-
1
-
-
5044239107
-
Pathways of chaperone-mediated protein folding in the cytosol
-
Young J.C., et al. Pathways of chaperone-mediated protein folding in the cytosol. Nat. Rev. Mol. Cell Biol. 5 (2004) 781-791
-
(2004)
Nat. Rev. Mol. Cell Biol.
, vol.5
, pp. 781-791
-
-
Young, J.C.1
-
2
-
-
30344462410
-
Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
-
Albanèse V., et al. Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell 124 (2006) 75-88
-
(2006)
Cell
, vol.124
, pp. 75-88
-
-
Albanèse, V.1
-
3
-
-
18344363175
-
Estrogen receptor beta in breast cancer
-
Palmieri C., et al. Estrogen receptor beta in breast cancer. Endocr. Relat. Cancer 9 (2002) 1-13
-
(2002)
Endocr. Relat. Cancer
, vol.9
, pp. 1-13
-
-
Palmieri, C.1
-
4
-
-
0034463399
-
Molecular chaperone interactions with steroid receptors: an update
-
Cheung J., and Smith D.F. Molecular chaperone interactions with steroid receptors: an update. Mol. Endocrinol. 14 (2000) 939-946
-
(2000)
Mol. Endocrinol.
, vol.14
, pp. 939-946
-
-
Cheung, J.1
Smith, D.F.2
-
5
-
-
3142550874
-
Role of molecular chaperones in steroid receptor action
-
Pratt W.B., et al. Role of molecular chaperones in steroid receptor action. Essays Biochem. 40 (2004) 41-58
-
(2004)
Essays Biochem.
, vol.40
, pp. 41-58
-
-
Pratt, W.B.1
-
6
-
-
0037315208
-
Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
-
Pratt W.B., and Toft D.O. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med (Maywood). 228 (2003) 111-133
-
(2003)
Exp. Biol. Med (Maywood).
, vol.228
, pp. 111-133
-
-
Pratt, W.B.1
Toft, D.O.2
-
7
-
-
3543037605
-
Tetratricopeptide repeat cochaperones in steroid receptor complexes
-
Smith D.F. Tetratricopeptide repeat cochaperones in steroid receptor complexes. Cell Stress Chaperones 9 (2004) 109-121
-
(2004)
Cell Stress Chaperones
, vol.9
, pp. 109-121
-
-
Smith, D.F.1
-
8
-
-
0037023732
-
HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor
-
Hernández M.P., et al. HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor. J. Biol. Chem. 277 (2002) 11873-11881
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 11873-11881
-
-
Hernández, M.P.1
-
9
-
-
0034629150
-
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., et al. 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 (2000) 6894-6900
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 6894-6900
-
-
Morishima, Y.1
-
10
-
-
0032484127
-
The assembly of progesterone receptor-hsp90 complexes using purified proteins
-
Kosano H., et al. The assembly of progesterone receptor-hsp90 complexes using purified proteins. J. Biol. Chem. 273 (1998) 32973-32979
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 32973-32979
-
-
Kosano, H.1
-
11
-
-
0031238563
-
Yeast molecular chaperones and the mechanism of steroid hormone action
-
Caplan A.J. Yeast molecular chaperones and the mechanism of steroid hormone action. Trends Endocrinol. Metab. 8 (1997) 271-276
-
(1997)
Trends Endocrinol. Metab.
, vol.8
, pp. 271-276
-
-
Caplan, A.J.1
-
12
-
-
18444405534
-
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 110 (2002) 93-105
-
(2002)
Cell
, vol.110
, pp. 93-105
-
-
Bledsoe, R.K.1
-
13
-
-
0025175208
-
Reduced levels of hsp90 compromise steroid receptor action in vivo
-
Picard D., et al. Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature 348 (1990) 166-168
-
(1990)
Nature
, vol.348
, pp. 166-168
-
-
Picard, D.1
-
14
-
-
0030810984
-
The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin
-
Segnitz B., and Gehring U. The function of steroid hormone receptors is inhibited by the hsp90-specific compound geldanamycin. J. Biol. Chem. 272 (1997) 18694-18701
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 18694-18701
-
-
Segnitz, B.1
Gehring, U.2
-
15
-
-
28144439277
-
CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-α
-
Fan M., et al. CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-α. Mol. Endocrinol. 19 (2005) 2901-2914
-
(2005)
Mol. Endocrinol.
