메뉴 건너뛰기




Volumn 383, Issue 9, 2002, Pages 1335-1342

The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically

Author keywords

Budding yeast; Cpr7; Hop; Mass spectrometry; Synthetic lethality; Tetratricopeptide repeat

Indexed keywords

CELL CYCLE PROTEIN; CELL CYCLE PROTEIN 37; CHAPERONE; FUNGAL PROTEIN; GLUTATHIONE TRANSFERASE; HEAT SHOCK PROTEIN 90; PHOSPHOTRANSFERASE; PROTEIN CPR7; PROTEIN STI1; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARRIER PROTEIN; CDC37 PROTEIN, S CEREVISIAE; CYCLOPHILIN; CYCLOPHILIN D; DROSOPHILA PROTEIN; PEPTIDYLPROLYL ISOMERASE; SACCHAROMYCES CEREVISIAE PROTEIN; STREPTOMYCES TRYPSIN INHIBITOR 1 PROTEIN, STREPTOMYCES;

EID: 0036754939     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2002.152     Document Type: Article
Times cited : (39)

References (52)
  • 1
    • 0034769599 scopus 로고    scopus 로고
    • Hsp104 interacts with Hsp90 cochaperones in respiring yeast
    • Abbas-Terki, T., Donzé, O., Briand, P.-A., and Picard, D. (2001). Hsp104 interacts with Hsp90 cochaperones in respiring yeast. Mol. Cell. Biol. 21, 7569-7575.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 7569-7575
    • Abbas-Terki, T.1    Donzé, O.2    Briand, P.-A.3    Picard, D.4
  • 2
    • 0033959642 scopus 로고    scopus 로고
    • The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest
    • Abbas-Terki, T, Donzé, O., and Picard, D. (2000). The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest. FEBS Lett. 467, 111-116.
    • (2000) FEBS Lett , vol.467 , pp. 111-116
    • Abbas-Terki, T.1    Donzé, O.2    Picard, D.3
  • 3
    • 0031868061 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins
    • Bohen, S. P. (1998). Genetic and biochemical analysis of p23 and ansamycin antibiotics in the function of Hsp90-dependent signaling proteins. Mol. Cell. Biol. 18, 3330-3339.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 3330-3339
    • Bohen, S.P.1
  • 4
    • 0024421221 scopus 로고
    • Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., and Lindquist, S. (1989). Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell. Biol. 9, 3919-3930.
    • (1989) Mol. Cell. Biol , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 5
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp9O-associated proteins
    • Bose, S., Weikl, T., Bügl, H., and Buchner, J. (1996). Chaperone function of Hsp9O-associated proteins. Science 274, 1715-1717.
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Bügl, H.3    Buchner, J.4
  • 6
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 & Co. - A holding for folding
    • Buchner, J. (1999). Hsp90 & Co. - a holding for folding. Trends Biochem. Sci. 24, 136-141.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 136-141
    • Buchner, J.1
  • 7
    • 0033168520 scopus 로고    scopus 로고
    • Hsp9O's secrets unfold: New insights from structural and functional studies
    • Caplan, A. J. (1999). Hsp9O's secrets unfold: new insights from structural and functional studies. Trends Cell Biol. 9, 262-268.
    • (1999) Trends Cell Biol , vol.9 , pp. 262-268
    • Caplan, A.J.1
  • 8
    • 0029885423 scopus 로고    scopus 로고
    • Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins Hsp90 and Hsp70
    • Chen, S., Prapapanich, V., Rimerman, R. A., Honoré, B., and Smith, D. F. (1996). Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins Hsp90 and Hsp70. Mol. Endocrinol. 10, 682-693.
    • (1996) Mol. Endocrinol , vol.10 , pp. 682-693
    • Chen, S.1    Prapapanich, V.2    Rimerman, R.A.3    Honoré, B.4    Smith, D.F.5
  • 9
    • 0034463399 scopus 로고    scopus 로고
    • Molecular chaperone interactions with steroid receptors: An update
    • Cheung, J., and Smith, D. F. (2000). Molecular chaperone interactions with steroid receptors: an update. Mol. Endocrinol. 14, 939-946.
    • (2000) Mol. Endocrinol , vol.14 , pp. 939-946
    • Cheung, J.1    Smith, D.F.2
  • 10
    • 0030869037 scopus 로고    scopus 로고
    • Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery
    • Dittmar, K. D., Demady, D. R., Stancato, L. F., Krishna, P., and Pratt, W. B. (1997). Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. J. Biol. Chem. 272, 21213-21220.
    • (1997) J. Biol. Chem , vol.272 , pp. 21213-21220
    • Dittmar, K.D.1    Demady, D.R.2    Stancato, L.F.3    Krishna, P.4    Pratt, W.B.5
  • 11
    • 0030692139 scopus 로고    scopus 로고
    • All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae
    • Dolinski, K., Muir, S., Cardenas, M., and Heitman, J. (1997). All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 94, 13093-13098.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13093-13098
    • Dolinski, K.1    Muir, S.2    Cardenas, M.3    Heitman, J.4
  • 12
    • 0031756340 scopus 로고    scopus 로고
    • CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90
    • Dolinski, K. J., Cardenas, M. E., and Heitman, J. (1998). CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90. Mol. Cell. Biol. 18, 7344-7352.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 7344-7352
    • Dolinski, K.J.1    Cardenas, M.E.2    Heitman, J.3
  • 13
    • 0033512306 scopus 로고    scopus 로고
    • Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the α subunit of eukaryotic translation initiation factor 2
    • Donzé, O., and Picard, D. (1999). Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the α subunit of eukaryotic translation initiation factor 2. Mol. Cell. Biol. 19, 8422-8432.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 8422-8432
    • Donzé, O.1    Picard, D.2
  • 14
    • 0035898534 scopus 로고    scopus 로고
    • The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR
    • Donzé, O., Abbas-Terki, T., and Picard, D. (2001). The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR. EMBO J. 20, 3771-3780.
    • (2001) EMBO J , vol.20 , pp. 3771-3780
    • Donzé, O.1    Abbas-Terki, T.2    Picard, D.3
  • 15
    • 0029750182 scopus 로고    scopus 로고
    • Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth
    • Duina, A. A., Marsh, J. A., and Gaber, R. F. (1996). Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth. Yeast 12, 943-952.
    • (1996) Yeast , vol.12 , pp. 943-952
    • Duina, A.A.1    Marsh, J.A.2    Gaber, R.F.3
  • 16
    • 0031832233 scopus 로고    scopus 로고
    • SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23
    • Fang, Y., Fliss, A. E., Rao, J., and Caplan, A. J. (1998). SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23. Mol. Cell. Biol. 18, 3727-3734.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 3727-3734
    • Fang, Y.1    Fliss, A.E.2    Rao, J.3    Caplan, A.J.4
  • 17
    • 0033974108 scopus 로고    scopus 로고
    • Cdc37 Promotes the Stability of Protein Kinases Cdc28 and Cak1
    • Farrell, A., and Morgan, D. O. (2000). Cdc37 Promotes the Stability of Protein Kinases Cdc28 and Cak1. Mol. Cell. Biol. 20, 749-754.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 749-754
    • Farrell, A.1    Morgan, D.O.2
  • 18
    • 0030659844 scopus 로고    scopus 로고
    • Differential in vivo regulation of steroid hormone receptor activation by Cdc37p
    • Fliss, A. E., Fang, Y., Boschelli, F., and Caplan, A. J. (1997). Differential in vivo regulation of steroid hormone receptor activation by Cdc37p. Mol. Biol. Cell 8, 2501-2509.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2501-2509
    • Fliss, A.E.1    Fang, Y.2    Boschelli, F.3    Caplan, A.J.4
  • 19
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cylophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman, B. C., Toft, D. O., and Morimoto, R. I. (1996). Molecular chaperone machines: chaperone activities of the cylophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science 274, 1718-1720.
    • (1996) Science , vol.274 , pp. 1718-1720
    • Freeman, B.C.1    Toft, D.O.2    Morimoto, R.I.3
  • 20
    • 0034102339 scopus 로고    scopus 로고
    • The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
    • Freeman, B. C., Felts, S. J., Toft, D. O., and Yamamoto, K. R. (2000). The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. Genes Dev. 14, 422-434.
    • (2000) Genes Dev , vol.14 , pp. 422-434
    • Freeman, B.C.1    Felts, S.J.2    Toft, D.O.3    Yamamoto, K.R.4
  • 21
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman, J., and Höhfeld, J. (1997). Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci. 22, 87-92.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 87-92
    • Frydman, J.1    Höhfeld, J.2
  • 22
  • 25
    • 0031018112 scopus 로고    scopus 로고
    • Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids
    • Hu, J., Toft, D. O., and Seeger, C. (1997). Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids. EMBO J. 16, 59-68.
    • (1997) EMBO J , vol.16 , pp. 59-68
    • Hu, J.1    Toft, D.O.2    Seeger, C.3
  • 26
    • 0031127737 scopus 로고    scopus 로고
    • Cdc37: A protein kinase chaperone
    • Hunter, T., and Poon, R. Y. C. (1997). Cdc37: a protein kinase chaperone. Trends Cell Biol. 7, 157-161.
    • (1997) Trends Cell Biol , vol.7 , pp. 157-161
    • Hunter, T.1    Poon, R.Y.C.2
