메뉴 건너뛰기




Volumn 15, Issue 11, 2007, Pages 1493-1504

Structure of the SOCS4-ElonginB/C Complex Reveals a Distinct SOCS Box Interface and the Molecular Basis for SOCS-Dependent EGFR Degradation

Author keywords

PROTEINS; SIGNALING

Indexed keywords

CYTOKINE; ELONGIN BC; EPIDERMAL GROWTH FACTOR RECEPTOR; GROWTH HORMONE RECEPTOR; JANUS KINASE 2; PEPTIDE; PROTEIN SH2; STAT3 PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING; SUPPRESSOR OF CYTOKINE SIGNALING 1; SUPPRESSOR OF CYTOKINE SIGNALING 2; SUPPRESSOR OF CYTOKINE SIGNALING 3; SUPPRESSOR OF CYTOKINE SIGNALING 4; UNCLASSIFIED DRUG;

EID: 35748984946     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2007.09.016     Document Type: Article
Times cited : (107)

References (59)
  • 1
    • 84986522918 scopus 로고
    • ICM: a new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation
    • Abagyan R.A., Totrov M., and Kuznetsov D. ICM: a new method for protein modeling and design: applications to docking and structure prediction from the distorted native conformation. J. Comput. Chem. 15 (1994) 488-506
    • (1994) J. Comput. Chem. , vol.15 , pp. 488-506
    • Abagyan, R.A.1    Totrov, M.2    Kuznetsov, D.3
  • 2
    • 33746826011 scopus 로고    scopus 로고
    • JAK/STAT signalling in Drosophila: insights into conserved regulatory and cellular functions
    • Arbouzova N.I., and Zeidler M.P. JAK/STAT signalling in Drosophila: insights into conserved regulatory and cellular functions. Development 133 (2006) 2605-2616
    • (2006) Development , vol.133 , pp. 2605-2616
    • Arbouzova, N.I.1    Zeidler, M.P.2
  • 3
    • 33646697347 scopus 로고    scopus 로고
    • The structure of SOCS3 reveals the basis of the extended SH2 domain function and identifies an unstructured insertion that regulates stability
    • Babon J.J., McManus E.J., Yao S., DeSouza D.P., Mielke L.A., Sprigg N.S., Willson T.A., Hilton D.J., Nicola N.A., Baca M., et al. The structure of SOCS3 reveals the basis of the extended SH2 domain function and identifies an unstructured insertion that regulates stability. Mol. Cell 22 (2006) 205-216
    • (2006) Mol. Cell , vol.22 , pp. 205-216
    • Babon, J.J.1    McManus, E.J.2    Yao, S.3    DeSouza, D.P.4    Mielke, L.A.5    Sprigg, N.S.6    Willson, T.A.7    Hilton, D.J.8    Nicola, N.A.9    Baca, M.10
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 5
    • 0035871693 scopus 로고    scopus 로고
    • A common epitope is shared by activated signal transducer and activator of transcription-5 (STAT5) and the phosphorylated erythropoietin receptor: implications for the docking model of STAT activation
    • Barber D.L., Beattie B.K., Mason J.M., Nguyen M.H., Yoakim M., Neel B.G., D'Andrea A.D., and Frank D.A. A common epitope is shared by activated signal transducer and activator of transcription-5 (STAT5) and the phosphorylated erythropoietin receptor: implications for the docking model of STAT activation. Blood 97 (2001) 2230-2237
    • (2001) Blood , vol.97 , pp. 2230-2237
    • Barber, D.L.1    Beattie, B.K.2    Mason, J.M.3    Nguyen, M.H.4    Yoakim, M.5    Neel, B.G.6    D'Andrea, A.D.7    Frank, D.A.8
  • 6
    • 1842478134 scopus 로고    scopus 로고
    • Suppressor of cytokine signaling 6 associates with KIT and regulates KIT receptor signaling
    • Bayle J., Letard S., Frank R., Dubreuil P., and De Sepulveda P. Suppressor of cytokine signaling 6 associates with KIT and regulates KIT receptor signaling. J. Biol. Chem. 279 (2004) 12249-12259
    • (2004) J. Biol. Chem. , vol.279 , pp. 12249-12259
