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Volumn 11, Issue 10, 2004, Pages 927-935

A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; NEDD8 PROTEIN; PROTEIN APPB1 UBA3; PROTEIN NEDD8 E1; PROTEIN NEDD8 E2; PROTEIN SUBUNIT; PROTEIN UBC12; PROTEIN UBC12N26; THIOESTER; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 4744338840     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb826     Document Type: Article
Times cited : (127)

References (51)
  • 1
    • 0038434056 scopus 로고    scopus 로고
    • A superfamily of protein tags: Ubiquitin, SUMO and related modifiers
    • Schwartz, D.C. & Hochstrasser, M. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem. Sci. 28, 321-328 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 321-328
    • Schwartz, D.C.1    Hochstrasser, M.2
  • 2
    • 0032053829 scopus 로고    scopus 로고
    • Modification of yeast Cdc53p by the ubiquitin-related protein rub 1p affects function of the SCFCdc4 complex
    • Lammer, D. et al. Modification of yeast Cdc53p by the ubiquitin-related protein rub1p affects function of the SCFCdc4 complex. Genes Dev. 12, 914-926 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 914-926
    • Lammer, D.1
  • 3
    • 0032522382 scopus 로고    scopus 로고
    • A novel protein modification pathway related to the ubiquitin system
    • Liakopoulos, D., Doenges, G., Matuschewski, K. & Jentsch, S. A novel protein modification pathway related to the ubiquitin system. EMBO J. 17, 2208-2214 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2208-2214
    • Liakopoulos, D.1    Doenges, G.2    Matuschewski, K.3    Jentsch, S.4
  • 4
    • 0032146145 scopus 로고    scopus 로고
    • A new NEDD8-ligating system for cullin-4A
    • Osaka, F. et al. A new NEDD8-ligating system for cullin-4A. Genes Dev. 12, 2263-2268 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 2263-2268
    • Osaka, F.1
  • 5
    • 0034117282 scopus 로고    scopus 로고
    • Nedd8 modification of cul-1 activates SCF(β(TrCP))-dependent ubiquitination of IκBα
    • Read, M.A. et al. Nedd8 modification of cul-1 activates SCF(β(TrCP))-dependent ubiquitination of IκBα. Mol. Cell. Biol. 20, 2326-2333 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2326-2333
    • Read, M.A.1
  • 6
    • 0034644650 scopus 로고    scopus 로고
    • Conjugation of Nedd8 to CUL1 enhances the ability of the ROC1-CUL 1 complex to promote ubiquitin polymerization
    • Wu, K., Chen, A. & Pan, Z.Q. Conjugation of Nedd8 to CUL1 enhances the ability of the ROC1-CUL1 complex to promote ubiquitin polymerization. J. Biol. Chem. 275, 32317-32324 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 32317-32324
    • Wu, K.1    Chen, A.2    Pan, Z.Q.3
  • 7
    • 0036929129 scopus 로고    scopus 로고
    • NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP 1 binding and SCF ligases
    • Liu, J., Furukawa, M., Matsumoto, T. & Xiong, Y. NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases. Mol. Cell 10, 1511-1518 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 1511-1518
    • Liu, J.1    Furukawa, M.2    Matsumoto, T.3    Xiong, Y.4
  • 8
    • 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 10, 1519-1526 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 1519-1526
    • Zheng, J.1
  • 9
    • 0034600951 scopus 로고    scopus 로고
    • Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission yeast
    • Osaka, F. et al. Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission yeast. EMBO J. 19, 3475-3484 (2000).
    • (2000) EMBO J. , vol.19 , pp. 3475-3484
    • Osaka, F.1
  • 10
    • 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. & Chiba, T. The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice. J. Cell Biol. 155, 571-579 (2001).
    • (2001) J. Cell Biol. , vol.155 , pp. 571-579
    • Tateishi, K.1    Omata, M.2    Tanaka, K.3    Chiba, T.4
  • 11
    • 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 295, 1294-1298 (2002).