, vol.19
, pp. 2901-2914
-
-
Fan, M.1
-
16
-
-
0023896114
-
Requirement of hormone for thermal conversion of the glucocorticoid receptor to a DNA-binding state
-
Denis M., et al. Requirement of hormone for thermal conversion of the glucocorticoid receptor to a DNA-binding state. Nature 333 (1988) 686-688
-
(1988)
Nature
, vol.333
, pp. 686-688
-
-
Denis, M.1
-
17
-
-
0023664416
-
Relationship of the 90-kDa murine heat shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor
-
Sanchez E.R., et al. Relationship of the 90-kDa murine heat shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor. J. Biol. Chem. 262 (1987) 6986-6991
-
(1987)
J. Biol. Chem.
, vol.262
, pp. 6986-6991
-
-
Sanchez, E.R.1
-
18
-
-
0022342203
-
Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein
-
Sanchez E.R., et al. Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. J. Biol. Chem. 260 (1985) 12398-12401
-
(1985)
J. Biol. Chem.
, vol.260
, pp. 12398-12401
-
-
Sanchez, E.R.1
-
19
-
-
0034581173
-
Posttranslational regulation of proteins by fusions to steroid-binding domains
-
Picard D. Posttranslational regulation of proteins by fusions to steroid-binding domains. Methods Enzymol. 327 (2000) 385-401
-
(2000)
Methods Enzymol.
, vol.327
, pp. 385-401
-
-
Picard, D.1
-
20
-
-
0029026540
-
Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways
-
Kimura Y., et al. Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268 (1995) 1362-1365
-
(1995)
Science
, vol.268
, pp. 1362-1365
-
-
Kimura, Y.1
-
21
-
-
0034005058
-
A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast
-
Johnson J.L., and Craig E.A. A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast. Mol. Cell. Biol. 20 (2000) 3027-3036
-
(2000)
Mol. Cell. Biol.
, vol.20
, pp. 3027-3036
-
-
Johnson, J.L.1
Craig, E.A.2
-
22
-
-
29244464699
-
Repressive domain of unliganded human estrogen receptor α associates with Hsc70
-
Ogawa S., et al. Repressive domain of unliganded human estrogen receptor α associates with Hsc70. Genes Cells 10 (2005) 1095-1102
-
(2005)
Genes Cells
, vol.10
, pp. 1095-1102
-
-
Ogawa, S.1
-
23
-
-
0035898534
-
The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR
-
Donzé O., et al. The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR. EMBO J. 20 (2001) 3771-3780
-
(2001)
EMBO J.
, vol.20
, pp. 3771-3780
-
-
Donzé, O.1
-
24
-
-
0043028205
-
What is a co-chaperone?
-
Caplan A.J. What is a co-chaperone?. Cell Stress Chaperones 8 (2003) 105-107
-
(2003)
Cell Stress Chaperones
, vol.8
, pp. 105-107
-
-
Caplan, A.J.1
-
25
-
-
0033578875
-
The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone
-
Liu X.D., et al. The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone. J. Biol. Chem. 274 (1999) 26654-26660
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 26654-26660
-
-
Liu, X.D.1
-
26
-
-
3042748160
-
The heat shock protein 70 cochaperone Hip enhances functional maturation of glucocorticoid receptor
-
Nelson G.M., et al. The heat shock protein 70 cochaperone Hip enhances functional maturation of glucocorticoid receptor. Mol. Endocrinol. 18 (2004) 1620-1630
-
(2004)
Mol. Endocrinol.
, vol.18
, pp. 1620-1630
-
-
Nelson, G.M.1
-
27
-
-
3042702990
-
γ synuclein, a novel heat-shock protein-associated chaperone, stimulates ligand-dependent estrogen receptor α signaling and mammary tumorigenesis
-
Jiang Y., et al. γ synuclein, a novel heat-shock protein-associated chaperone, stimulates ligand-dependent estrogen receptor α signaling and mammary tumorigenesis. Cancer Res. 64 (2004) 4539-4546
-
(2004)
Cancer Res.
