메뉴 건너뛰기




Volumn 23, Issue 5, 2006, Pages 697-707

Structure of an Hsp90-Cdc37-Cdk4 Complex

Author keywords

PROTEINS

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CELL CYCLE PROTEIN 37; CYCLIN DEPENDENT KINASE 4; HEAT SHOCK PROTEIN 90;

EID: 33747878717     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.07.016     Document Type: Article
Times cited : (264)

References (61)
  • 2
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • Basso A.D., Solit D.B., Chiosis G., Giri B., Tsichlis P., and Rosen N. Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J. Biol. Chem. 277 (2002) 39858-39866
    • (2002) J. Biol. Chem. , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 3
    • 0034112079 scopus 로고    scopus 로고
    • Hsp90 is essential for the synthesis and subsequent membrane association, but not the maintenance, of the Src-kinase p56(lck)
    • Bijlmakers M.J., and Marsh M. Hsp90 is essential for the synthesis and subsequent membrane association, but not the maintenance, of the Src-kinase p56(lck). Mol. Biol. Cell 11 (2000) 1585-1595
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1585-1595
    • Bijlmakers, M.J.1    Marsh, M.2
  • 4
    • 0037444766 scopus 로고    scopus 로고
    • Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability
    • Boudeau J., Deak M., Lawlor M.A., Morrice N.A., and Alessi D.R. Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability. Biochem. J. 370 (2003) 849-857
    • (2003) Biochem. J. , vol.370 , pp. 849-857
    • Boudeau, J.1    Deak, M.2    Lawlor, M.A.3    Morrice, N.A.4    Alessi, D.R.5
  • 5
    • 0022574582 scopus 로고
    • Interaction of the Rous sarcoma virus protein pp60v-src with the cellular proteins pp50 and pp90
    • Brugge J.S. Interaction of the Rous sarcoma virus protein pp60v-src with the cellular proteins pp50 and pp90. Curr. Top. Microbiol. Immunol. 123 (1986) 1-22
    • (1986) Curr. Top. Microbiol. Immunol. , vol.123 , pp. 1-22
    • Brugge, J.S.1
  • 7
    • 0036187476 scopus 로고    scopus 로고
    • TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90
    • Chen G., Cao P., and Goeddel D.V. TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol. Cell 9 (2002) 401-410
    • (2002) Mol. Cell , vol.9 , pp. 401-410
    • Chen, G.1    Cao, P.2    Goeddel, D.V.3
  • 8
    • 0029838168 scopus 로고    scopus 로고
    • Physical interaction of mammalian CDC37 with CDK4
    • Dai K., Kobayashi R., and Beach D. Physical interaction of mammalian CDC37 with CDK4. J. Biol. Chem. 271 (1996) 22030-22034
    • (1996) J. Biol. Chem. , vol.271 , pp. 22030-22034
    • Dai, K.1    Kobayashi, R.2    Beach, D.3
  • 9
    • 0037013152 scopus 로고    scopus 로고
    • Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release
    • Fontana J., Fulton D., Chen Y., Fairchild T.A., McCabe T.J., Fujita N., Tsuruo T., and Sessa W.C. Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release. Circ. Res. 90 (2002) 866-873
    • (2002) Circ. Res. , vol.90 , pp. 866-873
    • Fontana, J.1    Fulton, D.2    Chen, Y.3    Fairchild, T.A.4    McCabe, T.J.5    Fujita, N.6    Tsuruo, T.7    Sessa, W.C.8
  • 10
    • 0037155901 scopus 로고    scopus 로고
    • Involvement of Hsp90 in signaling and stability of 3-phosphoinositide-dependent kinase-1
    • Fujita N., Sato S., Ishida A., and Tsuruo T. Involvement of Hsp90 in signaling and stability of 3-phosphoinositide-dependent kinase-1. J. Biol. Chem. 277 (2002) 10346-10353
    • (2002) J. Biol. Chem. , vol.277 , pp. 10346-10353
    • Fujita, N.1    Sato, S.2    Ishida, A.3    Tsuruo, T.4
  • 12
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • Heck A.J., and Van Den Heuvel R.H. Investigation of intact protein complexes by mass spectrometry. Mass Spectrom. Rev. 23 (2004) 368-389
