메뉴 건너뛰기




Volumn 119, Issue 3, 2003, Pages 456-462

The 70-kDa protein bound to hsp90 in wheat germ lysate is a plant homologue of animal Hop

Author keywords

[No Author keywords available]

Indexed keywords

DEGRADATION; PROTEINS;

EID: 0242309035     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.2003.00185.x     Document Type: Article
Times cited : (6)

References (25)
  • 1
    • 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 RA, Honoré B, Smith DF (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
  • 2
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery
    • Chen S, Smith DF (1998) Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery. J Biol Chem 273: 35194-35200
    • (1998) J Biol Chem , vol.273 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 3
    • 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 273: 7358-7366
    • (1997) J Biol Chem , vol.273 , pp. 7358-7366
    • Dittmar, K.D.1    Demady, D.R.2    Stancato, L.F.3    Krishna, P.4    Pratt, W.B.5
  • 4
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman J (2001) Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem 70: 603-647
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 5
    • 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
  • 6
    • 0029872081 scopus 로고    scopus 로고
    • The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes
    • Johnson J, Corbisier R, Stensgard B, Toft DO (1996) The involvement of p23, hsp90, and immunophilins in the assembly of progesterone receptor complexes. J Steroid Biochem Mol Biol 56: 31-37
    • (1996) J Steroid Biochem Mol Biol , vol.56 , pp. 31-37
    • Johnson, J.1    Corbisier, R.2    Stensgard, B.3    Toft, D.O.4
  • 7
    • 0032488906 scopus 로고    scopus 로고
    • Hop modulates hsp70/hsp90 interactions in protein folding
    • Johnson BD, Schumacher RJ, Ross ED, Toft DO (1998) Hop modulates hsp70/hsp90 interactions in protein folding. J Biol Chem 273: 3679-3686
    • (1998) J Biol Chem , vol.273 , pp. 3679-3686
    • Johnson, B.D.1    Schumacher, R.J.2    Ross, E.D.3    Toft, D.O.4
  • 8
    • 0033607658 scopus 로고    scopus 로고
    • Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery
    • Kanelakis KC, Morishima Y, Dittmar KD, Galigniana MD, Takayama S, Reed JC, Pratt WB (1999) Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery. J Biol Chem 274: 34134-34140
    • (1999) J Biol Chem , vol.274 , pp. 34134-34140
    • Kanelakis, K.C.1    Morishima, Y.2    Dittmar, K.D.3    Galigniana, M.D.4    Takayama, S.5    Reed, J.C.6    Pratt, W.B.7
  • 9
    • 0034817255 scopus 로고    scopus 로고
    • The Hsp90 family of proteins in Arabidopsis thaliana
    • Krishna P, Gloor G (2001) The Hsp90 family of proteins in Arabidopsis thaliana. Cell Stress Chaperones 6: 238-246
    • (2001) Cell Stress Chaperones , vol.6 , pp. 238-246
    • Krishna, P.1    Gloor, G.2
  • 10
    • 0031081435 scopus 로고    scopus 로고
    • Analysis of the native forms of the 90 kDa heat shock protein (hsp90) in plant cytosolic extracts
    • Krishna P, Reddy RK, Sacco M, Frappier JR, Felsheim RF (1997) Analysis of the native forms of the 90 kDa heat shock protein (hsp90) in plant cytosolic extracts. Plant Mol Biol 33: 457-466
    • (1997) Plant Mol Biol , vol.33 , pp. 457-466
    • Krishna, P.1    Reddy, R.K.2    Sacco, M.3    Frappier, J.R.4    Felsheim, R.F.5
  • 11
    • 0029106880 scopus 로고
    • Cold-induced accumulation of hsp90 transcripts in Brassica napus
    • Krishna P, Sacco M, Cherutti JF, Hill S (1995) Cold-induced accumulation of hsp90 transcripts in Brassica napus. Plant Physiol 107: 915-923
    • (1995) Plant Physiol , vol.107 , pp. 915-923
    • Krishna, P.1    Sacco, M.2    Cherutti, J.F.3    Hill, S.4
  • 12
