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Volumn 27, Issue 1, 2006, Pages 194-210

NMR studies for identifying phosphopeptide ligands of the HIV-1 protein Vpu binding to the F-box protein β-TrCP

Author keywords

Binding fragment; Bound structure; Human immunodeficiency virus type 1; Phosphorylated peptide P Vpu; Restrained molecular dynamics; STD NMR; TRNOESY; Vpu

Indexed keywords

F BOX PROTEIN; HYBRID PROTEIN; PHOSPHOPEPTIDE; PROTEASOME; PROTEIN BETA TRCP; UNCLASSIFIED DRUG; VIRUS PROTEIN; VPU PROTEIN;

EID: 30344449470     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2005.07.018     Document Type: Article
Times cited : (17)

References (54)
  • 1
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • A. Bax, and D.G. Davis MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy J Magn Reson 65 1985 355 360
    • (1985) J Magn Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 2
    • 0345791500 scopus 로고    scopus 로고
    • HIV-1 Vpu sequesters beta-transducin repeat-containing protein (betaTrCP) in the cytoplasm and provokes the accumulation of beta-catenin and other SCFbetaTrCP substrates
    • C. Besnard-Guerin, N. Belaidouni, I. Lassot, E. Segeral, A. Jobart, and C. Marchal HIV-1 Vpu sequesters beta-transducin repeat-containing protein (betaTrCP) in the cytoplasm and provokes the accumulation of beta-catenin and other SCFbetaTrCP substrates J Biol Chem 279 2004 788 795
    • (2004) J Biol Chem , vol.279 , pp. 788-795
    • Besnard-Guerin, C.1    Belaidouni, N.2    Lassot, I.3    Segeral, E.4    Jobart, A.5    Marchal, C.6
  • 4
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system (CNS): A new software system for macromolecular structure determination
    • A.T. Brünger, P.D. Adams, G.M. Clore, P. Gros, R.W. Grosse-Kunstleve, and J.S. Jiang Crystallography and NMR system (CNS): a new software system for macromolecular structure determination Acta Cryst D54 1998 905 921
    • (1998) Acta Cryst , vol.54 , pp. 905-921
    • Brünger, A.T.1    Adams, P.D.2    Clore, G.M.3    Gros, P.4    Grosse-Kunstleve, R.W.5    Jiang, J.S.6
  • 5
    • 0000393431 scopus 로고
    • Theory applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bounds to proteins
    • G.M. Clore, and A.M. Gronenborn Theory applications of the transferred nuclear Overhauser effect to the study of the conformations of small ligands bounds to proteins J Magn Reson 48 1982 402 417
    • (1982) J Magn Reson , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 6
    • 0001342923 scopus 로고
    • Theory of the time dependent transferred nuclear Overhauser effect: Applications to structural analysis of ligand-protein complexes in solution
    • G.M. Clore, and A.M. Gronenborn Theory of the time dependent transferred nuclear Overhauser effect: applications to structural analysis of ligand-protein complexes in solution J Magn Reson 53 1983 423 442
    • (1983) J Magn Reson , vol.53 , pp. 423-442
    • Clore, G.M.1    Gronenborn, A.M.2
  • 8
    • 0346365107 scopus 로고    scopus 로고
    • NMR studies of the phosphorylation motif of the HIV-1 protein Vpu bound to the F-box protein β-TrCP
    • G. Coadou, J. Gharbi-Benarous, S. Megy, G. Bertho, N. Evrard-Todeschi, and E. Segeral NMR studies of the phosphorylation motif of the HIV-1 protein Vpu bound to the F-box protein β-TrCP Biochemistry 42 2003 14741 14751
    • (2003) Biochemistry , vol.42 , pp. 14741-14751
    • Coadou, G.1    Gharbi-Benarous, J.2    Megy, S.3    Bertho, G.4    Evrard-Todeschi, N.5    Segeral, E.6
  • 9
    • 0026162172 scopus 로고
    • 1H NMR study of antigene-antibody interactions: Binding of synthetic decapeptides to an anti-acetylcholine receptor monoclonal antibody
    • 1H NMR study of antigene-antibody interactions: binding of synthetic decapeptides to an anti-acetylcholine receptor monoclonal antibody Biopolymers 31 1991 769 776
    • (1991) Biopolymers , vol.31 , pp. 769-776
    • Cung, M.T.1    Demange, P.2    Marraud, M.3    Tsikaris, V.4    Sakarellos, C.5    Papadouli, I.6
  • 10
    • 0029977571 scopus 로고    scopus 로고