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 368-389
    • Heck, A.J.1    Van Den Heuvel, R.H.2
  • 13
    • 17044403753 scopus 로고    scopus 로고
    • Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding
    • Huai Q., Wang H., Liu Y., Kim H.Y., Toft D., and Ke H. Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding. Structure 13 (2005) 579-590
    • (2005) Structure , vol.13 , pp. 579-590
    • Huai, Q.1    Wang, H.2    Liu, Y.3    Kim, H.Y.4    Toft, D.5    Ke, H.6
  • 14
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: structural basis for regulation
    • Johnson L.N., Noble M.E.M., and Owen D.J. Active and inactive protein kinases: structural basis for regulation. Cell 85 (1996) 149-158
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 15
    • 0028270189 scopus 로고
    • Regulation of cyclin D-dependent kinase 4 (cdk4) by cdk4-activating kinase
    • Kato J.Y., Matsuoka M., Strom D.K., and Sherr C.J. Regulation of cyclin D-dependent kinase 4 (cdk4) by cdk4-activating kinase. Mol. Cell. Biol. 14 (1994) 2713-2721
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2713-2721
    • Kato, J.Y.1    Matsuoka, M.2    Strom, D.K.3    Sherr, C.J.4
  • 17
    • 0037107454 scopus 로고    scopus 로고
    • Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes
    • Lange B.M., Rebollo E., Herold A., and Gonzalez C. Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes. EMBO J. 21 (2002) 5364-5374
    • (2002) EMBO J. , vol.21 , pp. 5364-5374
    • Lange, B.M.1    Rebollo, E.2    Herold, A.3    Gonzalez, C.4
  • 18
    • 0037164751 scopus 로고    scopus 로고
    • The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability
    • Lee P., Rao J., Fliss A., Yang E., Garrett S., and Caplan A.J. The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability. J. Cell Biol. 159 (2002) 1051-1059
    • (2002) J. Cell Biol. , vol.159 , pp. 1051-1059
    • Lee, P.1    Rao, J.2    Fliss, A.3    Yang, E.4    Garrett, S.5    Caplan, A.J.6
  • 19
    • 0034615701 scopus 로고    scopus 로고
    • Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation
    • Lewis J., Devin A., Miller A., Lin Y., Rodriguez Y., Neckers L., and Liu Z.G. Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J. Biol. Chem. 275 (2000) 10519-10526
    • (2000) J. Biol. Chem. , vol.275 , pp. 10519-10526
    • Lewis, J.1    Devin, A.2    Miller, A.3    Lin, Y.4    Rodriguez, Y.5    Neckers, L.6    Liu, Z.G.7
  • 20
    • 0032485070 scopus 로고    scopus 로고
    • Active cdk6 complexes are predominantly nuclear and represent only a minority of the cdk6 in T cells
    • Mahony D., Parry D.A., and Lees E. Active cdk6 complexes are predominantly nuclear and represent only a minority of the cdk6 in T cells. Oncogene 16 (1998) 603-611
    • (1998) Oncogene , vol.16 , pp. 603-611
    • Mahony, D.1    Parry, D.A.2    Lees, E.3
  • 21
    • 0037352446 scopus 로고    scopus 로고
    • Structural and functional analysis of the middle segment of Hsp90: implications for ATP hydrolysis and client-protein and co-chaperone interactions
    • Meyer P., Prodromou C., Hu B., Vaughan C., Roe S.M., Panaretou B., Piper P.W., and Pearl L.H. Structural and functional analysis of the middle segment of Hsp90: implications for ATP hydrolysis and client-protein and co-chaperone interactions. Mol. Cell 11 (2003) 647-658
    • (2003) Mol. Cell , vol.11 , pp. 647-658
    • Meyer, P.1    Prodromou, C.2    Hu, B.3    Vaughan, C.4    Roe, S.M.5    Panaretou, B.6    Piper, P.W.7    Pearl, L.H.8
  • 23
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell J.A., and Grigorieff N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142 (2003) 334-347
