메뉴 건너뛰기




Volumn 2, Issue 3, 2011, Pages 104-106

Chaperones and the maturation of steroid hormone receptor complexes

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; STEROID RECEPTOR; FK 506 BINDING PROTEIN; HOMEODOMAIN PROTEIN; HOP PROTEIN, HUMAN; TACROLIMUS BINDING PROTEIN 4; TUMOR SUPPRESSOR PROTEIN;

EID: 80052046021     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.238     Document Type: Note
Times cited : (6)

References (21)
  • 1
    • 0035813186 scopus 로고    scopus 로고
    • Nuclear receptor minireview series
    • Olefsky, J.M., Nuclear receptor minireview series. J Biol Chem, 2001. 276(40): p. 36863-4.
    • (2001) J Biol Chem , vol.276 , Issue.40 , pp. 36863-36864
    • Olefsky, J.M.1
  • 2
    • 0033054115 scopus 로고    scopus 로고
    • The structure of the nuclear hormone receptors
    • Kumar, R. and E.B. Thompson, The structure of the nuclear hormone receptors. Steroids, 1999. 64(5): p. 310-9.
    • (1999) Steroids , vol.64 , Issue.5 , pp. 310-319
    • Kumar, R.1    Thompson, E.B.2
  • 3
    • 18444405534 scopus 로고    scopus 로고
    • Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition
    • Bledsoe, R.K., et al., Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell, 2002. 110(1): p. 93-105.
    • (2002) Cell , vol.110 , Issue.1 , pp. 93-105
    • Bledsoe, R.K.1
  • 4
    • 0025780755 scopus 로고
    • Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA
    • Luisi, B.F., et al., Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature, 1991. 352(6335): p. 497-505.
    • (1991) Nature , vol.352 , Issue.6335 , pp. 497-505
    • Luisi, B.F.1
  • 5
    • 33646138016 scopus 로고    scopus 로고
    • Comparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinity
    • Pereira de Jesus-Tran, K., et al., Comparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinity. Protein Sci, 2006. 15(5): p. 987-99.
    • (2006) Protein Sci , vol.15 , Issue.5 , pp. 987-999
    • Pereira de Jesus-Tran, K.1
  • 6
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau, A.K., et al., The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell, 1998. 95(7): p. 927-37.
    • (1998) Cell , vol.95 , Issue.7 , pp. 927-937
    • Shiau, A.K.1
  • 7
    • 0032575057 scopus 로고    scopus 로고
    • Atomic structure of progesterone complexed with its receptor
    • Williams, S.P. and P.B. Sigler, Atomic structure of progesterone complexed with its receptor. Nature, 1998. 393(6683): p. 392-6.
    • (1998) Nature , vol.393 , Issue.6683 , pp. 392-396
    • Williams, S.P.1    Sigler, P.B.2
  • 8
    • 77953020807 scopus 로고    scopus 로고
    • Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility
    • Echeverria, P.C. and D. Picard, Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility. Biochim Biophys Acta, 2010. 1803(6): p. 641-9.
    • (2010) Biochim Biophys Acta , vol.1803 , Issue.6 , pp. 641-649
    • Echeverria, P.C.1    Picard, D.2
  • 9
    • 0023441954 scopus 로고
    • Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor
    • Picard, D. and K.R. Yamamoto, Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor. Embo J, 1987. 6(11): p. 3333-40.
    • (1987) Embo J , vol.6 , Issue.11 , pp. 3333-3340
    • Picard, D.1    Yamamoto, K.R.2
  • 10
    • 0025382801 scopus 로고
    • Signal transduction by steroid hormones: nuclear localization is differentially regulated in estrogen and glucocorticoid receptors
    • Picard, D., et al., Signal transduction by steroid hormones: nuclear localization is differentially regulated in estrogen and glucocorticoid receptors. Cell Regul, 1990. 1(3): p. 291-9.
    • (1990) Cell Regul , vol.1 , Issue.3 , pp. 291-299
    • Picard, D.1
  • 11
    • 0028225858 scopus 로고