    • Solution structure of the cytoplasmic domain of human immunodeficiency virus type 1 encoded virus protein U (Vpu)
    • T. Federau, U. Schubert, J. Flossdorf, P. Henklein, D. Schomburg, and V. Wray Solution structure of the cytoplasmic domain of human immunodeficiency virus type 1 encoded virus protein U (Vpu) Int J Pept Protein Res 47 1996 297 310
    • (1996) Int J Pept Protein Res , vol.47 , pp. 297-310
    • Federau, T.1    Schubert, U.2    Flossdorf, J.3    Henklein, P.4    Schomburg, D.5    Wray, V.6
  • 11
    • 0031057925 scopus 로고    scopus 로고
    • Rapid degradation of CD4 in cells expressing human immunodeficiency virus type 1 Env and Vpu is blocked by proteasome inhibitors
    • K. Fujita, S. Omura, and J. Silver Rapid degradation of CD4 in cells expressing human immunodeficiency virus type 1 Env and Vpu is blocked by proteasome inhibitors J Gen Virol 78 1997 619 625
    • (1997) J Gen Virol , vol.78 , pp. 619-625
    • Fujita, K.1    Omura, S.2    Silver, J.3
  • 12
    • 0033602227 scopus 로고    scopus 로고
    • The F-box protein beta-TrCP associates with phosphorylated beta-catenin and regulates its activity in the cell
    • M. Hart, J.-P. Concordet, I. Lassot, I. Albert, R. Del los Santos, and H. Durand The F-box protein beta-TrCP associates with phosphorylated beta-catenin and regulates its activity in the cell Curr Biol 9 1999 207 210
    • (1999) Curr Biol , vol.9 , pp. 207-210
    • Hart, M.1    Concordet, J.-P.2    Lassot, I.3    Albert, I.4    Del Los Santos, R.5    Durand, H.6
  • 13
    • 0034613058 scopus 로고    scopus 로고
    • Membrane interactions and alignment of structures within the HIV-1 Vpu cytoplasmic domain: Effect of phosphorylation of serines 52 and 56
    • P. Henklein, R. Kinder, U. Schubert, and B. Bechinger Membrane interactions and alignment of structures within the HIV-1 Vpu cytoplasmic domain: effect of phosphorylation of serines 52 and 56 FEBS Lett 482 2000 220 224
    • (2000) FEBS Lett , vol.482 , pp. 220-224
    • Henklein, P.1    Kinder, R.2    Schubert, U.3    Bechinger, B.4
  • 14
    • 0033538283 scopus 로고    scopus 로고
    • Detecting binding affinity to immobilized receptor proteins in compound libraries by HR-MAS STD NMR
    • J. Klein, R. Meinecke, M. Mayer, and B. Meyer Detecting binding affinity to immobilized receptor proteins in compound libraries by HR-MAS STD NMR J Am Chem Soc 121 1999 5336 5337
    • (1999) J Am Chem Soc , vol.121 , pp. 5336-5337
    • Klein, J.1    Meinecke, R.2    Mayer, M.3    Meyer, B.4
  • 15
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wüthrich MOLMOL: a program for display and analysis of macromolecular structures J Mol Graph 14 51-55 1996 29 32
    • (1996) J Mol Graph , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 16
    • 0033582821 scopus 로고    scopus 로고
    • Inducible degradation of IkappaBalpha by the proteasome requires interaction with the F-box protein h-betaTrCP
    • M. Kroll, F. Margottin, A. Kohl, P. Renard, H. Durand, and J.-P. Concordet Inducible degradation of IkappaBalpha by the proteasome requires interaction with the F-box protein h-betaTrCP J Biol Chem 274 1999 7941 7945
    • (1999) J Biol Chem , vol.274 , pp. 7941-7945
    • Kroll, M.1    Margottin, F.2    Kohl, A.3    Renard, P.4    Durand, H.5    Concordet, J.-P.6
  • 17
    • 12644267957 scopus 로고
    • Buildup rates of the NOE measured by 2D proton magnetic resonance spectroscopy: Implication for studies of protein conformation
    • A. Kumar, G. Wagner, R.R. Ernst, and K. Wüthrich Buildup rates of the NOE measured by 2D proton magnetic resonance spectroscopy: implication for studies of protein conformation J Am Chem Soc 103 1981 3654 3658
    • (1981) J Am Chem Soc , vol.103 , pp. 3654-3658
    • Kumar, A.1    Wagner, G.2    Ernst, R.R.3    Wüthrich, K.4
  • 18
    • 0342467925 scopus 로고    scopus 로고
    • ATF4 degradation relies on a phosphorylation-dependent interaction with the SCFβ-TrCP ubiquitin ligase
    • I. Lassot, E. Ségéral, C. Berlioz-Torrent, H. Durand, L. Groussin, and T. Hai ATF4 degradation relies on a phosphorylation-dependent interaction with the SCFβ-TrCP ubiquitin ligase Mol Cell Biol 21 2001 2192 2202
