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Volumn 1, Issue , 2007, Pages 156-189

The Structural Biology of Ubiquitin-Protein Ligases

Author keywords

C Cbl UbcH7 complex; E3 function; E6AP HECT domain in complex with UbcH7; Mms2 Ubc13 complex; Protein degradation; RanGAP1 Ubc9 complex; SCF E3 superfamily; Structural biology; Ubiquitin protein ligases

Indexed keywords


EID: 33845467464     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527619320.ch7     Document Type: Chapter
Times cited : (1)

References (109)
  • 2
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke, L. Protein regulation by monoubiquitin. Nat Rev Mol Cell Biol 2001, 2, 195-201.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 195-201
    • Hicke, L.1
  • 3
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. Mechanisms underlying ubiquitination. Annu Rev Biochem 2001, 70, 503-33.
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 4
    • 0037397606 scopus 로고    scopus 로고
    • The ubiquitin proteolytic system and pathogenesis of human diseases: a novel platform for mechanism-based drug targeting
    • Ciechanover, A. The ubiquitin proteolytic system and pathogenesis of human diseases: a novel platform for mechanism-based drug targeting. Biochem Soc Trans 2003, 31, 474-81.
    • (2003) Biochem Soc Trans , vol.31 , pp. 474-481
    • Ciechanover, A.1
  • 5
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko, A., Heller, H., Elias, S. and Ciechanover, A. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J Biol Chem 1983, 258, 8206-14.
    • (1983) J Biol Chem , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 6
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: mediators of ubiquitin ligase activity
    • Joazeiro, C. A. and Weissman, A. M. RING finger proteins: mediators of ubiquitin ligase activity. Cell 2000, 102, 549-52.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 7
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner, M., Nuber, U. and Huibregtse, J. M. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature 1995, 373, 81-3.
    • (1995) Nature , vol.373 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 8
    • 0034308251 scopus 로고    scopus 로고
    • The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases
    • Jackson, P. K. et al. The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases. Trends Cell Biol 2000, 10, 429-39.
    • (2000) Trends Cell Biol , vol.10 , pp. 429-439
    • Jackson, P.K.1
  • 9
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • Cyr, D. M., Hohfeld, J. and Patterson, C. Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. Trends Biochem Sci 2002, 27, 368-75.
    • (2002) Trends Biochem Sci , vol.27 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 10
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas, A. L. and Siepmann, T. J. Pathways of ubiquitin conjugation. Faseb J 1997, 11, 1257-68.
    • (1997) Faseb J , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 11
    • 0032127912 scopus 로고    scopus 로고
    • GTPase-activating proteins: helping hands to complement an active site
    • Scheffzek, K., Ahmadian, M. R. and Wittinghofer, A. GTPase-activating proteins: helping hands to complement an active site. Trends Biochem Sci 1998, 23, 257-62.
    • (1998) Trends Biochem Sci , vol.23 , pp. 257-262
    • Scheffzek, K.1    Ahmadian, M.R.2    Wittinghofer, A.3
  • 12
    • 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 1999, 286, 309-12.
    • (1999) Science , vol.286 , pp. 309-312
    • Joazeiro, C.A.1
  • 13
    • 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 1999, 96, 11364-9.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11364-11369
    • Lorick, K.L.1
  • 14
    • 0141753130 scopus 로고    scopus 로고
    • A conserved catalytic residue in the ubiquitin-conjugating enzyme family
    • Wu, P. Y. et al. A conserved catalytic residue in the ubiquitin-conjugating enzyme family. Embo J 2003, 22, 5241-50.
    • (2003) Embo J , vol.22 , pp. 5241-5250
    • Wu, P.Y.1
  • 15
    • 0028607143 scopus 로고
    • Regulated degradation of the transcription factor Gcn4
    • Kornitzer, D., Raboy, B., Kulka, R. G. and Fink, G. R. Regulated degradation of the transcription factor Gcn4. Embo J 1994, 13, 6021-30.
    • (1994) Embo J , vol.13 , pp. 6021-6030
    • Kornitzer, D.1    Raboy, B.2    Kulka, R.G.3    Fink, G.R.4
  • 16
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • Treier, M., Staszewski, L. M. and Bohmann, D. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 1994, 78, 787-98.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 17
    • 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 1989, 243, 1576-83.