    • (2002) Science , vol.295 , pp. 1294-1298
    • Kurz, T.1
  • 12
    • 0032511111 scopus 로고    scopus 로고
    • The ubiquitin-related protein RUB 1 and auxin response in Arabidopsis
    • Pozo, J.C., Timpte, C., Tan, S., Callis, J. & Estelle, M. The ubiquitin-related protein RUB1 and auxin response in Arabidopsis. Science 280, 1760-1763 (1998).
    • (1998) Science , vol.280 , pp. 1760-1763
    • Pozo, J.C.1    Timpte, C.2    Tan, S.3    Callis, J.4    Estelle, M.5
  • 13
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • Hochstrasser, M. Evolution and function of ubiquitin-like protein-conjugation systems. Nat. Cell Biol. 2, E153-E157 (2000).
    • (2000) Nat. Cell Biol. , vol.2
    • Hochstrasser, M.1
  • 14
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 15
    • 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
  • 16
    • 0033565867 scopus 로고    scopus 로고
    • Structural basis for the specificity of ubiquitin C-terminal hydrolases
    • Johnston, S.C., Riddle, S.M., Cohen, R.E. & Hill, C.P. Structural basis for the specificity of ubiquitin C-terminal hydrolases. EMBO J. 18, 3877-3887 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3877-3887
    • Johnston, S.C.1    Riddle, S.M.2    Cohen, R.E.3    Hill, C.P.4
  • 17
    • 0033546283 scopus 로고    scopus 로고
    • The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1)
    • Liu, Q. et al. The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1). J. Biol. Chem. 274, 16979-16987 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 16979-16987
    • Liu, Q.1
  • 18
    • 0033638223 scopus 로고    scopus 로고
    • Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
    • Mossessova, E. & Lima, C.D. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell 5, 865-876 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 865-876
    • Mossessova, E.1    Lima, C.D.2
  • 19
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cb1-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng, N., Wang, P., Jeffrey, P.D. & Pavletich, N.P. Structure of a c-Cb1-UbcH7 complex: RING 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
  • 21
    • 0034788322 scopus 로고    scopus 로고
    • Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail
    • Hamilton, K.S. et al. Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail. Structured 9, 897-904 (2001).
    • (2001) Structured , vol.9 , pp. 897-904
    • Hamilton, K.S.1
  • 22
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
    • Bernier-Villamor, V, Sampson, D.A., Matunis, M.J. & Lima, C.D. Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell 108, 345-356 (2002).
    • (2002) Cell , vol.108 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3    Lima, C.D.4
  • 23
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu, M. et al. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 111, 1041-1054 (2002).
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1
  • 25
    • 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
  • 26
    • 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
    • Walden, H. et al. The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1. Mol. Cell 12, 1427-1437 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1427-1437
    • Walden, H.1
  • 27
    • 0033781272 scopus 로고    scopus 로고
    • The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDDS modification, and ubiquitin ligase activity of CUL1
    • Furukawa, M., Zhang, Y., McCarville, J., Ohta, T. & Xiong, Y. The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDDS modification, and ubiquitin ligase activity of CUL1. Mol. Cell. Biol. 20, 8185-8197 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8185-8197
    • Furukawa, M.1    Zhang, Y.2    McCarville, J.3    Ohta, T.4    Xiong, Y.5
  • 28
    • 0037456828 scopus 로고    scopus 로고
    • Insights into the ubiquitin transfer cascade from the structure of the E1 for NEDD8
    • Walden, H., Podgorski, M.S. & Schulman, B.A. Insights into the ubiquitin transfer cascade from the structure of the E1 for NEDD8. Nature 422, 330-334 (2003).
    • (2003) Nature , vol.422 , pp. 330-334
    • Walden, H.1    Podgorski, M.S.2    Schulman, B.A.3
  • 29
    • 0025861901 scopus 로고
    • Myc rescue of a mutant CSF-1 receptor impaired in mitogenic signalling
    • Roussel, M.F., Cleveland, J.L., Shurtleff, S.A. & Sherr, C.J. Myc rescue of a mutant CSF-1 receptor impaired in mitogenic signalling. Nature 353, 361-363 (1991).