  • 29
    • 0030462612 scopus 로고    scopus 로고
    • Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast
    • Louvion, J.-F., Warth, R., and Picard, D. (1996). Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast. Proc. Natl. Acad. Sci. USA 93, 13937-13942.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13937-13942
    • Louvion, J.-F.1    Warth, R.2    Picard, D.3
  • 30
    • 0031755018 scopus 로고    scopus 로고
    • Cns1 is an essential protein associated with the hsp9O chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Δ cells
    • Marsh, J. A., Kalton, H. M., and Gaber, R. F. (1998). Cns1 is an essential protein associated with the hsp9O chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Δ cells. Mol. Cell. Biol. 18, 7353-7359.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 7353-7359
    • Marsh, J.A.1    Kalton, H.M.2    Gaber, R.F.3
  • 31
    • 0034602390 scopus 로고    scopus 로고
    • Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from saccharomyces cerevisiae, differ in their functional properties
    • Mayr, C., Richter, K., Lilie, H., and Buchner, J. (2000). Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from saccharomyces cerevisiae, differ in their functional properties. J. Biol. Chem. 275, 34140-34146.
    • (2000) J. Biol. Chem , vol.275 , pp. 34140-34146
    • Mayr, C.1    Richter, K.2    Lilie, H.3    Buchner, J.4
  • 32
    • 0024469206 scopus 로고
    • Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae
    • Nicolet, C. M., and Craig, E. A. (1989). Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae. Mol. Cell. Biol. 9, 3638-3646.
    • (1989) Mol. Cell. Biol , vol.9 , pp. 3638-3646
    • Nicolet, C.M.1    Craig, E.A.2
  • 33
    • 0029101382 scopus 로고
    • The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin Hsp56 bind to a common site on Hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor
    • Owens-Grillo, J. K., Hoffmann, K., Hutchison, K. A., Yem, A. W., Deibel, M. R., Handschumacher, R. E., and Pratt, W. B. (1995). The cyclosporin A-binding immunophilin CyP-40 and the FK506-binding immunophilin Hsp56 bind to a common site on Hsp90 and exist in independent cytosolic heterocomplexes with the untransformed glucocorticoid receptor J. Biol. Chem. 270, 20479-20484.
    • (1995) J. Biol. Chem , vol.270 , pp. 20479-20484
    • Owens-Grillo, J.K.1    Hoffmann, K.2    Hutchison, K.A.3    Yem, A.W.4    Deibel, M.R.5    Handschumacher, R.E.6    Pratt, W.B.7
  • 34
    • 0029889955 scopus 로고    scopus 로고
    • A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains
    • Owens-Grillo, J. K., Czar, M. J., Hutchison, K. A., Hoffman, K., Perdew, G. H., and Pratt, W. B. (1996). A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains. J. Biol. Chem. 271, 13468-13475.
    • (1996) J. Biol. Chem , vol.271 , pp. 13468-13475
    • Owens-Grillo, J.K.1    Czar, M.J.2    Hutchison, K.A.3    Hoffman, K.4    Perdew, G.H.5    Pratt, W.B.6
  • 35
    • 0033951278 scopus 로고    scopus 로고
    • Structure and in vivo function of Hsp90
    • Pearl, L. H., and Prodromou, C. (2000). Structure and in vivo function of Hsp90. Curr. Opin. Struct. Biol. 10, 46-51.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 46-51
    • Pearl, L.H.1    Prodromou, C.2
  • 36
    • 0034968225 scopus 로고    scopus 로고
    • Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40
    • Pirkl, F., and Buchner, J. (2001). Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. J. Mol. Biol. 308, 795-806.
    • (2001) J. Mol. Biol , vol.308 , pp. 795-806
    • Pirkl, F.1    Buchner, J.2
  • 37
    • 0035205522 scopus 로고    scopus 로고
    • Hsp90-binding immunophilins in plants: The protein movers
    • Pratt, W. B., Krishna, P., and Olsen, L. J. (2001). Hsp90-binding immunophilins in plants: the protein movers. Trends Plant Sci. 6, 54-58.
    • (2001) Trends Plant Sci , vol.6 , pp. 54-58
    • Pratt, W.B.1    Krishna, P.2    Olsen, L.J.3
  • 40
    • 0034625327 scopus 로고    scopus 로고
    • Overlapping sites of tetratricopeptide repeat protein binding and chaperone activity in heat shock protein 90
    • Ramsey, A. J., Russell, L. C., Whitt, S. R., and Chinkers, M. (2000). Overlapping sites of tetratricopeptide repeat protein binding and chaperone activity in heat shock protein 90. J. Biol. Chem. 275, 17857-17862.
    • (2000) J. Biol. Chem , vol.275 , pp. 17857-17862
    • Ramsey, A.J.1    Russell, L.C.2    Whitt, S.R.3    Chinkers, M.4
  • 41
    • 0035937187 scopus 로고    scopus 로고
    • Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor
    • Rao, J., Lee, P., Benzeno, S., Cardozo, C., Albertus, J., Robins, D. M., and Caplan, A. J. (2001). Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor. J. Biol. Chem. 276, 5814-5820.
    • (2001) J. Biol. Chem , vol.276 , pp. 5814-5820
    • Rao, J.1    Lee, P.2    Benzeno, S.3    Cardozo, C.4    Albertus, J.5    Robins, D.M.6    Caplan, A.J.7
  • 42
    • 0019162297 scopus 로고
    • The selection of S. cerevisiae mutants defective in the start event of cell division
    • Reed, S. I. (1980). The selection of S. cerevisiae mutants defective in the start event of cell division. Genetics 95, 561-577.
    • (1980) Genetics , vol.95 , pp. 561-577
    • Reed, S.I.1
  • 44
    • 0027184524 scopus 로고
    • Silent domains are assembled continuously from the telomere and are defined by promoter distance and strength, and by SIR3 dosage
    • Renauld, H., Aparicio, O. M., Zierath, P. D., Billington, B. L., Chhablani, S. K., and Gottschling, D. E. (1993). Silent domains are assembled continuously from the telomere and are defined by promoter distance and strength, and by SIR3 dosage. Genes Dev. 7, 1133-1145.
    • (1993) Genes Dev , vol.7 , pp. 1133-1145
    • Renauld, H.1    Aparicio, O.M.2    Zierath, P.D.3    Billington, B.L.4    Chhablani, S.K.5    Gottschling, D.E.6
  • 45
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler, C., Brinker, A, Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., and Moarefi, I. (2000). Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 46
    • 0030946332 scopus 로고    scopus 로고
    • The yeast CDC37 gene interacts with MPS1 and is required for proper execution of spindle pole body duplication
    • Schutz, A. R., Giddings, T. H., Jr., Steiner, E., and Winey, M. (1997). The yeast CDC37 gene interacts with MPS1 and is required for proper execution of spindle pole body duplication. J. Cell Biol. 136, 969-982.
    • (1997) J. Cell Biol , vol.136 , pp. 969-982
    • Schutz, A.R.1    Giddings T.H., Jr.2    Steiner, E.3    Winey, M.4
  • 47
    • 0035808455 scopus 로고    scopus 로고
    • Hsp90 regulates p50(Cdc37) function during the biogenesis of the active conformation of the heme-regulated elF2α kinase
    • Shao, J., Grammatikakis, N., Scroggins, B. T., Uma, S., Huang, W., Chen, J. J., Hartson, S. D., and Matts, R. L. (2001). Hsp90 regulates p50(Cdc37) function during the biogenesis of the active conformation of the heme-regulated elF2α kinase. J. Biol. Chem. 276, 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.5    Chen, J.J.6    Hartson, S.D.7    Matts, R.L.8
  • 48
    • 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. (1998). 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, 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
  • 49
    • 0029008667 scopus 로고
    • The KIN28 gene is required both for RNA polymerase II mediated transcription and phosphorylation of the Rpb1p CTD
    • Valay, J. G., Simon, M., Dubois, M. F., Bensaude, O., Facca, C., and Faye, G. (1995). The KIN28 gene is required both for RNA polymerase II mediated transcription and phosphorylation of the Rpb1p CTD. J. Mol. Biol. 249, 535-544.
    • (1995) J. Mol. Biol , vol.249 , pp. 535-544
    • Valay, J.G.1    Simon, M.2    Dubois, M.F.3    Bensaude, O.4    Facca, C.5    Faye, G.6
  • 50
    • 0030919428 scopus 로고    scopus 로고
    • Functional analysis of the yeast 40 kDa cyclophilin Cyp40 and its role for viability and steroid receptor regulation
    • Warth, R., Briand, P.-A., and Picard, D. (1997). Functional analysis of the yeast 40 kDa cyclophilin Cyp40 and its role for viability and steroid receptor regulation. Biol. Chem. 378, 381-391.
    • (1997) Biol. Chem , vol.378 , pp. 381-391
    • Warth, R.1    Briand, P.-A.2    Picard, D.3
  • 51
    • 0032760261 scopus 로고    scopus 로고
    • An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function
    • Weikl, T., Abelmann, K., and Buchner, J. (1999). An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function. J. Mol. Biol. 293, 685-691.
    • (1999) J. Mol. Biol , vol.293 , pp. 685-691
    • Weikl, T.1    Abelmann, K.2    Buchner, J.3
  • 52
    • 0032541163 scopus 로고    scopus 로고
    • Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90
    • Young, J. C., Obermann, W. M. J., and Hartl, F. U. (1998). Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90. J. Biol. Chem. 273, 18007-18010.
    • (1998) J. Biol. Chem , vol.273 , pp. 18007-18010
    • Young, J.C.1    Obermann, W.M.J.2    Hartl, F.U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.