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1
  • 18
    • 0030070803 scopus 로고    scopus 로고
    • Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of I kappa B-alpha
    • Baldi, L., Brown, K., Franzoso, G. and Siebenlist, U. Critical role for lysines 21 and 22 in signal-induced, ubiquitin-mediated proteolysis of I kappa B-alpha. J Biol Chem 1996, 271, 376-9.
    • (1996) J Biol Chem , vol.271 , pp. 376-379
    • Baldi, L.1    Brown, K.2    Franzoso, G.3    Siebenlist, U.4
  • 19
    • 0028972488 scopus 로고
    • Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination
    • Scherer, D. C., Brockman, J. A., Chen, Z., Maniatis, T. and Ballard, D. W. Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination. Proc Natl Acad Sci USA 1995, 92, 11259-63.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11259-11263
    • Scherer, D.C.1    Brockman, J.A.2    Chen, Z.3    Maniatis, T.4    Ballard, D.W.5
  • 20
    • 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 2000, 11, 141-8.
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 21
    • 0037428081 scopus 로고    scopus 로고
    • Regulating the regulators: lysine modifications make their mark
    • Freiman, R. N. and Tjian, R. Regulating the regulators: lysine modifications make their mark. Cell 2003, 112, 11-7.
    • (2003) Cell , vol.112 , pp. 11-17
    • Freiman, R.N.1    Tjian, R.2
  • 22
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation
    • Desterro, J. M., Rodriguez, M. S. and Hay, R. T. SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol Cell 1998, 2, 233-9.
    • (1998) Mol Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 23
    • 0037184969 scopus 로고    scopus 로고
    • Acetylation of p53 inhibits its ubiquitination by Mdm2
    • Li, M., Luo, J., Brooks, C. L. and Gu, W. Acetylation of p53 inhibits its ubiquitination by Mdm2. J Biol Chem 2002, 277, 50607-11.
    • (2002) J Biol Chem , vol.277 , pp. 50607-50611
    • Li, M.1    Luo, J.2    Brooks, C.L.3    Gu, W.4
  • 25
    • 0038362292 scopus 로고    scopus 로고
    • When ubiquitin meets ubiquitin receptors: a signalling connection
    • Di Fiore, P. P., Polo, S. and Hofmann, K. When ubiquitin meets ubiquitin receptors: a signalling connection. Nat Rev Mol Cell Biol 2003, 4, 491-7.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 491-497
    • Di Fiore, P.P.1    Polo, S.2    Hofmann, K.3
  • 26
    • 0031962188 scopus 로고    scopus 로고
    • Role of UEV-1, an inactive variant of the E2 ubiquitinconjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells
    • Sancho, E. et al. Role of UEV-1, an inactive variant of the E2 ubiquitinconjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells. Mol Cell Biol 1998, 18, 576-89.
    • (1998) Mol Cell Biol , vol.18 , pp. 576-589
    • Sancho, E.1
  • 27
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann, R. M. and Pickart, C. M. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell 1999, 96, 645-53.
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 28
    • 0026653834 scopus 로고
    • Threedimensional structure of a ubiquitinconjugating enzyme (E2)
    • Cook, W. J., Jeffrey, L. C., Sullivan, M. L. and Vierstra, R. D. Threedimensional structure of a ubiquitinconjugating enzyme (E2). J Biol Chem 1992, 267, 15116-21.
    • (1992) J Biol Chem , vol.267 , pp. 15116-15121
    • Cook, W.J.1    Jeffrey, L.C.2    Sullivan, M.L.3    Vierstra, R.D.4
  • 30
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
    • Scheffner, M., Werness, B. A., Huibregtse, J. M., Levine, A. J. and Howley, P. M. The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 1990, 63, 1129-36.
    • (1990) Cell , vol.63 , pp. 1129-1136
    • Scheffner, M.1    Werness, B.A.2    Huibregtse, J.M.3    Levine, A.J.4    Howley, P.M.5
  • 31
    • 0025932933 scopus 로고
    • A cellular protein mediates association of p53 with the E6 oncoprotein of human papillomavirus types 16 or 18
    • Huibregtse, J. M., Scheffner, M. and Howley, P. M. A cellular protein mediates association of p53 with the E6 oncoprotein of human papillomavirus types 16 or 18. Embo J 1991, 10, 4129-35.
