS and implications for the evolutionary roots of ubiquitin
    • C. Wang, J. Xi, T.P. Begley, and L.K. Nicholson Solution structure of ThiS and implications for the evolutionary roots of ubiquitin Nat. Struct. Biol. 8 2001 47 51
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 47-51
    • Wang, C.1    Xi, J.2    Begley, T.P.3    Nicholson, L.K.4
  • 7
    • 0035891318 scopus 로고    scopus 로고
    • Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoeD complex
    • M.W. Lake, M.M. Wuebens, K.V. Rajagopalan, and H. Schindlein Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoeD complex Nature 414 2001 325 329
    • (2001) Nature , vol.414 , pp. 325-329
    • Lake, M.W.1    Wuebens, M.M.2    Rajagopalan, K.V.3    Schindlein, H.4
  • 8
    • 0141987892 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation
    • J. Bloom, V. Amador, F. Bartolini, G. DeMartino, and M. Pagano Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation Cell 115 2003 71 82
    • (2003) Cell , vol.115 , pp. 71-82
    • Bloom, J.1    Amador, V.2    Bartolini, F.3    Demartino, G.4    Pagano, M.5
  • 9
    • 1342321745 scopus 로고    scopus 로고
    • ISG15: The immunological kin of ubiquitin
    • K.J. Ritchie, and D.E. Zhang ISG15: the immunological kin of ubiquitin Semin. Cell Dev. Biol. 15 2004 237 246
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 237-246
    • Ritchie, K.J.1    Zhang, D.E.2
  • 11
    • 0034677757 scopus 로고    scopus 로고
    • A protein conjugation system in yeast with homology to biosynthetic reaction in prokaryotes
    • K. Furukawa, N. Mizushima, T. Noda, and Y. Ohsumi A protein conjugation system in yeast with homology to biosynthetic reaction in prokaryotes J. Biol. Chem. 275 2000 7462 7465
    • (2000) J. Biol. Chem. , vol.275 , pp. 7462-7465
    • Furukawa, K.1    Mizushima, N.2    Noda, T.3    Ohsumi, Y.4
  • 12
    • 0037192523 scopus 로고    scopus 로고
    • Role of a ubiquitin-like modification in polarized morphogenesis
    • G.A.G. Dittmar, C.R.M. Wilkinson, P.T. Jedrzejewski, and D. Finley Role of a ubiquitin-like modification in polarized morphogenesis Science 295 2002 2442 2446
    • (2002) Science , vol.295 , pp. 2442-2446
    • Dittmar, G.A.G.1    Wilkinson, C.R.M.2    Jedrzejewski, P.T.3    Finley, D.4
  • 13
    • 0344824569 scopus 로고    scopus 로고
    • Urmylation: A ubiquitin-like pathway that functions during invasive growth and budding in yeast
    • A.S. Goehring, D.M. Rivers, and G.F. Sprague Urmylation: a ubiquitin-like pathway that functions during invasive growth and budding in yeast Mol. Biol. Cell 14 2003 4329 4341
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4329-4341
    • Goehring, A.S.1    Rivers, D.M.2    Sprague, G.F.3
  • 14
    • 0034682843 scopus 로고    scopus 로고
    • Structure of GATE-16, membrane transport modulator and mammalian ortholog of autophagocytosis factor Aut7p
    • Y. Paz, Z. Elazar, and D. Fass Structure of GATE-16, membrane transport modulator and mammalian ortholog of autophagocytosis factor Aut7p J. Biol. Chem. 275 2000 25445 25450
    • (2000) J. Biol. Chem. , vol.275 , pp. 25445-25450
    • Paz, Y.1    Elazar, Z.2    Fass, D.3
  • 15
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Y. Ohsumi Molecular dissection of autophagy: two ubiquitin-like systems Nat. Rev., Mol. Cell Biol. 2 2001 211 216
    • (2001) Nat. Rev., Mol. Cell Biol. , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 16
    • 0037065732 scopus 로고    scopus 로고
    • Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a
    • K.J. Walters, M.F. Kleijnen, A.M. Goh, G. Wagner, and P.M. Howley Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a Biochemistry 41 2002 1767 1777
    • (2002) Biochemistry , vol.41 , pp. 1767-1777
    • Walters, K.J.1    Kleijnen, M.F.2    Goh, A.M.3    Wagner, G.4    Howley, P.M.5
  • 17
    • 0036569345 scopus 로고    scopus 로고
    • From UBA to UBX: New words in the ubiquitin vocabulary
    • A. Buchberger From UBA to UBX: new words in the ubiquitin vocabulary Trends Cell Biol. 12 2002 216 221
    • (2002) Trends Cell Biol. , vol.12 , pp. 216-221
    • Buchberger, A.1
  • 19
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • L. Hicke, and R. Dunn Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins Annu. Rev. Cell Dev. Biol. 19 2003 141 172
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 21
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • C. Hoege, B. Pfander, G.-L. Moldovan, G. Pyrowolakis, and S. Jentsch RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO Nature 419 2002 135 141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.-L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 22
