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Volumn 5, Issue 9, 2004, Pages 739-751

The SCF ubiquitin ligase: Insights into a molecular machine

Author keywords

[No Author keywords available]

Indexed keywords

CUL1 PROTEIN; F BOX PROTEIN; PROTEIN; SCF PROTEIN; SKP1 PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 4444318673     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1471     Document Type: Review
Times cited : (923)

References (128)
  • 1
    • 1842538779 scopus 로고    scopus 로고
    • Oncogenic aberrations of cullin-dependent ubiquitin ligases
    • Guardavaccaro, D. & Pagano, M. Oncogenic aberrations of cullin-dependent ubiquitin ligases. Oncogene 23, 2037-2049(2004).
    • (2004) Oncogene , vol.23 , pp. 2037-2049
    • Guardavaccaro, D.1    Pagano, M.2
  • 2
    • 0027960938 scopus 로고
    • A novel cyclin gene (CCNF) in the region of the polycysti kidney disease gene (PKD1)
    • Kraus. B, et al. A novel cyclin gene (CCNF) in the region of the polycysti kidney disease gene (PKD1). Genomics 24, 27-33 (1994).
    • (1994) Genomics , vol.24 , pp. 27-33
    • Kraus, B.1
  • 3
    • 0842324788 scopus 로고    scopus 로고
    • Recycling the cell cycle: Cyclins revisited
    • Murray, A. W. Recycling the cell cycle: cyclins revisited. Cell 116, 221-234 (2004).
    • (2004) Cell , vol.116 , pp. 221-234
    • Murray, A.W.1
  • 5
    • 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). Seminal paper that identified and assigned a function to the F-box domain.
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1
  • 6
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • Feldman, R. M., Correll, C. C., Kaplan, K. B. & Deshaies, R. J. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91, 221-230 (1997). References 6 and 7 were the first studies to put the data together to identify the SCF ubiquitin ligase as a functional entity.
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 7
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J. & Harper, J. W. F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91, 209-219 (1997).
    • (1997) Cell , vol.91 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 8
    • 0033592702 scopus 로고    scopus 로고
    • Identification of a family of human F-box proteins
    • Cenciarelli, C. et al. Identification of a family of human F-box proteins. Curr. Biol. 9, 1177-1179 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 1177-1179
    • Cenciarelli, C.1
  • 10
    • 0033133919 scopus 로고    scopus 로고
    • The WD repeat: A common architecture for diverse functions
    • Smith, T. F., Gatatzes, C., Saxena, K. & Neer, E. J. The WD repeat: a common architecture for diverse functions. Trends Biochem. Sci. 24, 181-185 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 181-185
    • Smith, T.F.1    Gatatzes, C.2    Saxena, K.3    Neer, E.J.4
  • 11
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe, B. & Kajava, A. V. The leucine-rich repeat as a protein recognition motif. Curr. 0pin. Struct. Biol. 11, 725-732 (2001).
    • (2001) Curr. 0pin. Struct. Biol. , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 13
    • 18444413218 scopus 로고    scopus 로고
    • E3 ubiquitin ligase that recognizes sugar chains
    • Yoshida, Y. et al. E3 ubiquitin ligase that recognizes sugar chains. Nature 418, 438-442 (2002).
    • (2002) Nature , vol.418 , pp. 438-442
    • Yoshida, Y.1
  • 14
    • 0242321836 scopus 로고    scopus 로고
    • Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains
    • Yoshida, Y. et al. Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains. J. Biol. Chem. 278, 43877-43884 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 43877-43884
    • Yoshida, Y.1
  • 16
    • 0035370009 scopus 로고    scopus 로고
    • Emi1 is a mitotic regulator that interacts with Cdc20 and inhibits the anaphase promoting complex
    • Reimann, J. D. et al. Emi1 is a mitotic regulator that interacts with Cdc20 and inhibits the anaphase promoting complex. Cell 105, 645-855 (2001).
    • (2001) Cell , vol.105 , pp. 645-855
    • Reimann, J.D.1
  • 17
    • 0034175809 scopus 로고    scopus 로고
    • Proviral insertions in the zebrafish hagoromo gene, encoding an F-box/WD40-repeat protein, cause stripe pattern anomalies
    • Kawakami, K. et al. Proviral insertions in the zebrafish hagoromo gene, encoding an F-box/WD40-repeat protein, cause stripe pattern anomalies. Curr. Biol. 10, 463-466 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 463-466
    • Kawakami, K.1
  • 18
    • 0032860480 scopus 로고    scopus 로고
    • A novel member of the F-box/WD40 gene family, encoding dactylin, is disrupted in the mouse dactytaplasia mutant
    • Sidow, A. et al. A novel member of the F-box/WD40 gene family, encoding dactylin, is disrupted in the mouse dactytaplasia mutant. Nature Genet 23, 104-107 (1999).