    • (1991) Embo J , vol.10 , pp. 4129-4135
    • Huibregtse, J.M.1    Scheffner, M.2    Howley, P.M.3
  • 33
    • 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. and Scheffner, M. Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. J Biol Chem 1998, 273, 12148-54.
    • (1998) J Biol Chem , vol.273 , pp. 12148-12154
    • Schwarz, S.E.1    Rosa, J.L.2    Scheffner, M.3
  • 34
    • 0032907946 scopus 로고    scopus 로고
    • Functional domains of the Rsp5 ubiquitin-protein ligase
    • Wang, G., Yang, J. and Huibregtse, J. M. Functional domains of the Rsp5 ubiquitin-protein ligase. Mol Cell Biol 1999, 19, 342-52.
    • (1999) Mol Cell Biol , vol.19 , pp. 342-352
    • Wang, G.1    Yang, J.2    Huibregtse, J.M.3
  • 35
    • 0028607435 scopus 로고
    • Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53
    • Scheffner, M., Huibregtse, J. M. and Howley, P. M. Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53. Proc Natl Acad Sci USA 1994, 91, 8797-801.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8797-8801
    • Scheffner, M.1    Huibregtse, J.M.2    Howley, P.M.3
  • 36
    • 0030043724 scopus 로고    scopus 로고
    • Cloning of human ubiquitinconjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5
    • Nuber, U., Schwarz, S., Kaiser, P., Schneider, R. and Scheffner, M. Cloning of human ubiquitinconjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. J Biol Chem 1996, 271, 2795-800.
    • (1996) J Biol Chem , vol.271 , pp. 2795-2800
    • Nuber, U.1    Schwarz, S.2    Kaiser, P.3    Schneider, R.4    Scheffner, M.5
  • 37
    • 0030908874 scopus 로고    scopus 로고
    • Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity
    • Kumar, S., Kao, W. H. and Howley, P. M. Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity. J Biol Chem 1997, 272, 13548-54.
    • (1997) J Biol Chem , vol.272 , pp. 13548-13554
    • Kumar, S.1    Kao, W.H.2    Howley, P.M.3
  • 38
    • 0032741446 scopus 로고    scopus 로고
    • Structure of an E6APUbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade
    • Huang, L. et al. Structure of an E6APUbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science 1999, 286, 1321-6.
    • (1999) Science , vol.286 , pp. 1321-1326
    • Huang, L.1
  • 39
    • 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 2003, 11, 249-59.
    • (2003) Mol Cell , vol.11 , pp. 249-259
    • Verdecia, M.A.1
  • 40
    • 0035316576 scopus 로고    scopus 로고
    • Cbl: many adaptations to regulate protein tyrosine kinases
    • Thien, C. B. and Langdon, W. Y. Cbl: many adaptations to regulate protein tyrosine kinases. Nat Rev Mol Cell Biol 2001, 2, 294-307.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 294-307
    • Thien, C.B.1    Langdon, W.Y.2
  • 41
    • 1542373897 scopus 로고    scopus 로고
    • Distinct monoubiquitin signals in receptor endocytosis
    • Haglund, K., Di Fiore, P. P. and Dikic, I. Distinct monoubiquitin signals in receptor endocytosis. Trends Biochem Sci 2003, 28, 598-603.
    • (2003) Trends Biochem Sci , vol.28 , pp. 598-603
    • Haglund, K.1    Di Fiore, P.P.2    Dikic, I.3
  • 42
    • 0037677208 scopus 로고    scopus 로고
    • Endocytsosis of receptor tyrosine kinases is driven by mono-, not poly-ubiquitylation
    • Mosesson, Y. et al. Endocytsosis of receptor tyrosine kinases is driven by mono-, not poly-ubiquitylation. J Biol Chem 2003.
    • (2003) J Biol Chem
    • Mosesson, Y.1
  • 43
    • 0037075606 scopus 로고    scopus 로고
    • The endophilin-CIN85-Cbl complex mediates liganddependent downregulation of c-Met
    • Petrelli, A. et al. The endophilin-CIN85-Cbl complex mediates liganddependent downregulation of c-Met. Nature 2002, 416, 187-90.