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • C.M. Pickart Back to the future with ubiquitin Cell 116 2004 181 190
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 24
    • 0035929607 scopus 로고    scopus 로고
    • The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis
    • S. Raasi, G. Schmidtke, and M. Goettrup The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis J. Biol. Chem. 276 2001 35334 35443
    • (2001) J. Biol. Chem. , vol.276 , pp. 35334-35443
    • Raasi, S.1    Schmidtke, G.2    Goettrup, M.3
  • 25
    • 0028146192 scopus 로고
    • Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant
    • D. Finley, S. Sadis, B.P. Monia, P. Boucher, D.J. Ecker, S.T. Crooke, and V. Chau Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant Mol. Cell. Biol. 14 1994 5501 5509
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5501-5509
    • Finley, D.1    Sadis, S.2    Monia, B.P.3    Boucher, P.4    Ecker, D.J.5    Crooke, S.T.6    Chau, V.7
  • 26
    • 0242414786 scopus 로고    scopus 로고
    • The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast
    • G.R. Bylebyl, I. Belichenko, and E.S. Johnson The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast J. Biol. Chem. 278 2003 44113 44120
    • (2003) J. Biol. Chem. , vol.278 , pp. 44113-44120
    • Bylebyl, G.R.1    Belichenko, I.2    Johnson, E.S.3
  • 28
    • 0037456828 scopus 로고    scopus 로고
    • Insights into the ubiquitin transfer cascade from the structure of the E1 for NEDD8
    • H. Walden, M.S. Podgorski, and B.A. Schulman Insights into the ubiquitin transfer cascade from the structure of the E1 for NEDD8 Nature 422 2003 330 334
    • (2003) Nature , vol.422 , pp. 330-334
    • Walden, H.1    Podgorski, M.S.2    Schulman, B.A.3
  • 29
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • C. Pickart Mechanisms underlying ubiquitination Annu. Rev. Biochem. 70 2001 503 533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.1
  • 31
    • 0028308828 scopus 로고
    • Site-directed mutagenesis of ubiquitin: Differential roles for arginine in the interaction with ubiquitin-activating enzyme
    • T. Burch, and A.L. Haas Site-directed mutagenesis of ubiquitin: differential roles for arginine in the interaction with ubiquitin-activating enzyme Biochemistry 33 1994 7300 7308
    • (1994) Biochemistry , vol.33 , pp. 7300-7308
    • Burch, T.1    Haas, A.L.2
  • 32
    • 0032567528 scopus 로고    scopus 로고
    • Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes
    • F.G. Whitby, G. Xia, C.M. Pickart, and C.P. Hill Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes J. Biol. Chem. 273 1998 34893 34991
    • (1998) J. Biol. Chem. , vol.273 , pp. 34893-34991
    • Whitby, F.G.1    Xia, G.2    Pickart, C.M.3    Hill, C.P.4
  • 33
    • 0347416977 scopus 로고    scopus 로고
    • The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1
    • H. Walden, M.S. Podgorski, D.T. Huang, D.W. Miller, R.J. Howard, D.L. Minor, J.M. Holton, and B.A. Schulman The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1 Mol. Cell 12 2003 1427 1437
    • (2003) Mol. Cell , vol.12 , pp. 1427-1437
    • Walden, H.1    Podgorski, M.S.2    Huang, D.T.3    Miller, D.W.4    Howard, R.J.5    Minor, D.L.6    Holton, J.M.7    Schulman, B.A.8
  • 34
    • 0036922992 scopus 로고    scopus 로고
    • Structural properties of polyubiquitin chains in solution
    • R. Varadan, O. Walker, C.M. Pickart, and D. Fushman Structural properties of polyubiquitin chains in solution J. Mol. Biol. 324 2002 637 647
    • (2002) J. Mol. Biol. , vol.324 , pp. 637-647
    • Varadan, R.1    Walker, O.2    Pickart, C.M.3    Fushman, D.4
  • 35
    • 0037090823 scopus 로고    scopus 로고
    • Regulation of the ubiquitin-conjugating enzyme hHR6A by CDK-mediated phosphorylation
    • B. Sarcevic, A. Mawson, R.T. Baker, and R.L. Sutherland Regulation of the ubiquitin-conjugating enzyme hHR6A by CDK-mediated phosphorylation EMBO J. 21 2002 2009 2018
    • (2002) EMBO J. , vol.21 , pp. 2009-2018
    • Sarcevic, B.1    Mawson, A.2    Baker, R.T.3    Sutherland, R.L.4
  • 36
    • 0033844911 scopus 로고    scopus 로고
    • Cell cycle-dependent expression of mammalian E2-C regulated by the anaphase-promoting complex/cyclosome
    • A. Yamanaka, S. Hatakeyama, K. Kominami, M. Kitagawa, M. Matsumoto, and K. Nakayama Cell cycle-dependent expression of mammalian E2-C regulated by the anaphase-promoting complex/cyclosome Mol. Biol. Cell 11 2000 2821 2831
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2821-2831
    • Yamanaka, A.1    Hatakeyama, S.2    Kominami, K.3    Kitagawa, M.4    Matsumoto, M.5    Nakayama, K.6
  • 37
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATa2 repressor