    • (1999) Nature Genet , vol.23 , pp. 104-107
    • Sidow, A.1
  • 19
    • 0141921323 scopus 로고    scopus 로고
    • Spilt hand foot malformation is associated with a reduced level of Dactylin gene expression
    • Basel, D., DePaepe, A., Kilpatrick, M. W. & Tsipouras, P. Spilt hand foot malformation is associated with a reduced level of Dactylin gene expression. Clin. Genet. 64, 350-354 (2003).
    • (2003) Clin. Genet. , vol.64 , pp. 350-354
    • Basel, D.1    DePaepe, A.2    Kilpatrick, M.W.3    Tsipouras, P.4
  • 20
    • 0033926317 scopus 로고    scopus 로고
    • Split-hand/split-foot malformation is caused by mutations in the p63 gene on 3q27
    • Ianakiev, P. et al. Split-hand/split-foot malformation is caused by mutations in the p63 gene on 3q27. Am. J. Hum. Genet. 67, 59-66 (2000).
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 59-66
    • Ianakiev, P.1
  • 21
    • 0037168527 scopus 로고    scopus 로고
    • CUL7: A DOC domain-containing cullin selectively binds Skp1-Fbx29 to form an SCF-like complex
    • Dias, D. C., Dolios, G., Wang, R. & Pan, Z. Q. CUL7: A DOC domain-containing cullin selectively binds Skp1-Fbx29 to form an SCF-like complex. Proc. Natl Acad. Sci. USA 99, 16601-16606 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16601-16606
    • Dias, D.C.1    Dolios, G.2    Wang, R.3    Pan, Z.Q.4
  • 22
    • 0042191755 scopus 로고    scopus 로고
    • Targeted disruption of p185/Cul7 gene results in abnormal vascular morphogenesis
    • Arai, T. et al. Targeted disruption of p185/Cul7 gene results in abnormal vascular morphogenesis. Proc. Natl Acad. Sci. USA 100, 9855-9860 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9855-9860
    • Arai, T.1
  • 23
    • 34247591787 scopus 로고    scopus 로고
    • Molecular profile of synovial fibroblasts in rheumatoid arthritis depends on the stage of proliferation
    • Masuda, K. et al. Molecular profile of synovial fibroblasts in rheumatoid arthritis depends on the stage of proliferation. Arthritis Res. 4, R8 (2002).
    • (2002) Arthritis Res. , vol.4
    • Masuda, K.1
  • 24
    • 0037648469 scopus 로고    scopus 로고
    • The small heat-shock protein αB-crystallin promotes FBX4-dependent ubiquitination
    • den Engelsman, J., Keijsers, V., de Jong, W. W. & Boelens, W. C. The small heat-shock protein αB-crystallin promotes FBX4-dependent ubiquitination. J. Biol. Chem. 278, 4699-4704 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 4699-4704
    • Den Engelsman, J.1    Keijsers, V.2    De Jong, W.W.3    Boelens, W.C.4
  • 25
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • Sandri, M. et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell 117, 399-412 (2004).
    • (2004) Cell , vol.117 , pp. 399-412
    • Sandri, M.1
  • 26
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • Gomes, M. D., Lecker, S. H., Jagoe, R. T., Navon, A. & Goldberg, A. L. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc. Natl Acad. Sci. USA 98, 14440-14445 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3    Navon, A.4    Goldberg, A.L.5
  • 27
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine, S. C. et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 294, 1704-1708 (2001).
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1
  • 28
    • 0036789555 scopus 로고    scopus 로고
    • The spindle checkpoint: Structural insights into dynamic signalling
    • Musacchio, A. & Hardwick, K. G. The spindle checkpoint: structural insights into dynamic signalling. Nature Rev. Mol. Cell Biol. 3, 731-741 (2002).
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 731-741
    • Musacchio, A.1    Hardwick, K.G.2
  • 29
    • 0033567387 scopus 로고    scopus 로고
    • Whose end is destruction: Cell division and the anaphase-promoting complex
    • Zachariae, W. & Nasmyth, K. Whose end is destruction: cell division and the anaphase-promoting complex. Genes Dev. 13, 2039-2058 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2039-2058
    • Zachariae, W.1    Nasmyth, K.2
  • 30
    • 0036284778 scopus 로고    scopus 로고
    • The anaphase-promoting complex: Proteolysis in mitosis and beyond
    • Peters, J. M. The anaphase-promoting complex: proteolysis in mitosis and beyond. Mol. Cell 9, 931-943 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 931-943
    • Peters, J.M.1
  • 31
    • 0344982141 scopus 로고    scopus 로고
    • Dynamics of the cell cycle: Checkpoints, sizers, and timers
    • Qu, Z., MacLellan, W. R. & Weiss, J. N. Dynamics of the cell cycle: checkpoints, sizers, and timers. Biophys. J. 85, 3600-3611 (2003).
    • (2003) Biophys. J. , vol.85 , pp. 3600-3611
    • Qu, Z.1    MacLellan, W.R.2    Weiss, J.N.3
  • 32
    • 2342650733 scopus 로고    scopus 로고
    • Degradation of p27 mediated by Skp2 is required for progression to mitosis
    • -/- phenotype is rescued by p27 deficiency. It also shows that p27 inhibits Cdk1 as well as Cdk2.