    • (1991) Nature , vol.353 , pp. 361-363
    • Roussel, M.F.1    Cleveland, J.L.2    Shurtleff, S.A.3    Sherr, C.J.4
  • 31
    • 0024397970 scopus 로고
    • Mouse NIH 3T3 cells expressing human colony-stimulating factor 1 (CSF-1) receptors overgrow in serum-free medium containing human CSF-1 as their only growth factor
    • Roussel, M.F. & Sherr, C.J. Mouse NIH 3T3 cells expressing human colony-stimulating factor 1 (CSF-1) receptors overgrow in serum-free medium containing human CSF-1 as their only growth factor. Proc. Natl. Acad. Sci. USA 86, 7924-7927 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7924-7927
    • Roussel, M.F.1    Sherr, C.J.2
  • 32
    • 0035891318 scopus 로고    scopus 로고
    • Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
    • Lake, M.W., Wuebbens, M.M., Rajagopalan, K.V. & Schindelin, H. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 414, 325-329 (2001).
    • (2001) Nature , vol.414 , pp. 325-329
    • Lake, M.W.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 33
    • 0032802393 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Inhibition and substrate recognition
    • Endicott, J.A., Noble, M.E. & Tucker, J.A. Cyclin-dependent kinases: inhibition and substrate recognition. Curr. Opin. Struct. Biol. 9, 738-744 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 738-744
    • Endicott, J.A.1    Noble, M.E.2    Tucker, J.A.3
  • 34
    • 0037954572 scopus 로고    scopus 로고
    • Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
    • Biondi, R.M. & Nebreda, A.R. Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions. Biochem. J. 372, 1-13 (2003).
    • (2003) Biochem. J. , vol.372 , pp. 1-13
    • Biondi, R.M.1    Nebreda, A.R.2
  • 35
    • 0035910422 scopus 로고    scopus 로고
    • A bipartite substrate recognition motif for cyclin-dependent kinases
    • Takeda, D.Y., Wohlschlegel, J.A. & Dutta, A. A bipartite substrate recognition motif for cyclin-dependent kinases. J. Biol. Chem. 276, 1993-1997 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 1993-1997
    • Takeda, D.Y.1    Wohlschlegel, J.A.2    Dutta, A.3
  • 36
    • 0242661605 scopus 로고    scopus 로고
    • Bull and But2 proteins bind to Uba3, a catalytic subunit of E1 for neddylation, in fission yeast
    • Yashiroda, H. & Tanaka, K. Bull and But2 proteins bind to Uba3, a catalytic subunit of E1 for neddylation, in fission yeast. Biochem. Biophys. Res. Commun. 311, 691-695 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 691-695
    • Yashiroda, H.1    Tanaka, K.2
  • 37
    • 0035906430 scopus 로고    scopus 로고
    • Promotion of NEDD8-CUL1 conjugate cleavage by COP9 signalosome
    • Lyapina, S. et al. Promotion of NEDD8-CUL1 conjugate cleavage by COP9 signalosome. Science 232, 1382-1385 (2001).
    • (2001) Science , vol.232 , pp. 1382-1385
    • Lyapina, S.1
  • 38
    • 0026776440 scopus 로고
    • Identification of a portable determinant of cell cycle function within the carboxyl-terminal domain of the yeast CDC34 (UBC3) ubiquitin conjugating (E2) enzyme
    • Kolman, C.J., Toth, J. & Gonda, D.K. Identification of a portable determinant of cell cycle function within the carboxyl-terminal domain of the yeast CDC34 (UBC3) ubiquitin conjugating (E2) enzyme. EMBO J. 11, 3081-3090 (1992).
    • (1992) EMBO J. , vol.11 , pp. 3081-3090
    • Kolman, C.J.1    Toth, J.2    Gonda, D.K.3
  • 39
    • 0026772161 scopus 로고
    • A chimeric ubiquitin conjugating enzyme that combines the cell cycle properties of CDC34 (UBC3) and the DNA repair properties of RAD6 (UBC2): Implications for the structure, function and evolution of the E2s
    • Silver, E.T., Gwozd, T.J., Ptak, C., Goebl, M. & Ellison, M. J. A chimeric ubiquitin conjugating enzyme that combines the cell cycle properties of CDC34 (UBC3) and the DNA repair properties of RAD6 (UBC2): implications for the structure, function and evolution of the E2s. EMBO J. 11, 3091-3098 (1992).