    • P. Chen, P. Johnson, T. Sommer, S. Jentsch, and M. Hochstrasser Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATa2 repressor Cell 74 1993 357 369
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 38
    • 0030700576 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation: Reverse protein flow of no return
    • T. Sommer, and D.H. Wolf Endoplasmic reticulum degradation: reverse protein flow of no return FASEB J. 11 1997 1227 1233
    • (1997) FASEB J. , vol.11 , pp. 1227-1233
    • Sommer, T.1    Wolf, D.H.2
  • 39
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Mata2 repressor degradation
    • R. Swanson, M. Locher, and M. Hochstrasser A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Mata2 repressor degradation Genes Dev. 15 2001 2660 2674
    • (2001) Genes Dev. , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 40
    • 0037016754 scopus 로고    scopus 로고
    • The Neddi-conjugated ROC1-CUL1 core ubiquitin ligase utilizes Nedd8 charged surface residues for efficient polyubiquitin chain assembly catalyzed by Cdc34
    • K. Wu, A. Chen, P. Tan, and Z.-Q. Pan The Neddi-conjugated ROC1-CUL1 core ubiquitin ligase utilizes Nedd8 charged surface residues for efficient polyubiquitin chain assembly catalyzed by Cdc34 J. Biol. Chem. 277 2002 516 527
    • (2002) J. Biol. Chem. , vol.277 , pp. 516-527
    • Wu, K.1    Chen, A.2    Tan, P.3    Pan, Z.-Q.4
  • 43
    • 0033516511 scopus 로고    scopus 로고
    • Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution
    • T. Miura, W. Klaus, B. Gsell, C. Miyamoto, and H. Senn Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution J. Mol. Biol. 290 1999 213 228
    • (1999) J. Mol. Biol. , vol.290 , pp. 213-228
    • Miura, T.1    Klaus, W.2    Gsell, B.3    Miyamoto, C.4    Senn, H.5
  • 45
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • N. Zheng, P. Wang, P.D. Jeffrey, and N.P. Pavletich 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
  • 46
    • 0037470244 scopus 로고    scopus 로고
    • Protein-protein interactions in an E2-RING finger complex: Implications for ubiquitin-dependent DNA damage repair
    • H.D. Ulrich Protein-protein interactions in an E2-RING finger complex: implications for ubiquitin-dependent DNA damage repair J. Biol. Chem. 278 2003 7051 7058
    • (2003) J. Biol. Chem. , vol.278 , pp. 7051-7058
    • Ulrich, H.D.1
  • 47
    • 0035174874 scopus 로고    scopus 로고
    • Identification of molecular determinants required for interaction of ubiquitin-conjugating enzymes and RING finger proteins
    • G. Martinez-Noel, U. Muller, and K. Harbers Identification of molecular determinants required for interaction of ubiquitin-conjugating enzymes and RING finger proteins Eur. J. Biochem. 268 2001 5912 5919
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5912-5919
    • Martinez-Noel, G.1    Muller, U.2    Harbers, K.3
  • 48
    • 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
    • Y. Xie, and A. Varshavsky 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 1999 6832 6844
    • (1999) EMBO J. , vol.18 , pp. 6832-6844
    • Xie, Y.1    Varshavsky, A.2
  • 49
    • 0027316341 scopus 로고
    • N-recognin/Ubc2 interactions in the N-end rule pathway
    • K. Madura, R.J. Dohmen, and A. Varshavsky N-recognin/Ubc2 interactions in the N-end rule pathway J. Biol. Chem. 268 1993 12046 12054
    • (1993) J. Biol. Chem. , vol.268 , pp. 12046-12054
    • Madura, K.1    Dohmen, R.J.2    Varshavsky, A.3
  • 50
    • 0037033071 scopus 로고    scopus 로고
    • Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation
    • K.P. Bencsath, M.S. Podgorski, V.R. Pagala, C.A. Slaughter, and B.A. Schulman Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation J. Biol. Chem. 277 2002 47938 47945
    • (2002) J. Biol. Chem. , vol.277 , pp. 47938-47945
    • Bencsath, K.P.1    Podgorski, M.S.2    Pagala, V.R.3    Slaughter, C.A.4    Schulman, B.A.5
  • 51
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
    • V. Bernier-Villamor, D.A. Sampson, M.J. Matunis, and C.D. Lima Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1 Cell 108 2002 345 356
    • (2002) Cell , vol.108 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3    Lima, C.D.4
  • 52
    • 0035877693 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification
    • D.A. Sampson, M. Wang, and M.J. Matunis The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification J. Biol. Chem. 276 2001 21664 21669
    • (2001) J. Biol. Chem. , vol.276 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 53
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • R.M. Hofmann, and C.M. Pickart Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair Cell 96 1999 645 653
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 55