    • (2001) Mol Cell Biol , vol.21 , pp. 2192-2202
    • Lassot, I.1    Ségéral, E.2    Berlioz-Torrent, C.3    Durand, H.4    Groussin, L.5    Hai, T.6
  • 19
    • 0042346262 scopus 로고    scopus 로고
    • Vpu exerts a positive effect on HIV-1 infectivity by down-modulating CD4 receptor molecules at the surface of HIV-1-producing cells
    • K. Levesque, Y.S. Zhao, and E.A. Cohen Vpu exerts a positive effect on HIV-1 infectivity by down-modulating CD4 receptor molecules at the surface of HIV-1-producing cells J Biol Chem 278 2003 28346 28353
    • (2003) J Biol Chem , vol.278 , pp. 28346-28353
    • Levesque, K.1    Zhao, Y.S.2    Cohen, E.A.3
  • 20
    • 0037316363 scopus 로고    scopus 로고
    • ARIA: Automated assignment and NMR structure calculation
    • J.P. Linge, M. Habeck, W. Rieping, and M. Nilges ARIA: automated assignment and NMR structure calculation Bioinformatics 19 2003 315 316
    • (2003) Bioinformatics , vol.19 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 22
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein, h-betaTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • F. Margottin, S. Bour, H. Durand, L. Selig, S. Benichou, and V. Richard A novel human WD protein, h-betaTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif Mol Cell 1 1998 565 574
    • (1998) Mol Cell , vol.1 , pp. 565-574
    • Margottin, F.1    Bour, S.2    Durand, H.3    Selig, L.4    Benichou, S.5    Richard, V.6
  • 23
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • M. Mayer, and B. Meyer Characterization of ligand binding by saturation transfer difference NMR spectroscopy Angew Chem Int Ed Engl 38 1999 1784 1788
    • (1999) Angew Chem Int Ed Engl , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 24
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • M. Mayer, and B. Meyer Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor J Am Chem Soc 123 2001 6108 6117
    • (2001) J Am Chem Soc , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 25
    • 0037463033 scopus 로고    scopus 로고
    • NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors
    • B. Meyer, and T. Peters NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors Angew Chem Int Ed Engl 42 2003 864 890
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 26
    • 0035969559 scopus 로고    scopus 로고
    • Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
    • P. Nash, X. Tang, S. Orlicky, Q. Chen, F.B. Gertler, and M.D. Mendenhall Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication Nature 414 2001 514 521
    • (2001) Nature , vol.414 , pp. 514-521
    • Nash, P.1    Tang, X.2    Orlicky, S.3    Chen, Q.4    Gertler, F.B.5    Mendenhall, M.D.6
  • 27
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • E.J. Neer, C.J. Schmidt, R. Nambudripad, and T.F. Smith The ancient regulatory-protein family of WD-repeat proteins Nature 371 1994 297 300
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 28
    • 0028728698 scopus 로고
    • Recent developments in transferred NOE methods
    • F. Ni Recent developments in transferred NOE methods Progr Nucl Magn Reson Spectrosc 26 1994 517 606
    • (1994) Progr Nucl Magn Reson Spectrosc , vol.26 , pp. 517-606
    • Ni, F.1
  • 30
    • 0027361390 scopus 로고
    • Experimental NMR techniques for studies of protein-ligand interactions
    • G. Otting Experimental NMR techniques for studies of protein-ligand interactions Curr Open Struct Biol 3 1993 760 768
    • (1993) Curr Open Struct Biol , vol.3 , pp. 760-768
    • Otting, G.1
  • 31
    • 0030921020 scopus 로고    scopus 로고
    • Phosphorylation of both phosphoacceptor sites in the HIV-1 Vpu cytoplasmique domain is essential for Vpu-mediated ER degradation of CD4
    • M. Paul, and M.A. Jabbar Phosphorylation of both phosphoacceptor sites in the HIV-1 Vpu cytoplasmique domain is essential for Vpu-mediated ER degradation of CD4 Virology 232 1997 207 216
    • (1997) Virology , vol.232 , pp. 207-216
    • Paul, M.1    Jabbar, M.A.2
