메뉴 건너뛰기




Volumn 9, Issue 1, 2004, Pages 4-20

Cooperation of heat shock protein 90 and p23 in aryl hydrocarbon receptor signaling

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AROMATIC HYDROCARBON RECEPTOR; BETA GALACTOSIDASE; CHAPERONE; FUNGAL PROTEIN; HEAT SHOCK PROTEIN 82; HEAT SHOCK PROTEIN 82G170D; HEAT SHOCK PROTEIN 90; LIGAND; PROTEIN P23; SBA1 PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; XENOBIOTIC AGENT;

EID: 1842614359     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/1466-1268(2004)009<0004:COHSPA>2.0.CO;2     Document Type: Article
Times cited : (56)

References (51)
  • 1
    • 0029852803 scopus 로고    scopus 로고
    • Chaperone function of Hsp90-associated proteins
    • Bose S, Weikl T, Bugl H, Buchner J. 1996. Chaperone function of Hsp90-associated proteins. Science 274: 1715-1717.
    • (1996) Science , vol.274 , pp. 1715-1717
    • Bose, S.1    Weikl, T.2    Bugl, H.3    Buchner, J.4
  • 2
    • 0031238563 scopus 로고    scopus 로고
    • Yeast molecular chaperones and the mechanism of steroid hormone action
    • Caplan AJ. 1997. Yeast molecular chaperones and the mechanism of steroid hormone action. Trends Endocrinol Metab 8: 271-275.
    • (1997) Trends Endocrinol Metab , vol.8 , pp. 271-275
    • Caplan, A.J.1
  • 3
    • 0028077887 scopus 로고
    • The 90-kDa heat shock protein is essential for Ah receptor signaling in a yeast expression system
    • Carver LA, Jackiw V, Bradfield CA. 1994. The 90-kDa heat shock protein is essential for Ah receptor signaling in a yeast expression system. J Biol Chem 269: 30109-30112.
    • (1994) J Biol Chem , vol.269 , pp. 30109-30112
    • Carver, L.A.1    Jackiw, V.2    Bradfield, C.A.3
  • 6
    • 0027970550 scopus 로고
    • Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex
    • Chen HS, Perdew GH. 1994. Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex. J Biol Chem 269: 27554-27558.
    • (1994) J Biol Chem , vol.269 , pp. 27554-27558
    • Chen, H.S.1    Perdew, G.H.2
  • 7
    • 0028823398 scopus 로고
    • Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity
    • Coumailleau P, Poellinger L, Gustafsson JA, Whitelaw ML. 1995. Definition of a minimal domain of the dioxin receptor that is associated with Hsp90 and maintains wild type ligand binding affinity and specificity. J Biol Chem 270: 25291-25300.
    • (1995) J Biol Chem , vol.270 , pp. 25291-25300
    • Coumailleau, P.1    Poellinger, L.2    Gustafsson, J.A.3    Whitelaw, M.L.4
  • 8
    • 0037165496 scopus 로고    scopus 로고
    • The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system
    • Cox MB, Miller CA. 2002. The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system. Toxicol Lett 129: 13-21.
    • (2002) Toxicol Lett , vol.129 , pp. 13-21
    • Cox, M.B.1    Miller, C.A.2
  • 9
    • 0032406634 scopus 로고    scopus 로고
    • The Ah receptor: A regulator of the biochemical and toxicological actions of structurally diverse chemicals
    • Denison MS, Heath-Pagliuso S. 1998. The Ah receptor: a regulator of the biochemical and toxicological actions of structurally diverse chemicals. Bull Environ Contam Toxicol 61: 557-568.
    • (1998) Bull Environ Contam Toxicol , vol.61 , pp. 557-568
    • Denison, M.S.1    Heath-Pagliuso, S.2
  • 10
    • 0030869037 scopus 로고    scopus 로고
    • Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60. hsp70
    • Dittmar KD, Demady DR, Stancato LF, Krishna P, Pratt WB. 1997. Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60. hsp70. 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
    • 0031832233 scopus 로고    scopus 로고
    • SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins
    • Fang Y, Fliss AE, Rao J, Caplan AJ. 1998. SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. 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
  • 12
    • 0034102339 scopus 로고    scopus 로고
    • The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
    • Freeman BC, Felts SJ, Toft DO, Yamamoto KR. 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
  • 13
    • 0029852712 scopus 로고    scopus 로고
    • Molecular chaperone machines: Chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23
    • Freeman BC, Toft DO, Morimoto RI. 1996. Molecular chaperone machines: chaperone activities of the cyclophilin 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
  • 14
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman BC, Yamamoto KR. 2002. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296: 2232-2235.