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 24
    • 1942486312 scopus 로고    scopus 로고
    • CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37
    • Miyata Y., and Nishida E. CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37. Mol. Cell. Biol. 24 (2004) 4065-4074
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4065-4074
    • Miyata, Y.1    Nishida, E.2
  • 25
    • 0034614455 scopus 로고    scopus 로고
    • Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription
    • O'Keeffe B., Fong Y., Chen D., Zhou S., and Zhou Q. Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription. J. Biol. Chem. 275 (2000) 279-287
    • (2000) J. Biol. Chem. , vol.275 , pp. 279-287
    • O'Keeffe, B.1    Fong, Y.2    Chen, D.3    Zhou, S.4    Zhou, Q.5
  • 26
    • 12344291243 scopus 로고    scopus 로고
    • Hsp90 and Cdc37-a chaperone cancer conspiracy
    • Pearl L.H. Hsp90 and Cdc37-a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 15 (2005) 55-61
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 55-61
    • Pearl, L.H.1
  • 27
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt W.B., and Toft D.O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr. Rev. 18 (1997) 306-360
    • (1997) Endocr. Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 28
    • 4544254444 scopus 로고    scopus 로고
    • Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37
    • Prince T., and Matts R.L. Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37. J. Biol. Chem. 279 (2004) 39975-39981
    • (2004) J. Biol. Chem. , vol.279 , pp. 39975-39981
    • Prince, T.1    Matts, R.L.2
  • 29
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., and Pearl L.H. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90 (1997) 65-75
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 31
    • 0032959590 scopus 로고    scopus 로고
    • The structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin
    • Roe S.M., Prodromou C., O'Brien R., Ladbury J.E., Piper P.W., and Pearl L.H. The structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. J. Med. Chem. 42 (1999) 260-266
    • (1999) J. Med. Chem. , vol.42 , pp. 260-266
    • Roe, S.M.1    Prodromou, C.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 33
    • 17844394935 scopus 로고    scopus 로고
    • Domain-mediated dimerization of the Hsp90 cochaperones Harc and Cdc37
    • Roiniotis J., Masendycz P., Ho S., and Scholz G.M. Domain-mediated dimerization of the Hsp90 cochaperones Harc and Cdc37. Biochemistry 44 (2005) 6662-6669
    • (2005) Biochemistry , vol.44 , pp. 6662-6669
    • Roiniotis, J.1    Masendycz, P.2    Ho, S.3    Scholz, G.M.4
  • 34
    • 0034081637 scopus 로고    scopus 로고
    • Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins
    • Saibil H. Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins. Curr. Opin. Struct. Biol. 10 (2000) 251-258
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 251-258
    • Saibil, H.1
  • 35
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of akt kinase activity by binding to hsp90
    • Sato S., Fujita N., and Tsuruo T. Modulation of akt kinase activity by binding to hsp90. Proc. Natl. Acad. Sci. USA 97 (2000) 10832-10837
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 36
    • 0028786332 scopus 로고
    • Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association
    • Schulte T.W., Blagosklonny M.V., Ingui C., and Neckers L. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J. Biol. Chem. 270 (1995) 24585-24588
    • (1995) J. Biol. Chem. , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3    Neckers, L.4
  • 38
    • 0035808455 scopus 로고    scopus 로고