    • (2004) Dev. Cell , vol.6 , pp. 661-672
    • Nakayama, K.1
  • 33
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibtors: Positive and negative regulators of G1-phase progression
    • Sherr, C. J. & Roberts, J. M. CDK inhibtors: positive and negative regulators of G1-phase progression. Genes Dev. 13, 1501-1512 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 34
    • 0033174155 scopus 로고    scopus 로고
    • Kip1 meets SKP2: New links in cell-cycle control
    • Amati, B. & Vlach, J. Kip1 meets SKP2: new links in cell-cycle control. Nature Cell Biol. 1, E91-E93 (1999).
    • (1999) Nature Cell Biol. , vol.1
    • Amati, B.1    Vlach, J.2
  • 35
    • 0033176887 scopus 로고    scopus 로고
    • Skp2 is required for the ubiquitin-mediated degradation of the Cdk-inhibitor p27
    • Carrano, A. C., Eytan, E., Hershko, A. & Pagano, M. Skp2 is required for the ubiquitin-mediated degradation of the Cdk-inhibitor p27. Nature Cell Biol. 1, 193-199 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 36
    • 0034595292 scopus 로고    scopus 로고
    • Kip1, potyploidy and centrosomeoverduplication
    • Kip1, potyploidy and centrosomeoverduplication. EMBO J. 19, 2069-2081 (2000).
    • (2000) EMBO J. , vol.19 , pp. 2069-2081
    • Nakayama, K.1
  • 38
    • 0033174070 scopus 로고    scopus 로고
    • Kip1 degradation and induces S phase in quiescent cells
    • Kip1 degradation and induces S phase in quiescent cells. Nature Cell Biol. 1, 207-214 (1999).
    • (1999) Nature Cell Biol. , vol.1 , pp. 207-214
    • Sutterluty, H.1
  • 40
    • 0038152755 scopus 로고    scopus 로고
    • Cip1 in S phase
    • Cip1 in S phase. J. Biol. Chem. 278, 25752-25757 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 25752-25757
    • Bomstein, G.1
  • 42
    • 1642399624 scopus 로고    scopus 로고
    • Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex
    • Wei, W. et al. Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex. Nature 428, 194-198 (2004).
    • (2004) Nature , vol.428 , pp. 194-198
    • Wei, W.1
  • 43
    • 0037119999 scopus 로고    scopus 로고
    • Dual mode of degradation of Cdc25 A phosphatase
    • Donzeili, M. et al. Dual mode of degradation of Cdc25 A phosphatase. EMBO J. 21, 4875-4884 (2002).
    • (2002) EMBO J. , vol.21 , pp. 4875-4884
    • Donzeili, M.1
  • 44
    • 0347128199 scopus 로고    scopus 로고
    • Loss of the anaphase-promoting complex in quiescent cells causes unscheduled hepatocyte proliferation
    • Wirth, K. G. et al. Loss of the anaphase-promoting complex in quiescent cells causes unscheduled hepatocyte proliferation. Genes Dev. 18, 88-98 (2004). Describes and confirms the phenotype of APC/C disruption.
    • (2004) Genes Dev. , vol.18 , pp. 88-98
    • Wirth, K.G.1
  • 45
    • 0035893917 scopus 로고    scopus 로고
    • Emi1 regulates the anaphase-promoting complex by a different mechanism than Mad2 proteins
    • Reimann, J. D., Gardner, B. E., Margottin-Goguet, F. & Jackson, P. K. Emi1 regulates the anaphase-promoting complex by a different mechanism than Mad2 proteins. Genes Dev. 15, 3278-3285 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 3278-3285
    • Reimann, J.D.1    Gardner, B.E.2    Margottin-Goguet, F.3    Jackson, P.K.4
  • 46
    • 0242497228 scopus 로고    scopus 로고
    • Degradation of Cdc25A by β-TrCP during S phase and in response to DNA damage
    • Busino, L. et al. Degradation of Cdc25A by β-TrCP during S phase and in response to DNA damage. Nature 426, 87-91 (2003).
    • (2003) Nature , vol.426 , pp. 87-91
    • Busino, L.1
  • 47
    • 0347361537 scopus 로고    scopus 로고
    • SCFβ-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase
    • Jin, J. et al. SCFβ-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase. Genes Dev. 17, 3062-3074 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 3062-3074
    • Jin, J.1
  • 48
    • 0035812709 scopus 로고    scopus 로고
    • Fbw7 ubiquitin ligase
    • Fbw7 ubiquitin ligase. Science 294, 173-177 (2001).
    • (2001) Science , vol.294 , pp. 173-177
    • Koepp, D.M.1
  • 49
    • 0035921928 scopus 로고    scopus 로고
    • Archipelago regulates cyclin E levels in Drosophila and is mutated in human cancer cell lines
    • Moberg, K. H., Bell, D. W., Wahrer, D. C., Haber, D. A. & Hariharan, I. K. Archipelago regulates cyclin E levels in Drosophila and is mutated in human cancer cell lines. Nature 413, 311-316 (2001).