    • A ligand-dependent bipartite nuclear targeting signal in the human androgen receptor Requirement for the DNA-binding domain and modulation by NH2-terminal and carboxyl-terminal sequences
    • Zhou, Z.X., et al., A ligand-dependent bipartite nuclear targeting signal in the human androgen receptor. Requirement for the DNA-binding domain and modulation by NH2-terminal and carboxyl-terminal sequences. J Biol Chem, 1994. 269(18): p. 13115-23.
    • (1994) J Biol Chem , vol.269 , Issue.18 , pp. 13115-13123
    • Zhou, Z.X.1
  • 12
    • 0031846768 scopus 로고    scopus 로고
    • Differential interactions of p23 and the TPRcontaining proteins Hop, Cyp40. FKBP52 and FKBP51 with Hsp90 mutants
    • Chen, S., et al., Differential interactions of p23 and the TPRcontaining proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants. Cell Stress Chaperones, 1998. 3(2): p. 118-29.
    • (1998) Cell Stress Chaperones , vol.3 , Issue.2 , pp. 118-129
    • Chen, S.1
  • 13
    • 0028998441 scopus 로고
    • Tetratrico peptide repeat interactions: to TPR or not to TPR?
    • Lamb, J.R., S. Tugendreich, and P. Hieter, Tetratrico peptide repeat interactions: to TPR or not to TPR? Trends Biochem Sci, 1995. 20(7): p. 257-9.
    • (1995) Trends Biochem Sci , vol.20 , Issue.7 , pp. 257-259
    • Lamb, J.R.1    Tugendreich, S.2    Hieter, P.3
  • 14
    • 1342294313 scopus 로고    scopus 로고
    • The hsp90 cochaperone p23 is the limiting component of the multiprotein hsp90/hsp70-based chaperone system in vivo where it acts to stabilize the client protein: hsp90 complex
    • Morishima, Y., et al., The hsp90 cochaperone p23 is the limiting component of the multiprotein hsp90/hsp70-based chaperone system in vivo where it acts to stabilize the client protein: hsp90 complex. J Biol Chem, 2003. 278(49): p. 48754-63.
    • (2003) J Biol Chem , vol.278 , Issue.49 , pp. 48754-48763
    • Morishima, Y.1
  • 15
    • 0033613950 scopus 로고    scopus 로고
    • The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90
    • Carrello, A., et al., The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90. J Biol Chem, 1999. 274(5): p. 2682-9.
    • (1999) J Biol Chem , vol.274 , Issue.5 , pp. 2682-2689
    • Carrello, A.1
  • 16
    • 0037315208 scopus 로고    scopus 로고
    • Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
    • Pratt, W.B. and D.O. Toft, Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp Biol Med (Maywood), 2003. 228(2): p. 111-33.
    • (2003) Exp Biol Med (Maywood) , vol.228 , Issue.2 , pp. 111-133
    • Pratt, W.B.1    Toft, D.O.2
  • 17
    • 0034817258 scopus 로고    scopus 로고
    • Heat shock protein 90 and the nuclear transport of progesterone receptor
    • Haverinen, M., et al., Heat shock protein 90 and the nuclear transport of progesterone receptor. Cell Stress Chaperones, 2001. 6(3): p. 256-62.
    • (2001) Cell Stress Chaperones , vol.6 , Issue.3 , pp. 256-262
    • Haverinen, M.1
  • 18
    • 0032567434 scopus 로고    scopus 로고
    • Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery
    • Chen, S. and D.F. Smith, Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery. J Biol Chem, 1998. 273(52): p. 35194-200.
    • (1998) J Biol Chem , vol.273 , Issue.52 , pp. 35194-35200
    • Chen, S.1    Smith, D.F.2
  • 19
    • 0031053574 scopus 로고    scopus 로고
    • Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor
    • Nair, S.C., et al., Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor. Mol Cell Biol, 1997. 17(2): p. 594-603.
    • (1997) Mol Cell Biol , vol.17 , Issue.2 , pp. 594-603
    • Nair, S.C.1
  • 20
    • 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., et al., 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, 1995. 270(35): p. 20479-84.
    • (1995) J Biol Chem , vol.270 , Issue.35 , pp. 20479-20484
    • Owens-Grillo, J.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.