    • (2002) Nature , vol.416 , pp. 187-190
    • Petrelli, A.1
  • 44
    • 0037075547 scopus 로고    scopus 로고
    • Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors
    • Soubeyran, P., Kowanetz, K., Szymkiewicz, I., Langdon, W. Y. and Dikic, I. Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors. Nature 2002, 416, 183-7.
    • (2002) Nature , vol.416 , pp. 183-187
    • Soubeyran, P.1    Kowanetz, K.2    Szymkiewicz, I.3    Langdon, W.Y.4    Dikic, I.5
  • 45
    • 0038394715 scopus 로고    scopus 로고
    • Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
    • Haglund, K. et al. Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat Cell Biol 2003, 5, 461-6.
    • (2003) Nat Cell Biol , vol.5 , pp. 461-466
    • Haglund, K.1
  • 46
    • 0031759356 scopus 로고    scopus 로고
    • C-Cbl: a regulator of T cell receptormediated signalling
    • Thien, C. B. and Langdon, W.Y. C-Cbl: a regulator of T cell receptormediated signalling. Immunol Cell Biol 1998, 76, 473-82.
    • (1998) Immunol Cell Biol , vol.76 , pp. 473-482
    • Thien, C.B.1    Langdon, W.Y.2
  • 47
    • 0033392493 scopus 로고    scopus 로고
    • Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1
    • Levkowitz, G. et al. Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1. Mol Cell 1999, 4, 1029-40.
    • (1999) Mol Cell , vol.4 , pp. 1029-1040
    • Levkowitz, G.1
  • 48
    • 0033522219 scopus 로고    scopus 로고
    • Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase
    • Meng, W., Sawasdikosol, S., Burakoff, S. J. and Eck, M. J. Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase. Nature 1999, 398, 84-90.
    • (1999) Nature , vol.398 , pp. 84-90
    • Meng, W.1    Sawasdikosol, S.2    Burakoff, S.J.3    Eck, M.J.4
  • 49
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng, N., Wang, P., Jeffrey, P. D. and Pavletich, N. P. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 2000, 102, 533-9.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 50
    • 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 1999, 15, 435-67.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 51
    • 0032549115 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the anaphasepromoting complex from yeast: identification of a subunit related to cullins
    • Zachariae, W. et al. Mass spectrometric analysis of the anaphasepromoting complex from yeast: identification of a subunit related to cullins. Science 1998, 279, 1216-9.
    • (1998) Science , vol.279 , pp. 1216-1219
    • Zachariae, W.1
  • 52
    • 0032549116 scopus 로고    scopus 로고
    • Identification of a cullin homology region in a subunit of the anaphase-promoting complex
    • Yu, H. et al. Identification of a cullin homology region in a subunit of the anaphase-promoting complex. Science 1998, 279, 1219-22.
    • (1998) Science , vol.279 , pp. 1219-1222
    • Yu, H.1
  • 53
    • 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. and Xiong, Y. ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. Mol Cell 1999, 3, 535-41.
    • (1999) Mol Cell , vol.3 , pp. 535-541
    • Ohta, T.1    Michel, J.J.2    Schottelius, A.J.3    Xiong, Y.4
  • 54
    • 0037168527 scopus 로고    scopus 로고
    • CUL7: A DOC domaincontaining cullin selectively binds Skp1.Fbx29 to form an SCF-like complex
    • Dias, D. C., Dolios, G., Wang, R. and Pan, Z. Q. CUL7: A DOC domaincontaining cullin selectively binds Skp1.Fbx29 to form an SCF-like complex. Proc Natl Acad Sci USA 2002, 99, 16601-6.
    • (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
  • 55
    • 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 2003, 425, 311-6.
    • (2003) Nature , vol.425 , pp. 311-316
    • Pintard, L.1
  • 56
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCFlike modular ubiquitin ligase containing CUL-3
    • Xu, L. et al. BTB proteins are substrate-specific adaptors in an SCFlike modular ubiquitin ligase containing CUL-3. Nature 2003, 425, 316-21.