    • Hsp90 regulates p50(cdc27) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase
    • Shao J., Grammatikakis N., Scroggins B.T., Uma S., Huang W.J., Chen J.J., Hartson S.D., and Matts R.L. Hsp90 regulates p50(cdc27) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase. J. Biol. Chem. 276 (2001) 206-214
    • (2001) J. Biol. Chem. , vol.276 , pp. 206-214
    • Shao, J.1    Grammatikakis, N.2    Scroggins, B.T.3    Uma, S.4    Huang, W.J.5    Chen, J.J.6    Hartson, S.D.7    Matts, R.L.8
  • 39
    • 0242349780 scopus 로고    scopus 로고
    • Functional dissection of cdc37: characterization of domain structure and amino acid residues critical for protein kinase binding
    • Shao J., Irwin A., Hartson S.D., and Matts R.L. Functional dissection of cdc37: characterization of domain structure and amino acid residues critical for protein kinase binding. Biochemistry 42 (2003) 12577-12588
    • (2003) Biochemistry , vol.42 , pp. 12577-12588
    • Shao, J.1    Irwin, A.2    Hartson, S.D.3    Matts, R.L.4
  • 40
    • 0141755381 scopus 로고    scopus 로고
    • Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37
    • Shao J., Prince T., Hartson S.D., and Matts R.L. Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. J. Biol. Chem. 278 (2003) 38117-38120
    • (2003) J. Biol. Chem. , vol.278 , pp. 38117-38120
    • Shao, J.1    Prince, T.2    Hartson, S.D.3    Matts, R.L.4
  • 42
  • 43
    • 0032493624 scopus 로고    scopus 로고
    • P50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site
    • Silverstein A.M., Grammatikakis N., Cochran B.H., Chinkers M., and Pratt W.B. P50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site. J. Biol. Chem. 273 (1998) 20090-20095
    • (1998) J. Biol. Chem. , vol.273 , pp. 20090-20095
    • Silverstein, A.M.1    Grammatikakis, N.2    Cochran, B.H.3    Chinkers, M.4    Pratt, W.B.5
  • 45
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • Sobott F., Hernandez H., McCammon M.G., Tito M.A., and Robinson C.V. A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal. Chem. 74 (2002) 1402-1407
    • (2002) Anal. Chem. , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 46
    • 0027433644 scopus 로고
    • Raf exists in a native heterocomplex with Hsp90 and p50 that can be reconstituted in a cell-free system
    • Stancato L.F., Chow Y.-H., Hutchinson K.A., Perdew G.H., Jove R., and Pratt W.B. Raf exists in a native heterocomplex with Hsp90 and p50 that can be reconstituted in a cell-free system. J. Biol. Chem. 268 (1993) 21711-21716
    • (1993) J. Biol. Chem. , vol.268 , pp. 21711-21716
    • Stancato, L.F.1    Chow, Y.-H.2    Hutchinson, K.A.3    Perdew, G.H.4    Jove, R.5    Pratt, W.B.6
  • 47
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent
    • Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., and Pavletich N.P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89 (1997) 239-250
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 48
    • 0029665779 scopus 로고    scopus 로고
    • Mammalian p50(Cdc37) is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Stepanova L., Leng X.H., Parker S.B., and Harper J.W. Mammalian p50(Cdc37) is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev. 10 (1996) 1491-1502
    • (1996) Genes Dev. , vol.10 , pp. 1491-1502
    • Stepanova, L.1    Leng, X.H.2    Parker, S.B.3    Harper, J.W.4
  • 49
    • 0034087051 scopus 로고    scopus 로고
    • The oncoprotein kinase chaperone CDC37 functions as an oncogene in mice and collaborates with both c-myc and cyclin D1 in transformation of multiple tissues
    • Stepanova L., Finegold M., DeMayo F., Schmidt E.V., and Harper J.W. The oncoprotein kinase chaperone CDC37 functions as an oncogene in mice and collaborates with both c-myc and cyclin D1 in transformation of multiple tissues. Mol. Cell. Biol. 20 (2000) 4462-4473