    • Bayle, J.1    Letard, S.2    Frank, R.3    Dubreuil, P.4    De Sepulveda, P.5
  • 7
    • 33746860377 scopus 로고    scopus 로고
    • Structural basis for phosphotyrosine recognition by suppressor of cytokine signaling-3
    • Bergamin E., Wu J., and Hubbard S. Structural basis for phosphotyrosine recognition by suppressor of cytokine signaling-3. Structure 14 (2006) 1285-1292
    • (2006) Structure , vol.14 , pp. 1285-1292
    • Bergamin, E.1    Wu, J.2    Hubbard, S.3
  • 8
    • 33646733227 scopus 로고    scopus 로고
    • Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase
    • Bullock A.N., Debreczeni J.E., Edwards A.M., Sundstrom M., and Knapp S. Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase. Proc. Natl. Acad. Sci. USA 103 (2006) 7637-7642
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7637-7642
    • Bullock, A.N.1    Debreczeni, J.E.2    Edwards, A.M.3    Sundstrom, M.4    Knapp, S.5
  • 9
    • 0037130445 scopus 로고    scopus 로고
    • SOCS36E, a novel Drosophila SOCS protein, suppresses JAK/STAT and EGF-R signalling in the imaginal wing disc
    • Callus B.A., and Mathey-Prevot B. SOCS36E, a novel Drosophila SOCS protein, suppresses JAK/STAT and EGF-R signalling in the imaginal wing disc. Oncogene 21 (2002) 4812-4821
    • (2002) Oncogene , vol.21 , pp. 4812-4821
    • Callus, B.A.1    Mathey-Prevot, B.2
  • 10
    • 0032577678 scopus 로고    scopus 로고
    • Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA
    • Chen X., Vinkemeier U., Zhao Y., Jeruzalmi D., Darnell J.J., and Kuriyan J. Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA. Cell 93 (1998) 827-839
    • (1998) Cell , vol.93 , pp. 827-839
    • Chen, X.1    Vinkemeier, U.2    Zhao, Y.3    Jeruzalmi, D.4    Darnell, J.J.5    Kuriyan, J.6
  • 11
    • 0000374718 scopus 로고    scopus 로고
    • The Grb2-mSos1 complex binds phosphopeptides with higher affinity than Grb2
    • Chook Y.M., Gish G.D., Kay C.M., Pai E.F., and Pawson T. The Grb2-mSos1 complex binds phosphopeptides with higher affinity than Grb2. J. Biol. Chem. 271 (1996) 30472-30478
    • (1996) J. Biol. Chem. , vol.271 , pp. 30472-30478
    • Chook, Y.M.1    Gish, G.D.2    Kay, C.M.3    Pai, E.F.4    Pawson, T.5
  • 12
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: towards the systems level
    • Citri A., and Yarden Y. EGF-ERBB signalling: towards the systems level. Nat. Rev. Mol. Cell Biol. 7 (2006) 505-516
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 13
    • 0037162397 scopus 로고    scopus 로고
    • SH2 domains from suppressor of cytokine signaling-3 and protein tyrosine phosphatase SHP-2 have similar binding specificities
    • De Souza D., Fabri L., Nash A., Hilton D., Nicola N., and Baca M. SH2 domains from suppressor of cytokine signaling-3 and protein tyrosine phosphatase SHP-2 have similar binding specificities. Biochemistry 41 (2002) 9229-9236
    • (2002) Biochemistry , vol.41 , pp. 9229-9236
    • De Souza, D.1    Fabri, L.2    Nash, A.3    Hilton, D.4    Nicola, N.5    Baca, M.6
  • 16
    • 1942469355 scopus 로고    scopus 로고
    • SOCS2 induces neurite outgrowth by regulation of epidermal growth factor receptor activation
    • Goldshmit Y., Walters C.E., Scott H.J., Greenhalgh C.J., and Turnley A.M. SOCS2 induces neurite outgrowth by regulation of epidermal growth factor receptor activation. J. Biol. Chem. 279 (2004) 16349-16355
    • (2004) J. Biol. Chem. , vol.279 , pp. 16349-16355
    • Goldshmit, Y.1    Walters, C.E.2    Scott, H.J.3    Greenhalgh, C.J.4    Turnley, A.M.5
  • 18
    • 34047249627 scopus 로고    scopus 로고
    • Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases
    • Hao B., Oehlmann S., Sowa M.E., Harper J.W., and Pavletich N.P. Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases. Mol. Cell 26 (2007) 131-143
    • (2007) Mol. Cell , vol.26 , pp. 131-143
    • Hao, B.1    Oehlmann, S.2    Sowa, M.E.3    Harper, J.W.4    Pavletich, N.P.5
  • 19
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change; new results on citrate synthase and T4 lysozyme
    • Hayward S., and Berendsen H. Systematic analysis of domain motions in proteins from conformational change; new results on citrate synthase and T4 lysozyme. Proteins 30 (1998) 144-154
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.2
  • 21
    • 0028845212 scopus 로고
    • Cytokine receptor signalling
    • Ihle J.N. Cytokine receptor signalling. Nature 377 (1995) 591-594
    • (1995) Nature , vol.377 , pp. 591-594
    • Ihle, J.N.1
  • 22
    • 22444439210 scopus 로고    scopus 로고
    • Backbone nuclear relaxation characteristics and calorimetric investigation of the human Grb7-SH2/erbB2 peptide complex
    • Ivancic M., Spuches A.M., Guth E.C., Daugherty M.A., Wilcox D.E., and Lyons B.A. Backbone nuclear relaxation characteristics and calorimetric investigation of the human Grb7-SH2/erbB2 peptide complex. Protein Sci. 14 (2005) 1556-1569
    • (2005) Protein Sci. , vol.14 , pp. 1556-1569
    • Ivancic, M.1    Spuches, A.M.2    Guth, E.C.3    Daugherty, M.A.4    Wilcox, D.E.5    Lyons, B.A.6
  • 23
    • 30544449081 scopus 로고    scopus 로고
    • A quantitative protein interaction network for the ErbB receptors using protein microarrays
    • Jones R.B., Gordus A., Krall J.A., and MacBeath G. A quantitative protein interaction network for the ErbB receptors using protein microarrays. Nature 439 (2006) 168-174
    • (2006) Nature , vol.439 , pp. 168-174
    • Jones, R.B.1    Gordus, A.2    Krall, J.A.3    MacBeath, G.4
  • 24
    • 0032535364 scopus 로고    scopus 로고
    • The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families
    • Kamura T., Sato S., Haque D., Liu L., Kaelin W.J., Conaway R., and Conaway J. The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families. Genes Dev. 12 (1998) 3872-3881
    • (1998) Genes Dev. , vol.12 , pp. 3872-3881
    • Kamura, T.1    Sato, S.2    Haque, D.3    Liu, L.4    Kaelin, W.J.5    Conaway, R.6    Conaway, J.7
  • 25
    • 10644276385 scopus 로고    scopus 로고
    • VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases
    • Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D., Conaway R.C., Conaway J.W., and Nakayama K.I. VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases. Genes Dev. 18 (2004) 3055-3065
    • (2004) Genes Dev. , vol.18 , pp. 3055-3065
    • Kamura, T.1    Maenaka, K.2    Kotoshiba, S.3    Matsumoto, M.4    Kohda, D.5    Conaway, R.C.6    Conaway, J.W.7    Nakayama, K.I.8
  • 29
    • 0028773467 scopus 로고
    • Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase
    • Lee C.H., Kominos D., Jacques S., Margolis B., Schlessinger J., Shoelson S.E., and Kuriyan J. Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase. Structure 2 (1994) 423-438
    • (1994) Structure , vol.2 , pp. 423-438
    • Lee, C.H.1    Kominos, D.2    Jacques, S.3    Margolis, B.4    Schlessinger, J.5    Shoelson, S.E.6    Kuriyan, J.7
  • 30
    • 0028151416 scopus 로고
    • Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2
    • Lemmon M.A., Ladbury J.E., Mandiyan V., Zhou M., and Schlessinger J. Independent binding of peptide ligands to the SH2 and SH3 domains of Grb2. J. Biol. Chem. 269 (1994) 31653-31658