    • (2003) Nature , vol.425 , pp. 316-321
    • Xu, L.1
  • 57
    • 0034568688 scopus 로고    scopus 로고
    • The Fbox protein family
    • REVIEWS
    • Kipreos, E. T. and Pagano, M. The Fbox protein family. Genome Biol 2000, 1, REVIEWS3002.
    • (2000) Genome Biol , vol.1 , pp. 3002
    • Kipreos, E.T.1    Pagano, M.2
  • 59
    • 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 1996, 86, 263-74.
    • (1996) Cell , vol.86 , pp. 263-274
    • Bai, C.1
  • 60
    • 0034676443 scopus 로고    scopus 로고
    • Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex
    • Schulman, B. A. et al. Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. Nature 2000, 408, 381-6.
    • (2000) Nature , vol.408 , pp. 381-386
    • Schulman, B.A.1
  • 61
    • 0035092687 scopus 로고    scopus 로고
    • The cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27
    • Ganoth, D. et al. The cell-cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27. Nat Cell Biol 2001, 3, 321-4.
    • (2001) Nat Cell Biol , vol.3 , pp. 321-324
    • Ganoth, D.1
  • 62
    • 0035265829 scopus 로고    scopus 로고
    • A CDK-independent function of mammalian Cks1: targeting of SCF(Skp2) to the CDK inhibitor p27Kip1
    • Spruck, C. et al. A CDK-independent function of mammalian Cks1: targeting of SCF(Skp2) to the CDK inhibitor p27Kip1. Mol Cell 2001, 7, 639-50.
    • (2001) Mol Cell , vol.7 , pp. 639-650
    • Spruck, C.1
  • 63
    • 0035812709 scopus 로고    scopus 로고
    • Phosphorylationdependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase
    • Koepp, D. M. et al. Phosphorylationdependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. Science 2001, 294, 173-7.
    • (2001) Science , vol.294 , pp. 173-177
    • Koepp, D.M.1
  • 64
    • 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. and Hariharan, I. K. Archipelago regulates Cyclin E levels in Drosophila and is mutated in human cancer cell lines. Nature 2001, 413, 311-6.
    • (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
  • 65
    • 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 2001, 413, 316-22.
    • (2001) Nature , vol.413 , pp. 316-322
    • Strohmaier, H.1
  • 66
    • 0037756787 scopus 로고    scopus 로고
    • Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase
    • Wu, G. et al. Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. Mol Cell 2003, 11, 1445-56.
    • (2003) Mol Cell , vol.11 , pp. 1445-1456
    • Wu, G.1
  • 67
    • 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. and Pavletich, N. P. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 1999, 284, 455-61.
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin Jr., W.G.2    Pavletich, N.P.3
  • 68
    • 0036558025 scopus 로고    scopus 로고
    • The SOCS box: a tale of destruction and degradation
    • Kile, B. T. et al. The SOCS box: a tale of destruction and degradation. Trends Biochem Sci 2002, 27, 235-41.
    • (2002) Trends Biochem Sci , vol.27 , pp. 235-241
    • Kile, B.T.1
  • 69
    • 0035917313 scopus 로고    scopus 로고
    • HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing
    • Ivan, M. et al. HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science 2001, 292, 464-8.
    • (2001) Science , vol.292 , pp. 464-468
    • Ivan, M.1
  • 70
    • 0036830636 scopus 로고    scopus 로고
    • SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2
    • Rui, L., Yuan, M., Frantz, D., Shoelson, S. and White, M. F. SOCS-1 and SOCS-3 block insulin signaling by ubiquitin-mediated degradation of IRS1 and IRS2. J Biol Chem 2002, 277, 42394-8.
    • (2002) J Biol Chem , vol.277 , pp. 42394-42398
    • Rui, L.1    Yuan, M.2    Frantz, D.3    Shoelson, S.4    White, M.F.5
  • 71
    • 0027240519 scopus 로고
    • Identification of the von Hippel-Lindau disease tumor suppressor gene
    • Latif, F. et al. Identification of the von Hippel-Lindau disease tumor suppressor gene. Science 1993, 260, 1317-20.