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4462-4473
    • Stepanova, L.1    Finegold, M.2    DeMayo, F.3    Schmidt, E.V.4    Harper, J.W.5
  • 50
    • 0034720255 scopus 로고    scopus 로고
    • Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia
    • Stepanova L., Yang G., DeMayo F., Wheeler T.M., Finegold M., Thompson T.C., and Harper J.W. Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia. Oncogene 19 (2000) 2186-2193
    • (2000) Oncogene , vol.19 , pp. 2186-2193
    • Stepanova, L.1    Yang, G.2    DeMayo, F.3    Wheeler, T.M.4    Finegold, M.5    Thompson, T.C.6    Harper, J.W.7
  • 51
    • 25444501262 scopus 로고    scopus 로고
    • A client-binding site of Cdc37
    • Terasawa K., and Minami Y. A client-binding site of Cdc37. FEBS J. 272 (2005) 4684-4690
    • (2005) FEBS J. , vol.272 , pp. 4684-4690
    • Terasawa, K.1    Minami, Y.2
  • 54
    • 1542298267 scopus 로고    scopus 로고
    • Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone
    • Workman P. Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone. Cancer Lett. 206 (2004) 149-157
    • (2004) Cancer Lett. , vol.206 , pp. 149-157
    • Workman, P.1
  • 55
    • 0032780181 scopus 로고    scopus 로고
    • Situs: a package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers W., Milligan R.A., and McCammon J.A. Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125 (1999) 185-195
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 56
    • 0027291238 scopus 로고
    • Heat-shock protein Hsp90 governs the activity of Pp60(V-Src) kinase
    • Xu Y., and Lindquist S. Heat-shock protein Hsp90 governs the activity of Pp60(V-Src) kinase. Proc. Natl. Acad. Sci. USA 90 (1993) 7074-7078
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7074-7078
    • Xu, Y.1    Lindquist, S.2
  • 57
    • 0033524442 scopus 로고    scopus 로고
    • Maturation of the tyrosine kinase c-Src as a kinase and as a substrate depends on the molecular chaperone Hsp90
    • Xu Y., Singer M.A., and Lindquist S. Maturation of the tyrosine kinase c-Src as a kinase and as a substrate depends on the molecular chaperone Hsp90. Proc. Natl. Acad. Sci. USA 96 (1999) 109-114
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 109-114
    • Xu, Y.1    Singer, M.A.2    Lindquist, S.3
  • 58
    • 0035793546 scopus 로고    scopus 로고
    • Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90
    • Xu W., Mimnaugh E., Rosser M.F., Nicchitta C., Marcu M., Yarden Y., and Neckers L. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J. Biol. Chem. 276 (2001) 3702-3708
    • (2001) J. Biol. Chem. , vol.276 , pp. 3702-3708
    • Xu, W.1    Mimnaugh, E.2    Rosser, M.F.3    Nicchitta, C.4    Marcu, M.5    Yarden, Y.6    Neckers, L.7
  • 59
    • 15544372341 scopus 로고    scopus 로고
    • Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex
    • Xu W., Yuan X., Xiang Z., Mimnaugh E., Marcu M., and Neckers L. Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex. Nat. Struct. Mol. Biol. 12 (2005) 120-126
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 120-126
    • Xu, W.1    Yuan, X.2    Xiang, Z.3    Mimnaugh, E.4    Marcu, M.5    Neckers, L.6
  • 61
    • 1842477464 scopus 로고    scopus 로고
    • Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4
    • Zhao Q., Boschelli F., Caplan A.J., and Arndt K.T. Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4. J. Biol. Chem. 279 (2004) 12560-12564
    • (2004) J. Biol. Chem. , vol.279 , pp. 12560-12564
    • Zhao, Q.1    Boschelli, F.2    Caplan, A.J.3    Arndt, K.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.