    • 0035147404 scopus 로고    scopus 로고
    • Molecular chaperones and the art of recognizing a lost cause
    • McClellan AJ, Frydman J (2001) Molecular chaperones and the art of recognizing a lost cause. Nature Cell Biol 3: E51-E53
    • (2001) Nature Cell Biol , vol.3
    • McClellan, A.J.1    Frydman, J.2
  • 13
    • 0034629150 scopus 로고    scopus 로고
    • The hsp organizer protein Hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein hsp90-based chaperone system
    • Morishima Y, Kanelakis KC, Silverstein AM, Dittmar KD, Estrada L, Pratt WB (2000) The hsp organizer protein Hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein hsp90-based chaperone system. J Biol Chem 275: 6894-6900
    • (2000) J Biol Chem , vol.275 , pp. 6894-6900
    • Morishima, Y.1    Kanelakis, K.C.2    Silverstein, A.M.3    Dittmar, K.D.4    Estrada, L.5    Pratt, W.B.6
  • 14
    • 0029856744 scopus 로고    scopus 로고
    • Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants
    • Owens-Grillo JK, Stancato LF, Hoffmann K, Pratt WB, Krishna P (1996) Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants. Biochemistry 35: 15249-15255
    • (1996) Biochemistry , vol.35 , pp. 15249-15255
    • Owens-Grillo, J.K.1    Stancato, L.F.2    Hoffmann, K.3    Pratt, W.B.4    Krishna, P.5
  • 15
    • 0035205522 scopus 로고    scopus 로고
    • Hsp90-binding immunophilins in plants: The protein movers
    • Pratt WB, Krishna P, Olsen LJ (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
  • 16
    • 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. Endocri Rev 18: 306-360
    • (1997) Endocri Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 18
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for phenotypic variation
    • Queitsch C, Sangster TA, Lindquist S (2002) Hsp90 as a capacitor for phenotypic variation. Nature 417: 618-624
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3
  • 19
    • 0032245891 scopus 로고    scopus 로고
    • High molecular weight FK506-binding proteins are components of heat shock protein 90 heterocomplexes in wheat germ lysate
    • Reddy RK, Kurek I, Silverstein AM, Chinkers M, Breiman A, Krishna P (1998) High molecular weight FK506-binding proteins are components of heat shock protein 90 heterocomplexes in wheat germ lysate. Plant Physiol 118: 1395-1401
    • (1998) Plant Physiol , vol.118 , pp. 1395-1401
    • Reddy, R.K.1    Kurek, I.2    Silverstein, A.M.3    Chinkers, M.4    Breiman, A.5    Krishna, P.6
  • 21
    • 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
  • 22
    • 0030054166 scopus 로고    scopus 로고
    • Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90
    • Stancato LF, Hutchison KA, Krishna P, Pratt WB (1996) Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90. Biochemistry 35: 554-561
    • (1996) Biochemistry , vol.35 , pp. 554-561
    • Stancato, L.F.1    Hutchison, K.A.2    Krishna, P.3    Pratt, W.B.4
  • 23
    • 0029257557 scopus 로고
    • Isolation and characterization of gmsti, a stress-inducible gene from soybean (Glycine max) coding for a protein belonging to the TPR (tetratricopeptide repeats) family
    • Torres JH, Chantellard P, Stutz E (1995) Isolation and characterization of gmsti, a stress-inducible gene from soybean (Glycine max) coding for a protein belonging to the TPR (tetratricopeptide repeats) family. Plant Mol Biol 27: 1221-1226
    • (1995) Plant Mol Biol , vol.27 , pp. 1221-1226
    • Torres, J.H.1    Chantellard, P.2    Stutz, E.3
  • 24
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young JC, Moarefi I, Hartl FU (2001) Hsp90: a specialized but essential protein-folding tool. J Cell Biol 154: 267-273
    • (2001) J Cell Biol , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.