    • (1994) J. Biol. Chem. , vol.269 , pp. 31653-31658
    • Lemmon, M.A.1    Ladbury, J.E.2    Mandiyan, V.3    Zhou, M.4    Schlessinger, J.5
  • 32
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 33
    • 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., and Eck M. Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase. Nature 398 (1999) 84-90
    • (1999) Nature , vol.398 , pp. 84-90
    • Meng, W.1    Sawasdikosol, S.2    Burakoff, S.3    Eck, M.4
  • 37
    • 0033555258 scopus 로고    scopus 로고
    • Mutational analyses of the SOCS proteins suggest a dual domain requirement but distinct mechanisms for inhibition of LIF and IL-6 signal transduction
    • Nicholson S.E., Willson T.A., Farley A., Starr R., Zhang J.G., Baca M., Alexander W.S., Metcalf D., Hilton D.J., and Nicola N.A. Mutational analyses of the SOCS proteins suggest a dual domain requirement but distinct mechanisms for inhibition of LIF and IL-6 signal transduction. EMBO J. 18 (1999) 375-385
    • (1999) EMBO J. , vol.18 , pp. 375-385
    • Nicholson, S.E.1    Willson, T.A.2    Farley, A.3    Starr, R.4    Zhang, J.G.5    Baca, M.6    Alexander, W.S.7    Metcalf, D.8    Hilton, D.J.9    Nicola, N.A.10
  • 41
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski M.D., and Deshaies R.J. Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 6 (2005) 9-20
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 42
    • 0037069388 scopus 로고    scopus 로고
    • Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3
    • Qiu X.B., and Goldberg A.L. Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and degradation of the epidermal growth factor receptor family member, ErbB3. Proc. Natl. Acad. Sci. USA 99 (2002) 14843-14848
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14843-14848
    • Qiu, X.B.1    Goldberg, A.L.2
  • 43
    • 10444257919 scopus 로고    scopus 로고
    • Two Drosophila suppressors of cytokine signaling (SOCS) differentially regulate JAK and EGFR pathway activities
    • Rawlings J.S., Rennebeck G., Harrison S.M., Xi R., and Harrison D.A. Two Drosophila suppressors of cytokine signaling (SOCS) differentially regulate JAK and EGFR pathway activities. BMC Cell Biol. 5 (2004) 38
    • (2004) BMC Cell Biol. , vol.5 , pp. 38
    • Rawlings, J.S.1    Rennebeck, G.2    Harrison, S.M.3    Xi, R.4    Harrison, D.A.5
  • 44
    • 1542305566 scopus 로고    scopus 로고
    • An oriented peptide array library (OPAL) strategy to study protein-protein interactions
    • Rodriguez M., Li S.S., Harper J.W., and Songyang Z. An oriented peptide array library (OPAL) strategy to study protein-protein interactions. J. Biol. Chem. 279 (2004) 8802-8807
    • (2004) J. Biol. Chem. , vol.279 , pp. 8802-8807
    • Rodriguez, M.1    Li, S.S.2    Harper, J.W.3    Songyang, Z.4
  • 45
    • 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. 277 (2002) 42394-42398
    • (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
  • 46
    • 33746905531 scopus 로고    scopus 로고
    • Phosphotyrosine interactome of the ErbB-receptor kinase family
    • Schulze W.X., Deng L., and Mann M. Phosphotyrosine interactome of the ErbB-receptor kinase family. Mol. Syst. Biol. 1 (2005) E1-E13
    • (2005) Mol. Syst. Biol. , vol.1
    • Schulze, W.X.1    Deng, L.2    Mann, M.3
  • 48
    • 0028875162 scopus 로고
    • Recognition and specificity in protein tyrosine kinase-mediated signalling
    • Songyang Z., and Cantley L.C. Recognition and specificity in protein tyrosine kinase-mediated signalling. Trends Biochem. Sci. 20 (1995) 470-475