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitin chain assembly: Crystal structure of the Mms2/Ubc13 heterodimer
    • A.P. VanDemark, R.M. Hofmann, C. Tsui, C.M. Pickart, and C. Wolberger Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer Cell 105 2001 711 720
    • (2001) Cell , vol.105 , pp. 711-720
    • Vandemark, A.P.1    Hofmann, R.M.2    Tsui, C.3    Pickart, C.M.4    Wolberger, C.5
  • 56
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • L. Deng, C. Wang, E. Spencer, L. Yang, A. Braun, J. You, C. Slaughter, C. Pickart, and Z.J. Chen Activation of the IkB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain Cell 103 2000 351 361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 57
    • 0035955731 scopus 로고    scopus 로고
    • Non-covalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for the Ubc13-mediated poly-ubiquitination
    • S. McKenna, L. Spyracopoulos, T. Moraes, L. Pastushok, C. Ptak, W. Xiao, and M.J. Ellison Non-covalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for the Ubc13-mediated poly-ubiquitination J. Biol. Chem. 276 2001 40120 40126
    • (2001) J. Biol. Chem. , vol.276 , pp. 40120-40126
    • McKenna, S.1    Spyracopoulos, L.2    Moraes, T.3    Pastushok, L.4    Ptak, C.5    Xiao, W.6    Ellison, M.J.7
  • 58
    • 0038579251 scopus 로고    scopus 로고
    • An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2-Ubc13: The structural basis for lysine 63 chain synthesis
    • S. McKenna, T. Moraes, L. Pastushok, C. Ptak, W. Xiao, L. Spyracopoulos, and M.J. Ellison An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2-Ubc13: the structural basis for lysine 63 chain synthesis J. Biol. Chem. 278 2003 13151 13158
    • (2003) J. Biol. Chem. , vol.278 , pp. 13151-13158
    • McKenna, S.1    Moraes, T.2    Pastushok, L.3    Ptak, C.4    Xiao, W.5    Spyracopoulos, L.6    Ellison, M.J.7
  • 60
    • 0037207126 scopus 로고    scopus 로고
    • The catalytic cycle of biosynthetic thiolase: A conformational journey of an acetyl group through four binding modes and two oxyanion holes
    • P. Kursula, J. Ojala, A.-M. Lambeir, and R.K. Wierenga The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes Biochemistry 41 2002 15543 15556
    • (2002) Biochemistry , vol.41 , pp. 15543-15556
    • Kursula, P.1    Ojala, J.2    Lambeir, A.-M.3    Wierenga, R.K.4
  • 61
    • 0024280501 scopus 로고
    • Dissecting the catalytic triad of a serine protease
    • P. Carter, and J.A. Wells Dissecting the catalytic triad of a serine protease Nature 332 1988 564 568
    • (1988) Nature , vol.332 , pp. 564-568
    • Carter, P.1    Wells, J.A.2
  • 62
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • M. Hu, P. Li, M. Li, W. Li, T. Yao, J.-W. Wu, W. Gu, R.E. Cohen, and Y. Shi Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde Cell 111 2002 1041 1054
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.-W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 64
    • 0038128204 scopus 로고    scopus 로고
    • High-throughput immunoblotting: Ubiquitin-like protein ISG15 modifies key regulators of signal transduction
    • M.P. Malakhov, K.I. Kim, O.A. Malakhova, B.S. Jacobs, E.C. Borden, and D.-E. Zhang High-throughput immunoblotting: ubiquitin-like protein ISG15 modifies key regulators of signal transduction J. Biol. Chem. 278 2003 16608 16613
    • (2003) J. Biol. Chem. , vol.278 , pp. 16608-16613
    • Malakhov, M.P.1    Kim, K.I.2    Malakhova, O.A.3    Jacobs, B.S.4    Borden, E.C.5    Zhang, D.-E.6
  • 65
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • E.S. Johnson, and A.A. Gupta An E3-like factor that promotes SUMO conjugation to the yeast septins Cell 106 2001 735 744
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 66
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • A. Hershko, H. Heller, S. Elias, and A. Ciechanover Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown J. Biol. Chem. 258 1983 8206 8214
    • (1983) J. Biol. Chem. , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 67
    • 2442529664 scopus 로고    scopus 로고
    • Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family
    • L. Pintard, A. Willems, and M. Peter Cullin-based ubiquitin ligases: Cul3-BTB complexes join the family EMBO J. 23 2004 1681 1687
    • (2004) EMBO J. , vol.23 , pp. 1681-1687
    • Pintard, L.1    Willems, A.2    Peter, M.3
  • 68
    • 0033279836 scopus 로고    scopus 로고
    • SCF and cullin/RING H2-based ubiquitin ligases
    • R.J. Deshaies SCF and cullin/RING H2-based ubiquitin ligases Annu. Rev. Cell Dev. Biol. 15 1999 435 467
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 69
    • 0034602928 scopus 로고    scopus 로고
    • RING domains: Master builders of molecular scaffolds?