    • (2001) Nature , vol.413 , pp. 311-316
    • Moberg, K.H.1    Bell, D.W.2    Wahrer, D.C.3    Haber, D.A.4    Hariharan, I.K.5
  • 50
    • 0035921849 scopus 로고    scopus 로고
    • Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line
    • Strohmaier, H. et al. Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature 413, 316-322 (2001).
    • (2001) Nature , vol.413 , pp. 316-322
    • Strohmaier, H.1
  • 52
    • 0037418836 scopus 로고    scopus 로고
    • Tome-1, a trigger of mitotic entry, is degraded during G1 via the APC
    • Ayad, N. G. et al. Tome-1, a trigger of mitotic entry, is degraded during G1 via the APC. Cell 113, 101-113 (2003).
    • (2003) Cell , vol.113 , pp. 101-113
    • Ayad, N.G.1
  • 53
    • 0038243172 scopus 로고    scopus 로고
    • Control of meiotic and mitotic progression by the F box protein β-Trcp1 in vivo
    • Guardavaccaro, D. et al. Control of meiotic and mitotic progression by the F box protein β-Trcp1 in vivo. Dev. Cell 4, 799-812 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 799-812
    • Guardavaccaro, D.1
  • 54
    • 0037534899 scopus 로고    scopus 로고
    • βTrCP/Slimb ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase
    • βTrCP/Slimb ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase. Dev. Cell 4, 813-826 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 813-826
    • Margottin-Goguet, F.1
  • 55
    • 0242551536 scopus 로고    scopus 로고
    • Ratchets and clocks: The cell cycle, ubiquitylation and protein turnover
    • Reed, S. I. Ratchets and clocks: the cell cycle, ubiquitylation and protein turnover. Nature Rev. Mol. Cell Biol. 4, 855-864 (2003).
    • (2003) Nature Rev. Mol. Cell Biol. , vol.4 , pp. 855-864
    • Reed, S.I.1
  • 57
    • 0033135878 scopus 로고    scopus 로고
    • Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation
    • Montagnoli, A. et al. Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation. Genes Dev. 13, 1181-1189 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1181-1189
    • Montagnoli, A.1
  • 59
    • 0141591688 scopus 로고    scopus 로고
    • Multisite phosphorylation by Cdk2 and GSK3 controls cyclin E degradation
    • Welcker, M. et al. Multisite phosphorylation by Cdk2 and GSK3 controls cyclin E degradation. Mol. Cell 12, 381-392 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 381-392
    • Welcker, M.1
  • 60
    • 2542617641 scopus 로고    scopus 로고
    • Role of Polo-like kinase in the degradation of Emi1, a regulator of the anaphase promoting complex/cyclosome
    • Moshe, Y., Boulaire, J., Pagano, M. & Hershko, A. Role of Polo-like kinase in the degradation of Emi1, a regulator of the anaphase promoting complex/cyclosome. Proc. Natl Acad. Sci. USA 101, 7937-7942 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7937-7942
    • Moshe, Y.1    Boulaire, J.2    Pagano, M.3    Hershko, A.4
  • 61
    • 0141426637 scopus 로고    scopus 로고
    • COP9 signalosome: A multifunctional regulator of SCF and other cullin-based ubiquitin ligases
    • Cope, G. A. & Deshaies, R. J. COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases. Cell 114, 663-671 (2003).
    • (2003) Cell , vol.114 , pp. 663-671
    • Cope, G.A.1    Deshaies, R.J.2
  • 62
    • 18444368709 scopus 로고    scopus 로고
    • Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL
    • Hon, W. C. et al. Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL. Nature 417, 975-978 (2002).
    • (2002) Nature , vol.417 , pp. 975-978
    • Hon, W.C.1
  • 63
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1α-pVHL complex: Hydroxyproline recognition in signaling
    • Min, J. H. et al. Structure of an HIF-1α-pVHL complex: hydroxyproline recognition in signaling. Science 296, 1886-1889 (2002).
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.H.1
  • 64
    • 0034676443 scopus 로고    scopus 로고
    • Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex
    • Schulman, B. et al. Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. Nature, 408, 381-386(2000). The only crystallographic study so far on the substrate-binding portion of an FBL protein.
    • (2000) Nature , vol.408 , pp. 381-386
    • Schulman, B.1
  • 65
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: Implications for VHL tumor suppressor function
    • Stebbins, C. E., Kaelin, W. G. Jr. & Pavletich, N. P. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 284, 455-461 (1999).