  • 32
    • 0026951903 scopus 로고
    • Gradient-tailored exitation for single-quantum NMR spectroscopy of aqueous solutions
    • M. Piotto, V. Saudek, and V. Sklenar Gradient-tailored exitation for single-quantum NMR spectroscopy of aqueous solutions J Biomol NMR 2 1992 661 665
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 33
    • 0035859948 scopus 로고    scopus 로고
    • The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles
    • D.J. Schibli, R.C. Montelaro, and H.J. Vogel The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles Biochemistry 40 2001 9570 9578
    • (2001) Biochemistry , vol.40 , pp. 9570-9578
    • Schibli, D.J.1    Montelaro, R.C.2    Vogel, H.J.3
  • 34
    • 0028349047 scopus 로고
    • Differential activities of the human immunodeficiency virus type I-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartiments
    • U. Schubert, and K. Strebel Differential activities of the human immunodeficiency virus type I-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartiments J Virol 68 1994 2260 2271
    • (1994) J Virol , vol.68 , pp. 2260-2271
    • Schubert, U.1    Strebel, K.2
  • 35
    • 0031935031 scopus 로고    scopus 로고
    • CD4 glycoprotein degradation induced by human immunodeficiency virus type-1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway
    • U. Schubert, L.C. Anton, J.H. Cox, S. Bour, J.R. Bennink, and M. Orlowski CD4 glycoprotein degradation induced by human immunodeficiency virus type-1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway J Virol 72 1998 2280 2288
    • (1998) J Virol , vol.72 , pp. 2280-2288
    • Schubert, U.1    Anton, L.C.2    Cox, J.H.3    Bour, S.4    Bennink, J.R.5    Orlowski, M.6
  • 38
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • D.J. States, R.A. Haberkorn, and D.J. Ruben A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants J Magn Res 48 1982 286 292
    • (1982) J Magn Res , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 39
    • 0023677668 scopus 로고
    • A novel gene of HIV-1, Vpu, and its 16 kDa product
    • K. Strebel, T. Klimkait, and M.A. Martin A novel gene of HIV-1, Vpu, and its 16 kDa product Science 241 1988 1221 1223
    • (1988) Science , vol.241 , pp. 1221-1223
    • Strebel, K.1    Klimkait, T.2    Martin, M.A.3
  • 40
    • 0024381228 scopus 로고
    • Molecular biochemical analyses of human immunodeficiency virus type 1 vpu protein
    • K. Strebel, T. Klimkait, F. Maldarelli, and M.A. Martin Molecular biochemical analyses of human immunodeficiency virus type 1 vpu protein J Virol 63 1989 3784 3791
    • (1989) J Virol , vol.63 , pp. 3784-3791
    • Strebel, K.1    Klimkait, T.2    Maldarelli, F.3    Martin, M.A.4
  • 41
    • 0035921849 scopus 로고    scopus 로고
    • Human F-box protein hCdc4 targets cyclin e for proteolysis and is mutated in a breast cancer cell line
    • H. Strohmaier, C.H. Spruck, P. Kaiser, K.A. Won, O. Sangfelt, and S.I. Reed Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line Nature 413 2001 316 322
    • (2001) Nature , vol.413 , pp. 316-322
    • Strohmaier, H.1    Spruck, C.H.2    Kaiser, P.3    Won, K.A.4    Sangfelt, O.5    Reed, S.I.6
  • 42
    • 0030962174 scopus 로고    scopus 로고
    • Putative alpha-helical structures in the human immunodeficiency virus type 1 Vpu protein and CD4 are involved in binding and degradation of the CD4 molecule
    • E. Tiganos, X.J. Yao, J. Friborg, N. Daniel, and E.A. Cohen Putative alpha-helical structures in the human immunodeficiency virus type 1 Vpu protein and CD4 are involved in binding and degradation of the CD4 molecule J Virol 71 1997 4452 4460
    • (1997) J Virol , vol.71 , pp. 4452-4460
    • Tiganos, E.1    Yao, X.J.2    Friborg, J.3    Daniel, N.4    Cohen, E.A.5
  • 43
    • 0034587285 scopus 로고    scopus 로고
    • Dissociation-equilibrium constant and bound conformation for weak antibiotic binding interaction with different bacterial ribosomes
    • L. Verdier, J. Gharbi-Benarous, G. Bertho, N. Evrard-Todeschi, P. Mauvais, and J.-P. Girault Dissociation-equilibrium constant and bound conformation for weak antibiotic binding interaction with different bacterial ribosomes J Chem Soc Perkin Trans 2 2000 2363 2371