    • K.L. Borden RING domains: master builders of molecular scaffolds? J. Mol. Biol. 295 2000 1103 1112
    • (2000) J. Mol. Biol. , vol.295 , pp. 1103-1112
    • Borden, K.L.1
  • 75
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • C.A.P. Joazeiro, and A.M. Weissman RING finger proteins: mediators of ubiquitin ligase activity Cell 102 2000 549 552
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.P.1    Weissman, A.M.2
  • 76
    • 0037462424 scopus 로고    scopus 로고
    • Structural basis for phosphodependent substrate selection and orientation by the SDFCdc4 ubiquitin ligase
    • S. Orlicky, X. Tang, A. Willems, M. Tyers, and F. Sicheri Structural basis for phosphodependent substrate selection and orientation by the SDFCdc4 ubiquitin ligase Cell 112 2003 243 256
    • (2003) Cell , vol.112 , pp. 243-256
    • Orlicky, S.1    Tang, X.2    Willems, A.3    Tyers, M.4    Sicheri, F.5
  • 79
    • 0037756792 scopus 로고    scopus 로고
    • Context of multiubiquitin chain attachment influences the rate of Sic1 degradation
    • M.D. Petroski, and R.J. Deshaies Context of multiubiquitin chain attachment influences the rate of Sic1 degradation Mol. Cell 11 2003 1435 1444
    • (2003) Mol. Cell , vol.11 , pp. 1435-1444
    • Petroski, M.D.1    Deshaies, R.J.2
  • 81
    • 0035805582 scopus 로고    scopus 로고
    • The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation
    • R. Hashizume, M. Fukuda, I. Maeda, H. Nishikawa, D. Oyake, Y. Yabuki, H. Ogata, and T. Ohta The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation J. Biol. Chem. 276 2001 14537 14540
    • (2001) J. Biol. Chem. , vol.276 , pp. 14537-14540
    • Hashizume, R.1    Fukuda, M.2    Maeda, I.3    Nishikawa, H.4    Oyake, D.5    Yabuki, Y.6    Ogata, H.7    Ohta, T.8
  • 82
    • 0037088624 scopus 로고    scopus 로고
    • Identification of residues required for the interaction of BARD1 with BRCA1
    • J.R. Morris, N.H. Keep, and E. Solomon Identification of residues required for the interaction of BARD1 with BRCA1 J. Biol. Chem. 277 2002 9382 9386
    • (2002) J. Biol. Chem. , vol.277 , pp. 9382-9386
    • Morris, J.R.1    Keep, N.H.2    Solomon, E.3
  • 83
    • 0033120027 scopus 로고    scopus 로고
    • ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity
    • T. Ohta, J.J. Michel, A.J. Schottelius, and Y. Xiong ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity Mol. Cell 3 1999 535 541
    • (1999) Mol. Cell , vol.3 , pp. 535-541
    • Ohta, T.1    Michel, J.J.2    Schottelius, A.J.3    Xiong, Y.4
  • 84
    • 0033120593 scopus 로고    scopus 로고
    • Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of IkBa
    • P. Tan, S.Y. Fuchs, A. Chen, K. Wu, C. Gomez, Z. Ronai, and Z.-Q. Pan Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of IkBa Mol. Cell 3 1999 527 533
    • (1999) Mol. Cell , vol.3 , pp. 527-533
    • Tan, P.1    Fuchs, S.Y.2    Chen, A.3    Wu, K.4    Gomez, C.5    Ronai, Z.6    Pan, Z.-Q.7
  • 85
    • 0036284778 scopus 로고    scopus 로고
    • The anaphase-promoting complex: Proteolysis in mitosis and beyond
    • J.M. Peters The anaphase-promoting complex: proteolysis in mitosis and beyond Mol. Cell 9 2002 931 943
    • (2002) Mol. Cell , vol.9 , pp. 931-943
    • Peters, J.M.1
  • 87
    • 0035661566 scopus 로고    scopus 로고
    • APC2 cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex
    • Z. Tang, B. Li, R. Bharadwaj, H. Zhu, E. Ozkan, K. Hakala, J. Deisenhofer, and H. Yu APC2 cullin protein and APC11 RING protein comprise the minimal ubiquitin ligase module of the anaphase-promoting complex Mol. Biol. Cell 12 2001 3839 3851
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3839-3851
    • Tang, Z.1    Li, B.2    Bharadwaj, R.3    Zhu, H.4    Ozkan, E.5    Hakala, K.6    Deisenhofer, J.7    Yu, H.8
  • 89
    • 0032727343 scopus 로고    scopus 로고
    • The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2
    • T. Kamura, M.N. Conrad, Q. Yan, R.C. Conaway, and J.W. Conaway The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2 Genes Dev. 13 1999 2928 2933
    • (1999) Genes Dev. , vol.13 , pp. 2928-2933
    • Kamura, T.1    Conrad, M.N.2    Yan, Q.3    Conaway, R.C.4    Conaway, J.W.5
  • 90
    • 0033545860 scopus 로고    scopus 로고
    • Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function
    • D. Liakopoulos, T. Busgen, A. Brychzy, A. Jentsch, and A. Pause Conjugation of the ubiquitin-like protein NEDD8 to cullin-2 is linked to von Hippel-Lindau tumor suppressor function Proc. Natl. Acad. Sci. U. S. A. 11 1999 5510 5515