    • (1993) Science , vol.260 , pp. 1317-1320
    • Latif, F.1
  • 72
    • 0029126892 scopus 로고
    • Inhibition of transcription elongation by the VHL tumor suppressor protein
    • Duan, D. R. et al. Inhibition of transcription elongation by the VHL tumor suppressor protein. Science 1995, 269, 1402-6.
    • (1995) Science , vol.269 , pp. 1402-1406
    • Duan, D.R.1
  • 73
    • 0030953635 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins
    • Pause, A. et al. The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins. Proc Natl Acad Sci USA 1997, 94, 2156-61.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2156-2161
    • Pause, A.1
  • 74
    • 0031907152 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2
    • Lonergan, K. M. et al. Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2. Mol Cell Biol 1998, 18, 732-41.
    • (1998) Mol Cell Biol , vol.18 , pp. 732-741
    • Lonergan, K.M.1
  • 75
    • 0035253381 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein.
    • Ivan, M. and Kaelin, W. G., Jr. The von Hippel-Lindau tumor suppressor protein. Curr Opin Genet Dev 2001, 11, 27-34.
    • (2001) Curr Opin Genet Dev , vol.11 , pp. 27-34
    • Ivan, M.1    Kaelin Jr., W.G.2
  • 76
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIFalpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • Jaakkola, P. et al. Targeting of HIFalpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 2001, 292, 468-72.
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1
  • 77
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick, R. K. and McKnight, S. L. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 2001, 294, 1337-40.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 78
    • 17944375360 scopus 로고    scopus 로고
    • C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
    • Epstein, A. C. et al. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 2001, 107, 43-54.
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.C.1
  • 79
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition in signaling
    • Min, J. H. et al. Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition in signaling. Science 2002, 296, 1886-9.
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.H.1
  • 80
    • 0034816198 scopus 로고    scopus 로고
    • Regulation of the cell cycle at the G1-S transition by proteolysis of cyclin E and p27Kip1
    • Nakayama, K. I., Hatakeyama, S. and Nakayama, K. Regulation of the cell cycle at the G1-S transition by proteolysis of cyclin E and p27Kip1. Biochem Biophys Res Commun 2001, 282, 853-60.
    • (2001) Biochem Biophys Res Commun , vol.282 , pp. 853-860
    • Nakayama, K.I.1    Hatakeyama, S.2    Nakayama, K.3
  • 81
    • 0035942224 scopus 로고    scopus 로고
    • Skp2 is oncogenic and overexpressed in human cancers
    • Gstaiger, M. et al. Skp2 is oncogenic and overexpressed in human cancers. Proc Natl Acad Sci USA 2001, 98, 5043-8.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5043-5048
    • Gstaiger, M.1
  • 82
    • 0037112174 scopus 로고    scopus 로고
    • The pRb-related protein p130 is regulated by phosphorylationdependent proteolysis via the proteinubiquitin ligase SCF(Skp2)
    • Tedesco, D., Lukas, J. and Reed, S. I. The pRb-related protein p130 is regulated by phosphorylationdependent proteolysis via the proteinubiquitin ligase SCF(Skp2). Genes Dev 2002, 16, 2946-57.
    • (2002) Genes Dev , vol.16 , pp. 2946-2957
    • Tedesco, D.1    Lukas, J.2    Reed, S.I.3
  • 84
    • 12444264823 scopus 로고    scopus 로고
    • The F-box protein Skp2 participates in c-Myc proteosomal degradation and acts as a cofactor for c-Myc-regulated transcription
    • von der Lehr, N. et al. The F-box protein Skp2 participates in c-Myc proteosomal degradation and acts as a cofactor for c-Myc-regulated transcription. Mol Cell 2003, 11, 1189-200.
    • (2003) Mol Cell , vol.11 , pp. 1189-1200
    • Von Der Lehr, N.1
  • 85
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cul1-Rbx1-Skp1-F-boxSkp2 SCF ubiquitin ligase complex
    • Zheng, N. et al. Structure of the Cul1-Rbx1-Skp1-F-boxSkp2 SCF ubiquitin ligase complex. Nature 2002, 416, 703-9.
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1
  • 86
    • 0037509859 scopus 로고    scopus 로고
    • The Ubiquitin Ligase Activity in the DDB2 and CSA Complexes Is Differentially Regulated by the COP9 Signalosome in Response to DNA Damage
    • Groisman, R. et al. The Ubiquitin Ligase Activity in the DDB2 and CSA Complexes Is Differentially Regulated by the COP9 Signalosome in Response to DNA Damage. Cell 2003, 113, 357-67.