    • (2000) J Chem Soc Perkin Trans , vol.2 , pp. 2363-2371
    • Verdier, L.1    Gharbi-Benarous, J.2    Bertho, G.3    Evrard-Todeschi, N.4    Mauvais, P.5    Girault, J.-P.6
  • 44
    • 0028820287 scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein: A potential regulator of proteolysis and protein transport in the mammalian secretory pathway
    • M.J. Vincent, and M.A. Jabbar The human immunodeficiency virus type 1 Vpu protein: a potential regulator of proteolysis and protein transport in the mammalian secretory pathway Virology 213 1995 639 649
    • (1995) Virology , vol.213 , pp. 639-649
    • Vincent, M.J.1    Jabbar, M.A.2
  • 45
    • 0030943906 scopus 로고    scopus 로고
    • Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution
    • D. Willbold, S. Hoffmann, and P. Rosch Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution Eur J Biochem 245 1997 581 588
    • (1997) Eur J Biochem , vol.245 , pp. 581-588
    • Willbold, D.1    Hoffmann, S.2    Rosch, P.3
  • 46
    • 0026452726 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4
    • R.L. Willey, F. Maldarelli, M.A. Martin, and K. Strebel Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4 J Virol 66 1992 7193 7200
    • (1992) J Virol , vol.66 , pp. 7193-7200
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 47
    • 0033068154 scopus 로고    scopus 로고
    • The SCF β-TrCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro
    • J.T. Winston, P. Strack, P. Beer-Romero, C.Y. Chu, S.J. Elledge, and J.W. Harper The SCF 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 1999 270 283
    • (1999) Genes Dev , vol.13 , pp. 270-283
    • Winston, J.T.1    Strack, P.2    Beer-Romero, P.3    Chu, C.Y.4    Elledge, S.J.5    Harper, J.W.6
  • 49
    • 0033586794 scopus 로고    scopus 로고
    • Solution structure and orientation of the transmembrane anchor domain of the HIV-1 encoded virus protein U by high-resolution and solid-state NMR spectroscopy
    • V. Wray, R. Kinder, T. Federau, P. Henklein, B. Bechinger, and U. Schubert Solution structure and orientation of the transmembrane anchor domain of the HIV-1 encoded virus protein U by high-resolution and solid-state NMR spectroscopy Biochemistry 38 1999 5272 5282
    • (1999) Biochemistry , vol.38 , pp. 5272-5282
    • Wray, V.1    Kinder, R.2    Federau, T.3    Henklein, P.4    Bechinger, B.5    Schubert, U.6
  • 50
    • 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
    • G. Wu, G. Xu, B.A. Schulman, P.D. Jeffrey, J.W. Harper, and N.P. Pavletich Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase Mol Cell 11 2003 1445 1456
    • (2003) Mol Cell , vol.11 , pp. 1445-1456
    • Wu, G.1    Xu, G.2    Schulman, B.A.3    Jeffrey, P.D.4    Harper, J.W.5    Pavletich, N.P.6
  • 52
    • 0035313699 scopus 로고    scopus 로고
    • Phosphoserine/threonine-binding domains
    • M.B. Yaffe, and A.E. Elia Phosphoserine/threonine-binding domains Curr Opin Cell Biol 13 2001 131 138
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 131-138
    • Yaffe, M.B.1    Elia, A.E.2
  • 53
    • 17944401842 scopus 로고    scopus 로고
    • Identification of the receptor component of the IkappaBalpha-ubiquitin ligase
    • A. Yaron, A. Hatzubai, M. Davis, I. Lavon, S. Amit, and A.M. Manning Identification of the receptor component of the IkappaBalpha-ubiquitin ligase Nature 396 1998 590 594
    • (1998) Nature , vol.396 , pp. 590-594
    • Yaron, A.1    Hatzubai, A.2    Davis, M.3    Lavon, I.4    Amit, S.5    Manning, A.M.6
  • 54
    • 0344198598 scopus 로고    scopus 로고
    • Exploring the functional complexity of cellular proteins by protein knockout
    • J. Zhang, N. Zheng, and P. Zhou Exploring the functional complexity of cellular proteins by protein knockout Proc Natl Acad Sci USA 100 2003 14127 14132
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14127-14132
    • Zhang, J.1    Zheng, N.2    Zhou, P.3


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