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.11 , pp. 5510-5515
    • Liakopoulos, D.1    Busgen, T.2    Brychzy, A.3    Jentsch, A.4    Pause, A.5
  • 92
    • 0034671463 scopus 로고    scopus 로고
    • Structure of the PHD zinc finger from human Williams-Beuren Syndrome transcription factor
    • J. Pascual, M. Martinez-Yamout, H.J. Dyson, and P.E. Wright Structure of the PHD zinc finger from human Williams-Beuren Syndrome transcription factor J. Mol. Biol. 304 2000 723 729
    • (2000) J. Mol. Biol. , vol.304 , pp. 723-729
    • Pascual, J.1    Martinez-Yamout, M.2    Dyson, H.J.3    Wright, P.E.4
  • 93
    • 0035863152 scopus 로고    scopus 로고
    • Solution structure of the PHD domain from the KAP-1 corepressor: Structural determinants for PHD, RING and LIM zinc-binding domains
    • A.D. Capili, D.C. Schultz, F.J. Rauscher, and K.L.B. Borden Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domains EMBO J. 20 2001 165 177
    • (2001) EMBO J. , vol.20 , pp. 165-177
    • Capili, A.D.1    Schultz, D.C.2    Rauscher, F.J.3    Borden, K.L.B.4
  • 94
    • 0037972167 scopus 로고    scopus 로고
    • Scores of RINGS but no PHDs in ubiquitin signaling
    • L. Aravind, L.M. Iyer, and E.V. Koonin Scores of RINGS but no PHDs in ubiquitin signaling Cell Cycle 2 2003 123 126
    • (2003) Cell Cycle , vol.2 , pp. 123-126
    • Aravind, L.1    Iyer, L.M.2    Koonin, E.V.3
  • 95
    • 0035945349 scopus 로고    scopus 로고
    • A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition
    • L. Coscoy, D.J. Sanchez, and D. Ganem A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition J. Cell Biol. 155 2001 1265 1273
    • (2001) J. Cell Biol. , vol.155 , pp. 1265-1273
    • Coscoy, L.1    Sanchez, D.J.2    Ganem, D.3
  • 96
    • 0037093467 scopus 로고    scopus 로고
    • Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation
    • E.W. Hewitt, L. Duncan, D. Mufti, J. Baker, P.G. Stevenson, and P.J. Lehner Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation EMBO J. 21 2002 2418 2429
    • (2002) EMBO J. , vol.21 , pp. 2418-2429
    • Hewitt, E.W.1    Duncan, L.2    Mufti, D.3    Baker, J.4    Stevenson, P.G.5    Lehner, P.J.6
  • 97
    • 0037213013 scopus 로고    scopus 로고
    • PHD domains and E3 ubiquitin ligases: Viruses make the connection
    • L. Coscoy, and D. Ganem PHD domains and E3 ubiquitin ligases: viruses make the connection Trends Cell Biol. 13 2003 7 12
    • (2003) Trends Cell Biol. , vol.13 , pp. 7-12
    • Coscoy, L.1    Ganem, D.2
  • 98
    • 0037155246 scopus 로고    scopus 로고
    • Functional organization of MIR2, a novel viral regulator of selective endocytosis
    • D.J. Sanchez, L. Coscoy, and D. Ganem Functional organization of MIR2, a novel viral regulator of selective endocytosis J. Biol. Chem. 277 2002 6124 6130
    • (2002) J. Biol. Chem. , vol.277 , pp. 6124-6130
    • Sanchez, D.J.1    Coscoy, L.2    Ganem, D.3
  • 99
    • 0036279167 scopus 로고    scopus 로고
    • The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2
    • Z. Lu, S. Xu, C. Joazeiro, M.H. Cobb, and T. Hunter The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2 Mol. Cell 9 2002 945 956
    • (2002) Mol. Cell , vol.9 , pp. 945-956
    • Lu, Z.1    Xu, S.2    Joazeiro, C.3    Cobb, M.H.4    Hunter, T.5
  • 100
    • 0035979738 scopus 로고    scopus 로고
    • Regulation of transcriptional activation domain function by ubiquitin
    • S.E. Salghetti, A.A. Caudy, J.G. Chenoweth, and W.P. Tansey Regulation of transcriptional activation domain function by ubiquitin Science 293 2001 1651 1653
    • (2001) Science , vol.293 , pp. 1651-1653
    • Salghetti, S.E.1    Caudy, A.A.2    Chenoweth, J.G.3    Tansey, W.P.4
  • 101
    • 0037123605 scopus 로고    scopus 로고
    • Emerging roles of ubiquitin in transcription regulation
    • R.C. Conaway, C.S. Brower, and J.W. Conaway Emerging roles of ubiquitin in transcription regulation Science 296 2002 1254 1258
    • (2002) Science , vol.296 , pp. 1254-1258
    • Conaway, R.C.1    Brower, C.S.2    Conaway, J.W.3
  • 102
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • M. Koegl, T. Hoppe, S. Schlenker, H.D. Ulrich, T.U. Mayer, and S. Jentsch A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly Cell 96 1999 635 644
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 103