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin Jr., W.G.2    Pavletich, N.P.3
  • 66
    • 0037756787 scopus 로고    scopus 로고
    • β-TrCP1 ubiquitin ligase
    • β-TrCP1 ubiquitin ligase. Mol. Cell 11, 445-1456 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 445-1456
    • Wu, G.1
  • 67
    • 18344391432 scopus 로고    scopus 로고
    • Skp2 SCF ubiquitin ligase complex
    • Skp2 SCF ubiquitin ligase complex. Nature 416, 703-709 (2002). Reports the pivotal three-dimensional structural study of the SCF ligase.
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1
  • 68
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RlNG domain function in ubiquitin-protein ligases
    • Zheng, N., Wang, P., Jeffrey, P. D. & Pavletich, N. P. Structure of a c-Cbl-UbcH7 complex: RlNG domain function in ubiquitin-protein ligases. Cell 102, 533-539 (2000).
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 69
    • 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
  • 70
    • 0037249354 scopus 로고    scopus 로고
    • Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase
    • Verdecia, M. A. et al. Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase. Mol. Cell 11, 249-259 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 249-259
    • Verdecia, M.A.1
  • 72
    • 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
  • 73
    • 0141493448 scopus 로고    scopus 로고
    • The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase
    • Pintard, L. et al. The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase. Nature 425, 311-316 (2003).
    • (2003) Nature , vol.425 , pp. 311-316
    • Pintard, L.1
  • 74
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
    • Xu, L. et al. BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3. Nature 425, 316-321 (2003).
    • (2003) Nature , vol.425 , pp. 316-321
    • Xu, L.1
  • 75
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • Geyer, R., Wee, S., Andereon, S., Yates, J. & Wolf, D. A. BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases. Mol. Cell 12, 783-790 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Andereon, S.3    Yates, J.4    Wolf, D.A.5
  • 76
    • 0242575197 scopus 로고    scopus 로고
    • Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases
    • Furukawa, M., He, Y. J., Borchers, C. & Xiong, Y. Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases. Nature Cell Biol. 5, 1001-1007 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 1001-1007
    • Furukawa, M.1    He, Y.J.2    Borchers, C.3    Xiong, Y.4
  • 77
    • 0033602227 scopus 로고    scopus 로고
    • The F-box protein β-TrCP associates with phosphorylated β-catenin and regulates its activity in the cell
    • Hart, M. et al. The F-box protein β-TrCP associates with phosphorylated β-catenin and regulates its activity in the cell. Curr. Biol. 9, 207-210 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 207-210
    • Hart, M.1
  • 78
    • 0033522491 scopus 로고    scopus 로고
    • An F-box protein, FWD1, mediates ubiquitin-dependent proteolysis of β-catenin
    • Kitagawa, M. et al. An F-box protein, FWD1, mediates ubiquitin-dependent proteolysis of β-catenin. EMBO J. 18, 2401-2410 (1999).
    • (1999) EMBO J. , vol.18 , pp. 2401-2410
    • Kitagawa, M.1
  • 79
    • 0033611567 scopus 로고    scopus 로고
    • The human F box protein β-Trcp associates with the Cul1/Skp1 complex and regulates the stability of β-catenin
    • Latres, E., Chiaur, D. S. & Pagano, M. The human F box protein β-Trcp associates with the Cul1/Skp1 complex and regulates the stability of β-catenin. Oncogene 18, 849-854 (1999).
    • (1999) Oncogene , vol.18 , pp. 849-854
    • Latres, E.1    Chiaur, D.S.2    Pagano, M.3
  • 80
    • 0033068154 scopus 로고    scopus 로고
    • β-TRCP ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro
    • β-TRCP ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro. Genes Dev. 13, 270-283 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 270-283
    • Winston, J.T.1
  • 81
    • 0037756792 scopus 로고    scopus 로고
    • Context of multiubiquitin chain attachment influences the rate of Sci1 degradation
    • Petroski, M. D. & Deshaies, R. J. Context of multiubiquitin chain attachment influences the rate of Sci1 degradation. Mol. Cell 11, 1435-1444 (2003). Provides a detailed structure-function analysis of Sci1 degradation by an SCF.
    • (2003) Mol. Cell , vol.11 , pp. 1435-1444
    • Petroski, M.D.1    Deshaies, R.J.2
  • 82
    • 0141838136 scopus 로고    scopus 로고
    • Mathematical modeling suggests cooperative interactions between a disordered polyvalent ligand and a single receptor site
    • Klein, R, Pawson, T. & Tyers, M. Mathematical modeling suggests cooperative interactions between a disordered polyvalent ligand and a single receptor site. Curr. Biol. 13, 1669-1678 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 1669-1678
    • Klein, R.1    Pawson, T.2    Tyers, M.3
  • 83
    • 0029670193 scopus 로고    scopus 로고
    • Rapid degradation of the G1 cyclin Cln2 induced by Cdk-dependent phosphorylation
    • Lanker, S., Valdivieso, M. & Wittenberg, C. Rapid degradation of the G1 cyclin Cln2 induced by Cdk-dependent phosphorylation. Science 271, 1597-1601 (1996).