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1
  • 87
    • 0033581899 scopus 로고    scopus 로고
    • Covalent modification of all members of human cullin family proteins by NEDD8
    • Hori, T. et al. Covalent modification of all members of human cullin family proteins by NEDD8. Oncogene 1999, 18, 6829-34.
    • (1999) Oncogene , vol.18 , pp. 6829-6834
    • Hori, T.1
  • 88
    • 0037447311 scopus 로고    scopus 로고
    • The RUB/Nedd8 conjugation pathway is required for early development in Arabidopsis
    • Dharmasiri, S., Dharmasiri, N., Hellmann, H. and Estelle, M. The RUB/Nedd8 conjugation pathway is required for early development in Arabidopsis. Embo J 2003, 22, 1762-70.
    • (2003) Embo J , vol.22 , pp. 1762-1770
    • Dharmasiri, S.1    Dharmasiri, N.2    Hellmann, H.3    Estelle, M.4
  • 89
    • 0037083528 scopus 로고    scopus 로고
    • Cytoskeletal regulation by the Nedd8 ubiquitin-like protein modification pathway
    • Kurz, T. et al. Cytoskeletal regulation by the Nedd8 ubiquitin-like protein modification pathway. Science 2002, 295, 1294-8.
    • (2002) Science , vol.295 , pp. 1294-1298
    • Kurz, T.1
  • 90
    • 0034600951 scopus 로고    scopus 로고
    • Covalent modifier NEDD8 is essential for SCF ubiquitinligase in fission yeast
    • Osaka, F. et al. Covalent modifier NEDD8 is essential for SCF ubiquitinligase in fission yeast. Embo J 2000, 19, 3475-84.
    • (2000) Embo J , vol.19 , pp. 3475-3484
    • Osaka, F.1
  • 91
    • 0035969236 scopus 로고    scopus 로고
    • The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice
    • Tateishi, K., Omata, M., Tanaka, K. and Chiba, T. The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice. J Cell Biol 2001, 155, 571-9.
    • (2001) J Cell Biol , vol.155 , pp. 571-579
    • Tateishi, K.1    Omata, M.2    Tanaka, K.3    Chiba, T.4
  • 92
    • 0034117282 scopus 로고    scopus 로고
    • Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of Ikappa-Balpha
    • Read, M. A. et al. Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of Ikappa-Balpha. Mol Cell Biol 2000, 20, 2326-33.
    • (2000) Mol Cell Biol , vol.20 , pp. 2326-2333
    • Read, M.A.1
  • 93
    • 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. and Pan, Z. Q. Conjugation of Nedd8 to CUL1 enhances the ability of the ROC1-CUL1 complex to promote ubiquitin polymerization. J Biol Chem 2000, 275, 32317-24.
    • (2000) J Biol Chem , vol.275 , pp. 32317-32324
    • Wu, K.1    Chen, A.2    Pan, Z.Q.3
  • 94
    • 0034696819 scopus 로고    scopus 로고
    • Modification of cullin-1 by ubiquitin-like protein Nedd8 enhances the activity of SCF(skp2) toward p27(kip1)
    • Morimoto, M., Nishida, T., Honda, R. and Yasuda, H. Modification of cullin-1 by ubiquitin-like protein Nedd8 enhances the activity of SCF(skp2) toward p27(kip1). Biochem Biophys Res Commun 2000, 270, 1093-6.
    • (2000) Biochem Biophys Res Commun , vol.270 , pp. 1093-1096
    • Morimoto, M.1    Nishida, T.2    Honda, R.3    Yasuda, H.4
  • 95
    • 0036924046 scopus 로고    scopus 로고
    • CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex
    • Zheng, J. et al. CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. Mol Cell 2002, 10, 1519-26.
    • (2002) Mol Cell , vol.10 , pp. 1519-1526
    • Zheng, J.1
  • 96
    • 0036929129 scopus 로고    scopus 로고
    • NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases
    • Liu, J., Furukawa, M., Matsumoto, T. and Xiong, Y. NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases. Mol Cell 2002, 10, 1511-8.