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • Y. Imai, M. Soda, S. Hatakeyama, T. Akagi, T. Hasikawa, K.-I. Nakayama, and R. Takahashi CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity Mol. Cell 10 2002 55 67
    • (2002) Mol. Cell , vol.10 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hasikawa, T.5    Nakayama, K.-I.6    Takahashi, R.7
  • 104
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger-a common domain in ubiquitination
    • L. Aravind, and E.V. Koonin The U box is a modified RING finger-a common domain in ubiquitination Curr. Biol. 10 2000 R124 R132
    • (2000) Curr. Biol. , vol.10
    • Aravind, L.1    Koonin, E.V.2
  • 106
    • 0035375052 scopus 로고    scopus 로고
    • Interaction of the RING finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes
    • E. Pringa, G. Martinez-Noel, U. Muller, and K. Harbers Interaction of the RING finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes J. Biol. Chem. 276 2001 19617 19623
    • (2001) J. Biol. Chem. , vol.276 , pp. 19617-19623
    • Pringa, E.1    Martinez-Noel, G.2    Muller, U.3    Harbers, K.4
  • 107
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • S. Murata, Y. Minami, M. Minami, T. Chiba, and K. Tanaka CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein EMBO Rep. 2 2001 1133 1138
    • (2001) EMBO Rep. , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 109
    • 0031901697 scopus 로고    scopus 로고
    • Snt309p, a component of the Prp19p-associated complex that interacts with prp19p and associates with the spliceosome simultaneously with or immediately after dissociation of U4 in the same manner of Prp19p
    • H.R. Chen, S.P. Jan, T.Y. Tsao, Y.J. Sheu, J. Banroques, and S.C. Cheng Snt309p, a component of the Prp19p-associated complex that interacts with prp19p and associates with the spliceosome simultaneously with or immediately after dissociation of U4 in the same manner of Prp19p Mol. Cell. Biol. 18 1998 2196 2204
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2196-2204
    • Chen, H.R.1    Jan, S.P.2    Tsao, T.Y.3    Sheu, Y.J.4    Banroques, J.5    Cheng, S.C.6
  • 111
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • D.M. Cyr, J. Hohfeld, and C. Patterson Protein quality control: U-box-containing E3 ubiquitin ligases join the fold Trends Biochem. Sci. 27 2002 368 375
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 112
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • G.C. Meachem, C. Patterson, W. Zhang, J.M. Younger, and D.M. Cyr The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation Nat. Cell Biol. 3 2001 100 105
    • (2001) Nat. Cell Biol. , vol.3 , pp. 100-105
    • Meachem, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 114
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • H. Shimura, D. Schwartz, S.P. Gygi, and K.S. Kosik CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival J. Biol. Chem. 279 2004 4869 4876
    • (2004) J. Biol. Chem. , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 116
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • M. Scheffner, U. Nuber, and J.M. Huibregtse Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade Nature 373 1995 81 83
    • (1995) Nature , vol.373 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 117
    • 0028674213 scopus 로고
    • E6-AP directs the HPV E6-dependent inactivation of p53 and is representative of a family of structurally and functionally related proteins
    • J.M. Huibregtse, M. Scheffner, and P.M. Howley E6-AP directs the HPV E6-dependent inactivation of p53 and is representative of a family of structurally and functionally related proteins Cold Spring Harbor Symp. Quant. Biol. 59 1994 237 245
    • (1994) Cold Spring Harbor Symp. Quant. Biol. , vol.59 , pp. 237-245
    • Huibregtse, J.M.1    Scheffner, M.2    Howley, P.M.3
  • 118
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • J.M. Huibregtse, M. Scheffner, S. Beaudenon, and P.M. Howley A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase Proc. Natl. Acad. Sci. U. S. A. 92 1995 2563 2567
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 122
    • 0035966288 scopus 로고    scopus 로고
    • Multisite phosphorylation and the countdown to S phase
    • R.J. Deshaies, and J.E. Ferrell Multisite phosphorylation and the countdown to S phase Cell 107 2001 819 822
    • (2001) Cell , vol.107 , pp. 819-822
    • Deshaies, R.J.1    Ferrell, J.E.2
  • 124
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • J.D. Laney, and M. Hochstrasser Substrate targeting in the ubiquitin system Cell 97 1999 427 430
