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Volumn 8, Issue 2, 2003, Pages 125-133

Comparison of the carboxy-terminal DP-repeat region in the co-chaperones Hop and Hip

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROGESTERONE RECEPTOR; PROTEIN HIP; PROTEIN HOP; PROTEINASE; UNCLASSIFIED DRUG;

EID: 0042026344     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/1466-1268(2003)008<0125:COTCDR>2.0.CO;2     Document Type: Article
Times cited : (42)

References (19)
  • 1
    • 0037205411 scopus 로고    scopus 로고
    • Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes
    • Brinker A, Scheufler C, Von Der Mulbe F, et al. 2002. Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes. J Biol Chem 277: 19265-19275.
    • (2002) J Biol Chem , vol.277 , pp. 19265-19275
    • Brinker, A.1    Scheufler, C.2    Von Der Mulbe, F.3
  • 2
    • 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, Honore 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    Honore, B.4    Smith, D.F.5
  • 3
    • 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
  • 4
    • 0034463399 scopus 로고    scopus 로고
    • Molecular chaperone interactions with steroid receptors: An update
    • Cheung J, Smith DF. 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
  • 5
    • 0028842615 scopus 로고
    • Hip, a novel co-chaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Hohfeld J, Minami Y, Hartl FU. 1995. Hip, a novel co-chaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83: 589-598.
    • (1995) Cell , vol.83 , pp. 589-598
    • Hohfeld, J.1    Minami, Y.2    Hartl, F.U.3
  • 6
    • 0031029286 scopus 로고    scopus 로고
    • Characterization of functional domains of the eukaryotic co-chaperone Hip
    • Irmer H, Hohfeld J. 1997. Characterization of functional domains of the eukaryotic co-chaperone Hip. J Biol Chem 272: 2230-2235.
    • (1997) J Biol Chem , vol.272 , pp. 2230-2235
    • Irmer, H.1    Hohfeld, J.2
  • 7
    • 0034700318 scopus 로고    scopus 로고
    • Hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1
    • Kanelakis KC, Murphy PJ, Galigniana MD, et al. 2000. Hsp70 interacting protein Hip does not affect glucocorticoid receptor folding by the hsp90-based chaperone machinery except to oppose the effect of BAG-1. Biochemistry 39: 14314-14321.
    • (2000) Biochemistry , vol.39 , pp. 14314-14321
    • Kanelakis, K.C.1    Murphy, P.J.2    Galigniana, M.D.3
  • 8
    • 0028860567 scopus 로고
    • Limited proteolysis of DNA polymerases as probe of functional domains
    • Konigsberg WH. 1995. Limited proteolysis of DNA polymerases as probe of functional domains. Methods Enzymol 262: 331-346.
    • (1995) Methods Enzymol , vol.262 , pp. 331-346
    • Konigsberg, W.H.1
  • 9
    • 0031036746 scopus 로고    scopus 로고
    • Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases
    • Lassle M, Blatch GL, Kundra V, Takatori T, Zetter BR. 1997. Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases. J Biol Chem 272: 1876-1884.
    • (1997) J Biol Chem , vol.272 , pp. 1876-1884
    • Lassle, M.1    Blatch, G.L.2    Kundra, V.3    Takatori, T.4    Zetter, B.R.5
  • 10
    • 0029964506 scopus 로고    scopus 로고
    • Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein
    • Prapapanich V, Chen S, Nair SC, Rimerman RA, Smith DF. 1996a. Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein. Mol Endocrinol 10: 420-431.
    • (1996) Mol Endocrinol , vol.10 , pp. 420-431
    • Prapapanich, V.1    Chen, S.2    Nair, S.C.3    Rimerman, R.A.4    Smith, D.F.5
  • 11
    • 0031931061 scopus 로고    scopus 로고
    • Mutation of Hip's carboxyterminal region inhibits a transitional stage of progesterone receptor assembly
    • Prapapanich V, Chen S, Smith DF. 1998. Mutation of Hip's carboxyterminal region inhibits a transitional stage of progesterone receptor assembly. Mol Cell Biol 18: 944-952.
    • (1998) Mol Cell Biol , vol.18 , pp. 944-952
    • Prapapanich, V.1    Chen, S.2    Smith, D.F.3
  • 13
    • 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. Endocr Rev 18: 306-360.
    • (1997) Endocr Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 14
    • 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, et al. 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
  • 15
    • 0027439595 scopus 로고
    • Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70
    • Smith D, Sullivan W, Marion T, et al. 1993. Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol Cell Biol 13: 869-876.
    • (1993) Mol Cell Biol , vol.13 , pp. 869-876
    • Smith, D.1    Sullivan, W.2    Marion, T.3
  • 16
    • 0027484097 scopus 로고
    • Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes
    • Smith DF. 1993. Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol Endocrinol 7: 1418-1429.
    • (1993) Mol Endocrinol , vol.7 , pp. 1418-1429
    • Smith, D.F.1
  • 17
    • 0031925151 scopus 로고    scopus 로고
    • Sequence motifs shared between chaperone components participating in the assembly of progesterone receptor complexes
    • Smith DF. 1998. Sequence motifs shared between chaperone components participating in the assembly of progesterone receptor complexes. Biol Chem 379: 283-288.
    • (1998) Biol Chem , vol.379 , pp. 283-288
    • Smith, D.F.1
  • 18
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.