    • (2002) Mol Cell , vol.10 , pp. 1511-1518
    • Liu, J.1    Furukawa, M.2    Matsumoto, T.3    Xiong, Y.4
  • 97
    • 0033602227 scopus 로고    scopus 로고
    • The F-box protein beta-TrCP associates with phosphorylated beta-catenin and regulates its activity in the cell
    • Hart, M. et al. The F-box protein beta-TrCP associates with phosphorylated beta-catenin and regulates its activity in the cell. Curr Biol 1999, 9, 207-10.
    • (1999) Curr Biol , vol.9 , pp. 207-210
    • Hart, M.1
  • 98
    • 0036781052 scopus 로고    scopus 로고
    • NF-kappaB regulation in the immune system
    • Li, Q. and Verma, I. M. NF-kappaB regulation in the immune system. Nat Rev Immunol 2002, 2, 725-34.
    • (2002) Nat Rev Immunol , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 99
    • 0033895709 scopus 로고    scopus 로고
    • Wnt signaling and cancer
    • Polakis, P. Wnt signaling and cancer. Genes Dev 2000, 14, 1837-51.
    • (2000) Genes Dev , vol.14 , pp. 1837-1851
    • Polakis, P.1
  • 100
    • 0033054464 scopus 로고    scopus 로고
    • The oncogenic activation of beta-catenin
    • Polakis, P. The oncogenic activation of beta-catenin. Curr Opin Genet Dev 1999, 9, 15-21.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 15-21
    • Polakis, P.1
  • 101
    • 0029146930 scopus 로고
    • Signal-induced sitespecific phosphorylation targets I kappa B alpha to the ubiquitinproteasome pathway
    • Chen, Z. et al. Signal-induced sitespecific phosphorylation targets I kappa B alpha to the ubiquitinproteasome pathway. Genes Dev 1995, 9, 1586-97.
    • (1995) Genes Dev , vol.9 , pp. 1586-1597
    • Chen, Z.1
  • 102
    • 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. and Deshaies, R. J. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 1997, 91, 221-30.
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 103
    • 0037462424 scopus 로고    scopus 로고
    • Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase
    • Orlicky, S., Tang, X., Willems, A., Tyers, M. and Sicheri, F. Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase. Cell 2003, 112, 243-56.
    • (2003) Cell , vol.112 , pp. 243-256
    • Orlicky, S.1    Tang, X.2    Willems, A.3    Tyers, M.4    Sicheri, F.5
  • 104
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of beta-catenin
    • Huber, A. H., Nelson, W. J. and Weis, W. I. Three-dimensional structure of the armadillo repeat region of beta-catenin. Cell 1997, 90, 871-82.
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1    Nelson, W.J.2    Weis, W.I.3
  • 105
    • 0016502735 scopus 로고
    • Distribution of end-to-end distances of oligopeptides in solution as estimated by energy transfer
    • Haas, E., Wilchek, M., Katchalski-Katzir, E. and Steinberg, I. Z. Distribution of end-to-end distances of oligopeptides in solution as estimated by energy transfer. Proc Natl Acad Sci USA 1975, 72, 1807-11.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 1807-1811
    • Haas, E.1    Wilchek, M.2    Katchalski-Katzir, E.3    Steinberg, I.Z.4
  • 106
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer
    • VanDemark, A. P., Hofmann, R. M., Tsui, C., Pickart, C. M. and Wolberger, C. Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer. Cell 2001, 105, 711-20.
    • (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
  • 107
    • 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
    • Miura, T., Klaus, W., Gsell, B., Miyamoto, C. and Senn, H. 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 1999, 290, 213-28.
    • (1999) J Mol Biol , vol.290 , pp. 213-228
    • Miura, T.1    Klaus, W.2    Gsell, B.3    Miyamoto, C.4    Senn, H.5
  • 109
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitinconjugating enzyme Ubc9 and RanGAP1
    • Bernier-Villamor, V., Sampson, D. A., Matunis, M. J. and Lima, C. D. Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitinconjugating enzyme Ubc9 and RanGAP1. Cell 2002, 108, 345-56.
    • (2002) Cell , vol.108 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3    Lima, C.D.4


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