    • (1996) Science , vol.271 , pp. 1597-1601
    • Lanker, S.1    Valdivieso, M.2    Wittenberg, C.3
  • 84
    • 0035106567 scopus 로고    scopus 로고
    • F-box protein Grr1 interacts with phosphorylated targets via the cationic surface of its leucine-rich repeat
    • Hsiung, Y. G. et al. F-box protein Grr1 interacts with phosphorylated targets via the cationic surface of its leucine-rich repeat. Mol. Cell. Biol. 21, 2506-2520 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2506-2520
    • Hsiung, Y.G.1
  • 85
  • 86
    • 0035092687 scopus 로고    scopus 로고
    • Skp2-mediated ubiquitylation of p27
    • Skp2-mediated ubiquitylation of p27. Nature Cell Biol. 3, 321-324 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 321-324
    • Ganoth, D.1
  • 89
    • 0038583881 scopus 로고    scopus 로고
    • Protein-protein interactions involved in the recognition of p27 by E3 ubiquitin ligase
    • Xu, K. et al. Protein-protein interactions involved in the recognition of p27 by E3 ubiquitin ligase. Biochem. J. 371, 957-964 (2003).
    • (2003) Biochem. J. , vol.371 , pp. 957-964
    • Xu, K.1
  • 93
    • 1842473094 scopus 로고    scopus 로고
    • p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding
    • Lacy, E. R. et al. p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. Nature Struct. Mol. Biol. 11, 358-364 (2004).
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 358-364
    • Lacy, E.R.1
  • 94
    • 0036829681 scopus 로고    scopus 로고
    • Three different binding sites of Cks1 are required for p27-ubiquitin ligation
    • Sitry, D. et al. Three different binding sites of Cks1 are required for p27-ubiquitin ligation. J. Biol. Chem. 277, 42233-42240 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 42233-42240
    • Sitry, D.1
  • 95
    • 0029918062 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1
    • Bourne, Y. et al. Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1. Cell 84, 863-874 (1996).
    • (1996) Cell , vol.84 , pp. 863-874
    • Bourne, Y.1
  • 96
    • 0029665852 scopus 로고    scopus 로고
    • Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex
    • Russo, A. A., Jeffrey, P. D., Patten, A. K., Massague, J. & Pavletich, N. P. Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 382, 325-331 (1996). Provides the most complete set of structural data on p27.
    • (1996) Nature , vol.382 , pp. 325-331
    • Russo, A.A.1    Jeffrey, P.D.2    Patten, A.K.3    Massague, J.4    Pavletich, N.P.5
  • 97
    • 12144289596 scopus 로고    scopus 로고
    • Structural basis of sugar-recognizing ubiquitin ligase
    • Mizushima, T. et al. Structural basis of sugar-recognizing ubiquitin ligase. Nature Struct. Mol. Biol. 11, 365-370 (2004).
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 365-370
    • Mizushima, T.1
  • 98
    • 0141987892 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of p21 via N-terminal ubiquitylation
    • Bloom, J., Amador, V., Bartolini, F., DeMartino, G. & Pagano, M. Proteasome-mediated degradation of p21 via N-terminal ubiquitylation. Cell 115, 71-82 (2003).
    • (2003) Cell , vol.115 , pp. 71-82
    • Bloom, J.1    Amador, V.2    Bartolini, F.3    DeMartino, G.4    Pagano, M.5
  • 99
    • 0033525234 scopus 로고    scopus 로고
    • IκBα ubiquitination is catalyzed by an SCF-like complex containing Skp1, cullin-1, and two F-box/WD40-repeat proteins, βTrCP1 and βTrCP2
    • Suzuki, H. et al. IκBα ubiquitination is catalyzed by an SCF-like complex containing Skp1, cullin-1, and two F-box/WD40-repeat proteins, βTrCP1 and βTrCP2. Biochem. Biophys. Res. Commun. 256,127-132 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 127-132
    • Suzuki, H.1
  • 100
    • 0141522457 scopus 로고    scopus 로고
    • Cdc4-bound substrate Sic1
    • Cdc4-bound substrate Sic1. Cell 114, 611-622 (2003).
    • (2003) Cell , vol.114 , pp. 611-622
    • Deffenbaugh, A.E.1
  • 101
    • 0042090923 scopus 로고    scopus 로고
    • Cdc34 self-association is facilitated by ubiquitin thiolester formation and is required for its catalytic activity
    • Varelas, X., Ptak, C. & Ellison, M. J. Cdc34 self-association is facilitated by ubiquitin thiolester formation and is required for its catalytic activity. Mol. Cell. Biol. 23, 5388-5400 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5388-5400
    • Varelas, X.1    Ptak, C.2    Ellison, M.J.3
  • 102
    • 1842591241 scopus 로고    scopus 로고
    • Nedd8 on cullin: Building an expressway to protein destruction
    • Pan, Z. Q., Kentsis, A., Dias, D. C., Yamoah, K. & Wu, K. Nedd8 on cullin: building an expressway to protein destruction. Oncogene 23, 1985-1997 (2004).