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 15
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D, St Jean A, Woods RA, Schiestl RH. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res 20: 1425.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1425
    • Gietz, D.1    St. Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 16
    • 0033581021 scopus 로고    scopus 로고
    • The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes
    • Grenert JP, Johnson BD, Toft DO. 1999. The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes. J Biol Chem 274: 17525-17533.
    • (1999) J Biol Chem , vol.274 , pp. 17525-17533
    • Grenert, J.P.1    Johnson, B.D.2    Toft, D.O.3
  • 17
    • 0030863995 scopus 로고    scopus 로고
    • The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation
    • Grenert JP, Sullivan WP, Fadden P, et al. 1997. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J Biol Chem 272: 23843-23850.
    • (1997) J Biol Chem , vol.272 , pp. 23843-23850
    • Grenert, J.P.1    Sullivan, W.P.2    Fadden, P.3
  • 18
    • 0034116376 scopus 로고    scopus 로고
    • The PAS superfamily: Sensors of environmental and developmental signals
    • Gu YZ, Hogenesch JB, Bradfield CA. 2000. The PAS superfamily: sensors of environmental and developmental signals. Annu Rev Pharmacol Toxicol 40: 519-561.
    • (2000) Annu Rev Pharmacol Toxicol , vol.40 , pp. 519-561
    • Gu, Y.Z.1    Hogenesch, J.B.2    Bradfield, C.A.3
  • 19
    • 0028987872 scopus 로고
    • The aryl hydrocarbon receptor complex
    • Hankinson O. 1995. The aryl hydrocarbon receptor complex. Annu Rev Pharmacol Toxicol 35: 307-340.
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 307-340
    • Hankinson, O.1
  • 20
    • 0034667405 scopus 로고    scopus 로고
    • Relative contributions of affinity and intrinsic efficacy to aryl hydrocarbon receptor ligand potency
    • Hestermann EV, Stegeman JJ, Hahn ME. 2000. Relative contributions of affinity and intrinsic efficacy to aryl hydrocarbon receptor ligand potency. Toxicol Appl Pharmacol 168: 160-172.
    • (2000) Toxicol Appl Pharmacol , vol.168 , pp. 160-172
    • Hestermann, E.V.1    Stegeman, J.J.2    Hahn, M.E.3
  • 21
    • 0029161506 scopus 로고
    • The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90
    • Hutchison KA, Stancato LF, Owens-Grillo JK, Johnson JL, Krishna P, Toft DO, Pratt WB. 1995. The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90. J Biol Chem 270: 18841-18847.
    • (1995) J Biol Chem , vol.270 , pp. 18841-18847
    • Hutchison, K.A.1    Stancato, L.F.2    Owens-Grillo, J.K.3    Johnson, J.L.4    Krishna, P.5    Toft, D.O.6    Pratt, W.B.7
  • 22
    • 0028266874 scopus 로고
    • Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes
    • Johnson JL, Beito TG, Krco CJ, Toft DO. 1994. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol Cell Biol 14: 1956-1963.
    • (1994) Mol Cell Biol , vol.14 , pp. 1956-1963
    • Johnson, J.L.1    Beito, T.G.2    Krco, C.J.3    Toft, D.O.4
  • 23
    • 0029075280 scopus 로고
    • Binding of p23 and hsp90 during assembly with the progesterone receptor
    • Johnson JL, Toft DO. 1995. Binding of p23 and hsp90 during assembly with the progesterone receptor. Mol Endocrinol 9: 670-678.
    • (1995) Mol Endocrinol , vol.9 , pp. 670-678
    • Johnson, J.L.1    Toft, D.O.2
  • 24
    • 0033531928 scopus 로고    scopus 로고
    • Evidence that the cochaperone p23 regulates ligand responsiveness of the dioxin (aryl hydrocarbon) receptor
    • Kazlauskas A, Poellinger L, Pongratz I. 1999. Evidence that the cochaperone p23 regulates ligand responsiveness of the dioxin (aryl hydrocarbon) receptor. J Biol Chem 274: 13519-13524.
    • (1999) J Biol Chem , vol.274 , pp. 13519-13524
    • Kazlauskas, A.1    Poellinger, L.2    Pongratz, I.3
  • 25
    • 0034731609 scopus 로고    scopus 로고
    • The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor
    • Kazlauskas A, Poellinger L, Pongratz I. 2000. The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor. J Biol Chem 275: 41317-41324.