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 125
    • 0037307858 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein: New insights into oxygen sensing and cancer
    • W. Kim, and W.G. Kaelin The von Hippel-Lindau tumor suppressor protein: new insights into oxygen sensing and cancer Curr. Opin. Genet. Dev. 13 2003 55 60
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 55-60
    • Kim, W.1    Kaelin, W.G.2
  • 126
    • 2342597973 scopus 로고    scopus 로고
    • Inhibition of HIF2α is sufficient to suppress pVHL-defective tumor growth
    • K. Kondo, W.Y. Kim, M. Lechpammer, and W.G. Kaelin Inhibition of HIF2α is sufficient to suppress pVHL-defective tumor growth PLoS Biol. 1 2003 439 444
    • (2003) PLoS Biol. , vol.1 , pp. 439-444
    • Kondo, K.1    Kim, W.Y.2    Lechpammer, M.3    Kaelin, W.G.4
  • 127
    • 0035859692 scopus 로고    scopus 로고
    • HIF-1a binding to VHL is regulated by stimulus-sensitive proline hydroxylation
    • F. Yu, S.B. White, Q. Zhao, and F.S. Lee HIF-1a binding to VHL is regulated by stimulus-sensitive proline hydroxylation Proc. Natl. Acad. Sci. U. S. A. 98 2001 9630 9635
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9630-9635
    • Yu, F.1    White, S.B.2    Zhao, Q.3    Lee, F.S.4
  • 128
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation
    • N. Masson, C. William, P.H. Maxwell, C.W. Pugh, and P.J. Ratcliffe Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation EMBO J. 20 2001 5197 5206
    • (2001) EMBO J. , vol.20 , pp. 5197-5206
    • Masson, N.1    William, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 129
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: Implications for VHL tumor suppressor function
    • C.E. Stebbins, W.G. Kaelin, and N.P. Pavletich Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function Science 284 1999 455 461
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin, W.G.2    Pavletich, N.P.3
  • 130
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1a-pVHL complex: Hydroxyproline recognition in signaling
    • J.-H. Min, H. Yang, M. Ivan, F. Gertler, W.G. Kaelin, and N.P. Pavletich Structure of an HIF-1a-pVHL complex: hydroxyproline recognition in signaling Science 296 2002 1886 1889
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.-H.1    Yang, H.2    Ivan, M.3    Gertler, F.4    Kaelin, W.G.5    Pavletich, N.P.6
  • 133
    • 0030612012 scopus 로고    scopus 로고
    • Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase
    • R. Verma, R.S. Annan, M.J. Huddleston, S.A. Carr, G. Reynard, and R.J. Deshaies Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase Science 278 1997 455 460
    • (1997) Science , vol.278 , pp. 455-460
    • Verma, R.1    Annan, R.S.2    Huddleston, M.J.3    Carr, S.A.4    Reynard, G.5    Deshaies, R.J.6
  • 134
    • 0141838136 scopus 로고    scopus 로고
    • Mathematical modeling suggests cooperative interactions between a disordered polyvalent ligand and a receptor site
    • P. Klein, T. Pawson, and M. Tyers Mathematical modeling suggests cooperative interactions between a disordered polyvalent ligand and a receptor site Curr. Biol. 13 2003 1669 1678
    • (2003) Curr. Biol. , vol.13 , pp. 1669-1678
    • Klein, P.1    Pawson, T.2    Tyers, M.3
  • 135
    • 1942437663 scopus 로고    scopus 로고
    • Regulating the p53 system through ubiquitination
    • Y. Yang, C.-C.H. Li, and A.M. Weissman Regulating the p53 system through ubiquitination Oncogene 23 2004 2096 2106
    • (2004) Oncogene , vol.23 , pp. 2096-2106
    • Yang, Y.1    Li, C.-C.H.2    Weissman, A.M.3
  • 136
    • 0030575937 scopus 로고    scopus 로고
    • Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain
    • P.H. Kussie, S. Gorina, V. Marechal, B. Elenbaas, J. Moreau, and N.P. Pavletich Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain Science 274 1996 948 953
    • (1996) Science , vol.274 , pp. 948-953
    • Kussie, P.H.1    Gorina, S.2    Marechal, V.3    Elenbaas, B.4    Moreau, J.5    Pavletich, N.P.6
  • 138
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 a resolution
    • S. Vijay-Kumar, C.E. Bugg, and W.J. Cook Structure of ubiquitin refined at 1.8 A resolution J. Mol. Biol. 194 1987 531 544
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 140
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 141
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster 3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.