    • (2004) Oncogene , vol.23 , pp. 1985-1997
    • Pan, Z.Q.1    Kentsis, A.2    Dias, D.C.3    Yamoah, K.4    Wu, K.5
  • 103
    • 1042268088 scopus 로고    scopus 로고
    • Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro
    • Kus, B. M., Caldon, C. E., Andorn-Broza, R. & Edwards. A. M. Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro. Proteins 54, 455-467 (2004).
    • (2004) Proteins , vol.54 , pp. 455-467
    • Kus, B.M.1    Caldon, C.E.2    Andorn-Broza, R.3    Edwards, A.M.4
  • 104
    • 0032215237 scopus 로고    scopus 로고
    • Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases
    • Zhou, P. & Howley, P. M. Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases. Mol. Cell 2, 571-580 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 571-580
    • Zhou, P.1    Howley, P.M.2
  • 105
    • 0034675922 scopus 로고    scopus 로고
    • The F-box protein Skp2 is a ubiquitylation target of a Cul1-based core ubiquitin ligase complex: Evidence for a role of Cul1 in the suppression of Skp2 expression in quiescent fibroblasts
    • Wirbelauer, C. et al. The F-box protein Skp2 is a ubiquitylation target of a Cul1-based core ubiquitin ligase complex: evidence for a role of Cul1 in the suppression of Skp2 expression in quiescent fibroblasts. EMBO J. 19, 5362-5375 (2000).
    • (2000) EMBO J. , vol.19 , pp. 5362-5375
    • Wirbelauer, C.1
  • 106
    • 1642442587 scopus 로고    scopus 로고
    • Stability of homologue of slimb F-box protein is regulated by availability of its substrate
    • Li, Y., Gazdoiu, S., Pan, Z. Q. & Fuchs, S. Y. Stability of homologue of slimb F-box protein is regulated by availability of its substrate. J. Biol. Chem. 279, 11074-11080 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 11074-11080
    • Li, Y.1    Gazdoiu, S.2    Pan, Z.Q.3    Fuchs, S.Y.4
  • 107
    • 0142165038 scopus 로고    scopus 로고
    • When protein destruction runs amok, malignancy is on the loose
    • Pagano, M. & Benmaamar, R. When protein destruction runs amok, malignancy is on the loose. Cancer Cell 4, 251-256 (2003).
    • (2003) Cancer Cell , vol.4 , pp. 251-256
    • Pagano, M.1    Benmaamar, R.2
  • 108
    • 0037233286 scopus 로고    scopus 로고
    • Aberrant ubiquitin-mediated proteolysis of cell cycle regulatory proteins and oncogenesis
    • Bashir, T. & Pagano, M. Aberrant ubiquitin-mediated proteolysis of cell cycle regulatory proteins and oncogenesis. Adv. Cancer Res. 88, 101-144 (2003).
    • (2003) Adv. Cancer Res. , vol.88 , pp. 101-144
    • Bashir, T.1    Pagano, M.2
  • 109
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • Pickart, C. M. Back to the future with ubiquitin. Cell 116, 181-190 (2004).
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 110
    • 0034296394 scopus 로고    scopus 로고
    • Basic Medical Research Award. The ubiquitin system
    • Hershko, A., Ciechanover, A. & Varshavsky, A. Basic Medical Research Award. The ubiquitin system. Nature Med. 6, 1073-1081 (2000).
    • (2000) Nature Med. , vol.6 , pp. 1073-1081
    • Hershko, A.1    Ciechanover, A.2    Varshavsky, A.3
  • 111
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart, C. M. & Cohen, R. E. Proteasomes and their kin: proteases in the machine age. Nature Rev. Mol. Cell Biol. 5, 177-187 (2004).
    • (2004) Nature Rev. Mol. Cell Biol. , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 112
    • 2542501657 scopus 로고    scopus 로고
    • Ubiquitin ligases and the immune response
    • Liu, Y. C. Ubiquitin ligases and the immune response. Annu. Rev. Immunol. 22, 81-127 (2004).
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 81-127
    • Liu, Y.C.1
  • 113
    • 0034568688 scopus 로고    scopus 로고
    • The F-box protein family
    • REVIEWS3002
    • Kipreos, E. T. & Pagano, M. The F-box protein family. Genome Biol. 1, REVIEWS3002 (2000).