    • (2000) J Biol Chem , vol.275 , pp. 41317-41324
    • Kazlauskas, A.1    Poellinger, L.2    Pongratz, I.3
  • 26
    • 0035104164 scopus 로고    scopus 로고
    • The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor
    • Kazlauskas A, Sundstrom S, Poellinger L, Pongratz I. 2001. The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor. Mol Cell Biol 21: 2594-2607.
    • (2001) Mol Cell Biol , vol.21 , pp. 2594-2607
    • Kazlauskas, A.1    Sundstrom, S.2    Poellinger, L.3    Pongratz, I.4
  • 27
    • 0029053005 scopus 로고
    • A rapid permeabilization procedure for accurate quantitative determination of beta-galactosidase activity in yeast cells
    • Kippert F. 1995. A rapid permeabilization procedure for accurate quantitative determination of beta-galactosidase activity in yeast cells. FEMS Microbiol Lett 128: 201-206.
    • (1995) FEMS Microbiol Lett , vol.128 , pp. 201-206
    • Kippert, F.1
  • 28
    • 0032915424 scopus 로고    scopus 로고
    • Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction
    • Knoblauch R, Garabedian MJ. 1999. Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction. Mol Cell Biol 19: 3748-3759.
    • (1999) Mol Cell Biol , vol.19 , pp. 3748-3759
    • Knoblauch, R.1    Garabedian, M.J.2
  • 29
    • 0031002895 scopus 로고    scopus 로고
    • A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Ma Q, Whitlock JP Jr. 1997. A novel cytoplasmic protein that interacts with the Ah receptor, contains tetratricopeptide repeat motifs, and augments the transcriptional response to 2,3,7,8-tetrachlorodibenzo-p-dioxin. J Biol Chem 272: 8878-8884.
    • (1997) J Biol Chem , vol.272 , pp. 8878-8884
    • Ma, Q.1    Whitlock Jr., J.P.2
  • 30
    • 0036303385 scopus 로고    scopus 로고
    • Stimulation of the weak ATPase activity of human hsp90 by a client protein
    • McLaughlin SH, Smith HW, Jackson SE. 2002. Stimulation of the weak ATPase activity of human hsp90 by a client protein. J Mol Biol 315: 787-798.
    • (2002) J Mol Biol , vol.315 , pp. 787-798
    • McLaughlin, S.H.1    Smith, H.W.2    Jackson, S.E.3
  • 31
    • 0033551511 scopus 로고    scopus 로고
    • Characterization of the AhR-hsp90-XAP2 core complex and the role of the immunophilin-related protein XAP2 in AhR stabilization
    • Meyer BK, Perdew GH. 1999. Characterization of the AhR-hsp90-XAP2 core complex and the role of the immunophilin-related protein XAP2 in AhR stabilization. Biochemistry 38: 8907-8917.
    • (1999) Biochemistry , vol.38 , pp. 8907-8917
    • Meyer, B.K.1    Perdew, G.H.2
  • 32
    • 0031882767 scopus 로고    scopus 로고
    • Hepatitis B virus X-associated protein 2 is a subunit of the unliganded aryl hydrocarbon receptor core complex and exhibits transcriptional enhancer activity
    • Meyer BK, Pray-Grant MG, Vanden Heuvel JP, Perdew GH. 1998. Hepatitis B virus X-associated protein 2 is a subunit of the unliganded aryl hydrocarbon receptor core complex and exhibits transcriptional enhancer activity. Mol Cell Biol 18: 978-988.
    • (1998) Mol Cell Biol , vol.18 , pp. 978-988
    • Meyer, B.K.1    Pray-Grant, M.G.2    Vanden Heuvel, J.P.3    Perdew, G.H.4
  • 33
    • 0033231057 scopus 로고    scopus 로고
    • A human aryl hydrocarbon receptor signaling pathway constructed in yeast displays additive responses to ligand mixtures
    • Miller CA. 1999. A human aryl hydrocarbon receptor signaling pathway constructed in yeast displays additive responses to ligand mixtures. Toxicol Appl Pharmacol 160: 297-303.
    • (1999) Toxicol Appl Pharmacol , vol.160 , pp. 297-303
    • Miller, C.A.1
  • 34
    • 0036229641 scopus 로고    scopus 로고
    • Two tetratricopeptide repeat proteins facilitate human aryl hydrocarbon receptor signalling in yeast
    • Miller CA. 2002. Two tetratricopeptide repeat proteins facilitate human aryl hydrocarbon receptor signalling in yeast. Cell Signal 14: 615-623.