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 470-475
    • Songyang, Z.1    Cantley, L.C.2
  • 51
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function
    • Stebbins C.E., Kaelin Jr. W.G., and Pavletich N.P. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 284 (1999) 455-461
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin Jr., W.G.2    Pavletich, N.P.3
  • 53
    • 34247172195 scopus 로고    scopus 로고
    • Both the suppressor of cytokine signaling 1 (SOCS-1) kinase inhibitory region and SOCS-1 mimetic bind to JAK2 autophosphorylation site: implications for the development of a SOCS-1 antagonist
    • Waiboci L.W., Ahmed C.M., Mujtaba M.G., Flowers L.O., Martin J.P., Haider M.I., and Johnson H.M. Both the suppressor of cytokine signaling 1 (SOCS-1) kinase inhibitory region and SOCS-1 mimetic bind to JAK2 autophosphorylation site: implications for the development of a SOCS-1 antagonist. J. Immunol. 178 (2007) 5058-5068
    • (2007) J. Immunol. , vol.178 , pp. 5058-5068
    • Waiboci, L.W.1    Ahmed, C.M.2    Mujtaba, M.G.3    Flowers, L.O.4    Martin, J.P.5    Haider, M.I.6    Johnson, H.M.7
  • 54
    • 0037507282 scopus 로고    scopus 로고
    • Characterization of phosphopeptide motifs specific for the Src homology 2 domains of signal transducer and activator of transcription 1 (STAT1) and STAT3
    • Wiederkehr-Adam M., Ernst P., Muller K., Bieck E., Gombert F.O., Ottl J., Graff P., Grossmuller F., and Heim M.H. Characterization of phosphopeptide motifs specific for the Src homology 2 domains of signal transducer and activator of transcription 1 (STAT1) and STAT3. J. Biol. Chem. 278 (2003) 16117-16128
    • (2003) J. Biol. Chem. , vol.278 , pp. 16117-16128
    • Wiederkehr-Adam, M.1    Ernst, P.2    Muller, K.3    Bieck, E.4    Gombert, F.O.5    Ottl, J.6    Graff, P.7    Grossmuller, F.8    Heim, M.H.9
  • 55
    • 0037163125 scopus 로고    scopus 로고
    • Identification of both positive and negative domains within the epidermal growth factor receptor COOH-terminal region for signal transducer and activator of transcription (STAT) activation
    • Xia L., Wang L., Chung A.S., Ivanov S.S., Ling M.Y., Dragoi A.M., Platt A., Gilmer T.M., Fu X.Y., and Chin Y.E. Identification of both positive and negative domains within the epidermal growth factor receptor COOH-terminal region for signal transducer and activator of transcription (STAT) activation. J. Biol. Chem. 277 (2002) 30716-30723
    • (2002) J. Biol. Chem. , vol.277 , pp. 30716-30723
    • Xia, L.1    Wang, L.2    Chung, A.S.3    Ivanov, S.S.4    Ling, M.Y.5    Dragoi, A.M.6    Platt, A.7    Gilmer, T.M.8    Fu, X.Y.9    Chin, Y.E.10
  • 56
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu W., Marcu M., Yuan X., Mimnaugh E., Patterson C., and Neckers L. Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc. Natl. Acad. Sci. USA 99 (2002) 12847-12852
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12847-12852
    • Xu, W.1    Marcu, M.2    Yuan, X.3    Mimnaugh, E.4    Patterson, C.5    Neckers, L.6
  • 58
    • 24944539658 scopus 로고    scopus 로고
    • LNX1 is a perisynaptic Schwann cell specific E3 ubiquitin ligase that interacts with ErbB2
    • Young P., Nie J., Wang X., McGlade C.J., Rich M.M., and Feng G. LNX1 is a perisynaptic Schwann cell specific E3 ubiquitin ligase that interacts with ErbB2. Mol. Cell. Neurosci. 30 (2005) 238-248
    • (2005) Mol. Cell. Neurosci. , vol.30 , pp. 238-248
    • Young, P.1    Nie, J.2    Wang, X.3    McGlade, C.J.4    Rich, M.M.5    Feng, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.