    • (1992) EMBO J. , vol.11 , pp. 3091-3098
    • Silver, E.T.1    Gwozd, T.J.2    Ptak, C.3    Goebl, M.4    Ellison, M.J.5
  • 40
    • 0030772445 scopus 로고    scopus 로고
    • Structure and function of ubiquitin conjugating enzyme E2-25K: The tail is a core-dependent activity element
    • Haldeman, M.T., Xia, G., Kasperek, E.M. & Pickart, C.M. Structure and function of ubiquitin conjugating enzyme E2-25K: the tail is a core-dependent activity element. Biochemistry 36, 10526-10537 (1997).
    • (1997) Biochemistry , vol.36 , pp. 10526-10537
    • Haldeman, M.T.1    Xia, G.2    Kasperek, E.M.3    Pickart, C.M.4
  • 41
    • 0023972198 scopus 로고    scopus 로고
    • Domain structure and functional analysis of the carboxyl-terminal polyacidic sequence of the RAD6 protein of Saccharomyces cerevisiae
    • Morrison, A., Miller, E.J. & Prakash, L. Domain structure and functional analysis of the carboxyl-terminal polyacidic sequence of the RAD6 protein of Saccharomyces cerevisiae. Mol. Cell. Biol., 8, 1179-1185 (1998).
    • (1998) Mol. Cell. Biol. , vol.8 , pp. 1179-1185
    • Morrison, A.1    Miller, E.J.2    Prakash, L.3
  • 42
    • 0027316341 scopus 로고
    • N-recognin/Ubc2 interactions in the N-end rule pathway
    • Madura, K., Dohmen, R.J. & Varshavsky, A. N-recognin/Ubc2 interactions in the N-end rule pathway. J. Biol. Chem. 268, 12046-12054 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 12046-12054
    • Madura, K.1    Dohmen, R.J.2    Varshavsky, A.3
  • 43
    • 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
  • 44
    • 0037033071 scopus 로고    scopus 로고
    • Identification of a multifunctional binding site on Ubc 9p required for Smt3p conjugation
    • Bencsath, K.P., Podgorski, M.S., Pagala, V.R., Slaughter, C.A. & Schulman, B.A. Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation. J. Biol. Chem. 277, 47938-47945 (2002).
    • (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
  • 45
    • 18344391432 scopus 로고    scopus 로고
    • Skp2 SCF ubiquitin ligase complex
    • Skp2 SCF ubiquitin ligase complex. Nature 416, 703-709 (2002).
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1
  • 46
    • 0037697382 scopus 로고    scopus 로고
    • Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba 3 heterodimer
    • Bohnsack, R.N. & Haas, A.L. Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer. J. Biol. Chem. 278, 26823-26830 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 26823-26830
    • Bohnsack, R.N.1    Haas, A.L.2
  • 47
    • 0033582717 scopus 로고    scopus 로고
    • MaRX: An approach to genetics in mammalian cells
    • Hannon, G.J. et al. MaRX: an approach to genetics in mammalian cells. Science 283, 1129-1130 (1999).
    • (1999) Science , vol.283 , pp. 1129-1130
    • Hannon, G.J.1
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 176, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.176 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 49
    • 1242274650 scopus 로고    scopus 로고
    • Automated protein crystal structure determination using ELVES
    • Holton, J. & Alber, T. Automated protein crystal structure determination using ELVES. Proc. Natl. Acad. Sci. USA 101, 1537-1542 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1537-1542
    • Holton, J.1    Alber, T.2
  • 50
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 51
    • 0032567528 scopus 로고    scopus 로고
    • Crystal structure of the human ubiquitin-like protein NEDD 8 and interactions with ubiquitin pathway enzymes
    • Whitby, F.G., Xia, G., Pickart, C.M. & Hill, C.P. Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes. J. Biol. Chem. 273, 34983-34991 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 34983-34991
    • Whitby, F.G.1    Xia, G.2    Pickart, C.M.3    Hill, C.P.4


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