    • (2002) Cell Signal , vol.14 , pp. 615-623
    • Miller, C.A.1
  • 35
    • 0032145257 scopus 로고    scopus 로고
    • Assessment of aryl hydrocarbon receptor complex interactions using pBEVY plasmids: Expression vectors with bi-directional promoters for use in Saccharomyces cerevisiae
    • Miller CA, Martinat MA, Hyman LE. 1998. Assessment of aryl hydrocarbon receptor complex interactions using pBEVY plasmids: expression vectors with bi-directional promoters for use in Saccharomyces cerevisiae. Nucleic Acids Res 26: 3577-3583.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3577-3583
    • Miller, C.A.1    Martinat, M.A.2    Hyman, L.E.3
  • 36
    • 0030324952 scopus 로고    scopus 로고
    • A pathway of multi-chaperone interactions common to diverse regulatory proteins: Estrogen receptor. Fes tyrosine kinase, heat shock transcription factor Hsfl, and the aryl hydrocarbon receptor
    • Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF. 1996. A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsfl, and the aryl hydrocarbon receptor. Cell Stress Chaperones 1: 237-250.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 237-250
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hjermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 37
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: Interactions with a steroid receptor and a protein kinase
    • Nathan DF, Lindquist S. 1995. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol Cell Biol 15: 3917-3925.
    • (1995) Mol Cell Biol , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 38
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • Nathan DF, Vos MH, Lindquist S. 1997. In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. Proc Natl Acad Sci U S A 94: 12949-12956.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 40
    • 0026631538 scopus 로고
    • Dual roles of the 90-kDa heat shock protein hsp90 in modulating functional activities of the dioxin receptor. Evidence that the dioxin receptor functionally belongs to a subclass of nuclear receptors which require hsp90 both for ligand binding activity and repression of intrinsic DNA binding activity
    • Pongratz I, Mason GG, Poellinger L. 1992. Dual roles of the 90-kDa heat shock protein hsp90 in modulating functional activities of the dioxin receptor. Evidence that the dioxin receptor functionally belongs to a subclass of nuclear receptors which require hsp90 both for ligand binding activity and repression of intrinsic DNA binding activity. J Biol Chem 267: 13728-13734.
    • (1992) J Biol Chem , vol.267 , pp. 13728-13734
    • Pongratz, I.1    Mason, G.G.2    Poellinger, L.3
  • 41
    • 0031895351 scopus 로고    scopus 로고
    • The hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
    • Pratt WB. 1998. The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med 217: 420-434.
    • (1998) Proc Soc Exp Biol Med , vol.217 , pp. 420-434
    • Pratt, W.B.1
  • 42
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt WB, Toft DO. 1997. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocrinol Rev 18: 306-360.
    • (1997) Endocrinol Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 43
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative transformation in yeast
    • Rothstein R. 1991. Targeting, disruption, replacement, and allele rescue: integrative transformation in yeast. Methods Enzymol 194: 281-301.
    • (1991) Methods Enzymol , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 45
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent
    • Smith DF, Whitesell L, Nair SC, Chen S, Prapapanich V, Rimerman RA. 1995. Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol Cell Biol 15: 6804-6812.
    • (1995) Mol Cell Biol , vol.15 , pp. 6804-6812
    • Smith, D.F.1    Whitesell, L.2    Nair, S.C.3    Chen, S.4    Prapapanich, V.5    Rimerman, R.A.6
  • 46
    • 1842508460 scopus 로고    scopus 로고
    • The influence of ATP and p23 on the conformation of hsp90
    • Sullivan WP, Owen BA, Toft DO. 2002. The influence of ATP and p23 on the conformation of hsp90. J Biol Chem 24: 24.
    • (2002) J Biol Chem , vol.24 , pp. 24
    • Sullivan, W.P.1    Owen, B.A.2    Toft, D.O.3
  • 48
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • Webb MR. 1992. A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc Natl Acad Sci U S A 89: 4884-4887.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 4884-4887
    • Webb, M.R.1
  • 50
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM. 1994. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci U S A 91: 8324-8328.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 51
    • 0034329452 scopus 로고    scopus 로고
    • Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
    • Young JC, Hartl FU. 2000. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J 19: 5930-5940.
    • (2000) EMBO J , vol.19 , pp. 5930-5940
    • Young, J.C.1    Hartl, F.U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.