    • (2000) Genome Biol. , vol.1
    • Kipreos, E.T.1    Pagano, M.2
  • 114
    • 0037133036 scopus 로고    scopus 로고
    • The Caenorhabditis elegans Skp1-related gene family: Diverse functions in cell proliferation, morphogenesis, and meiosis
    • Nayak, S. et al. The Caenorhabditis elegans Skp1-related gene family: diverse functions in cell proliferation, morphogenesis, and meiosis. Curr. Biol. 12, 277-287 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 277-287
    • Nayak, S.1
  • 115
    • 0037133045 scopus 로고    scopus 로고
    • Multiple Skp1-related proteins in Caenorhabditis elegans: Diverse patterns of interaction with Cullins and F-box proteins
    • Yamanaka, A. et al. Multiple Skp1-related proteins in Caenorhabditis elegans: diverse patterns of interaction with Cullins and F-box proteins. Curr. Biol. 12, 267-275 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 267-275
    • Yamanaka, A.1
  • 116
    • 0344232728 scopus 로고    scopus 로고
    • The F box protein AFR is a positive regulator of phytochrome A-mediated light signaling
    • Harmon, F. G. & Kay. S. A. The F box protein AFR is a positive regulator of phytochrome A-mediated light signaling. Curr. Biol. 13, 2091-2096 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 2091-2096
    • Harmon, F.G.1    Kay, S.A.2
  • 117
    • 0042695874 scopus 로고    scopus 로고
    • The Arabidopsis SKP1-like genes present a spectrum of expression profiles
    • Marrocco, K., Lecureuil, A., Nicolas, P. & Guerche, P. The Arabidopsis SKP1-like genes present a spectrum of expression profiles. Plant Mol. Biol. 52, 715-727 (2003).
    • (2003) Plant Mol. Biol. , vol.52 , pp. 715-727
    • Marrocco, K.1    Lecureuil, A.2    Nicolas, P.3    Guerche, P.4
  • 118
    • 0037742392 scopus 로고    scopus 로고
    • Protein interaction analysis of SCF ubiquitin E3 ligase subunits from Arabidopsis
    • Risseeuw, E. P. et al. Protein interaction analysis of SCF ubiquitin E3 ligase subunits from Arabidopsis. Plant J. 34, 753-767 (2003).
    • (2003) Plant J. , vol.34 , pp. 753-767
    • Risseeuw, E.P.1
  • 119
    • 0017255087 scopus 로고
    • Inhibition of tubulin-microtubule polymerization by drugs of the Vinca alkaloid class
    • Owellen, R. J., Hartke. C. A., Dickerson, R. M. & Hans, F O. Inhibition of tubulin-microtubule polymerization by drugs of the Vinca alkaloid class. Cancer Res. 36, 1499-1502 (1976).
    • (1976) Cancer Res. , vol.36 , pp. 1499-1502
    • Owellen, R.J.1    Hartke, C.A.2    Dickerson, R.M.3    Hans, F.O.4
  • 120
    • 13044256383 scopus 로고    scopus 로고
    • A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-HIV-1 activity
    • Baba, M. et al. A small-molecule, nonpeptide CCR5 antagonist with highly potent and selective anti-HIV-1 activity. Proc. Natl Acad. Sci. USA 96, 5698-5703 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 5698-5703
    • Baba, M.1
  • 121
    • 0037452709 scopus 로고    scopus 로고
    • Binding of small molecules to an adaptive protein-protein interface
    • Arkin, M. R. et al. Binding of small molecules to an adaptive protein-protein interface. Proc. Natl Acad. Sci. USA 100, 1603-1608 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1603-1608
    • Arkin, M.R.1
  • 122
    • 0037133575 scopus 로고    scopus 로고
    • Small-molecule antagonists of Myc/Max dimerization inhibit Myc-induced transformation of chicken embryo fibroblasts
    • Berg, T. et al. Small-molecule antagonists of Myc/Max dimerization inhibit Myc-induced transformation of chicken embryo fibroblasts. Proc. Natl Acad. Sci. USA 99, 3830-3835 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3830-3835
    • Berg, T.1
  • 124
    • 1642512639 scopus 로고    scopus 로고
    • Small-molecule antagonists of the oncogenic Tcf/β-catenin protein complex
    • Lepourcelet, M. et al. Small-molecule antagonists of the oncogenic Tcf/β-catenin protein complex. Cancer Cell 5, 91-102 (2004).
    • (2004) Cancer Cell , vol.5 , pp. 91-102
    • Lepourcelet, M.1
  • 125
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev, L. T. et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 303, 844-848 (2004). This break-through drug-discovery work established that protein interfaces can be disrupted by small molecules, and that ubiquitin ligases can be targeted.
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1
  • 126
    • 0037061646 scopus 로고    scopus 로고
    • Inhibition of protein-protein association by small molecules: Approaches and progress
    • Toogood, P. L. Inhibition of protein-protein association by small molecules: approaches and progress. J. Med. Chem. 45, 1543-1558 (2002).
    • (2002) J. Med. Chem. , vol.45 , pp. 1543-1558
    • Toogood, P.L.1
  • 127
    • 0035630691 scopus 로고    scopus 로고
    • Protein-protein interfaces: Mimics and inhibitors
    • Cochran, A. G. Protein-protein interfaces: mimics and inhibitors. Curr. Opin. Chem. Biol. 5, 654-659 (2001).
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 654-659
    • Cochran, A.G.1
  • 128
    • 0028212411 scopus 로고
    • Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase
    • Mayer, B. J. & Baltimore, D. Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase. Mol. Cell. Biol. 14, 2883-2894 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2883-2894
    • Mayer, B.J.1    Baltimore, D.2


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