, vol.64
, pp. 4539-4546
-
-
Jiang, Y.1
-
28
-
-
0344443774
-
BAG-1 - a nucleotide exchange factor of Hsc70 with multiple cellular functions
-
Alberti S., et al. BAG-1 - a nucleotide exchange factor of Hsc70 with multiple cellular functions. Cell Stress Chaperones 8 (2003) 225-231
-
(2003)
Cell Stress Chaperones
, vol.8
, pp. 225-231
-
-
Alberti, S.1
-
29
-
-
0141640853
-
The cochaperone Bag-1L enhances androgen receptor action via interaction with the NH2-terminal region of the receptor
-
Shatkina L., et al. The cochaperone Bag-1L enhances androgen receptor action via interaction with the NH2-terminal region of the receptor. Mol. Cell. Biol. 23 (2003) 7189-7197
-
(2003)
Mol. Cell. Biol.
, vol.23
, pp. 7189-7197
-
-
Shatkina, L.1
-
30
-
-
0041783921
-
The nuclear BAG-1 isoform, BAG-1L, enhances oestrogen-dependent transcription
-
Cutress R.I., et al. The nuclear BAG-1 isoform, BAG-1L, enhances oestrogen-dependent transcription. Oncogene 22 (2003) 4973-4982
-
(2003)
Oncogene
, vol.22
, pp. 4973-4982
-
-
Cutress, R.I.1
-
31
-
-
14844283118
-
A type I DnaJ homolog, DjA1, regulates androgen receptor signaling and spermatogenesis
-
Terada K., et al. A type I DnaJ homolog, DjA1, regulates androgen receptor signaling and spermatogenesis. EMBO J. 24 (2005) 611-622
-
(2005)
EMBO J.
, vol.24
, pp. 611-622
-
-
Terada, K.1
-
32
-
-
0030659844
-
Differential in vivo regulation of steroid hormone receptor activation by Cdc37p
-
Fliss A.E., et al. Differential in vivo regulation of steroid hormone receptor activation by Cdc37p. Mol. Biol. Cell 8 (1997) 2501-2509
-
(1997)
Mol. Biol. Cell
, vol.8
, pp. 2501-2509
-
-
Fliss, A.E.1
-
33
-
-
0036931438
-
Activation of the ATPase activity of Hsp90 by the stress-regulated cochaperone Aha1
-
Panaretou B., et al. Activation of the ATPase activity of Hsp90 by the stress-regulated cochaperone Aha1. Mol. Cell 10 (2002) 1307-1318
-
(2002)
Mol. Cell
, vol.10
, pp. 1307-1318
-
-
Panaretou, B.1
-
34
-
-
18844406200
-
Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation
-
Harst A., et al. Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation. Biochem. J. 387 (2005) 789-796
-
(2005)
Biochem. J.
, vol.387
, pp. 789-796
-
-
Harst, A.1
-
35
-
-
0042815093
-
Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system
-
Brychzy A., et al. Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system. EMBO J. 22 (2003) 3613-3623
-
(2003)
EMBO J.
, vol.22
, pp. 3613-3623
-
-
Brychzy, A.1
-
36
-
-
33644524059
-
GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway
-
Chadli A., et al. GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway. Mol. Cell. Biol. 26 (2006) 1722-1730
-
(2006)
Mol. Cell. Biol.
, vol.26
, pp. 1722-1730
-
-
Chadli, A.1
-
37
-
-
20044382800
-
Navigating the chaperone network: integrative map of physical and genetic interactions mediated by the Hsp90 chaperone
-
Zhao R., et al. Navigating the chaperone network: integrative map of physical and genetic interactions mediated by the Hsp90 chaperone. Cell 120 (2005) 715-727
-
(2005)
Cell
, vol.120
, pp. 715-727
-
-
Zhao, R.1
-
38
-
-
0035146685
-
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
-
Connell P., et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell Biol. 3 (2001) 93-96
-
(2001)
Nat. Cell Biol.
, vol.3
, pp. 93-96
-
-
Connell, P.1
-
39
-
-
0042357461
-
Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae
-
Tesic M., et al. Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae. J. Biol. Chem. 278 (2003) 32692-32701
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 32692-32701
-
-
Tesic, M.1
-
40
-
-
11844276669
-
Functional specificity of co-chaperone interactions with Hsp90 client proteins
-
Riggs D., et al. Functional specificity of co-chaperone interactions with Hsp90 client proteins. Crit. Rev. Biochem. Mol. Biol. 39 (2004) 279-295
-
(2004)
Crit. Rev. Biochem. Mol. Biol.
, vol.39
, pp. 279-295
-
-
Riggs, D.1
-
41
-
-
0035169503
-
Overexpression of the FK506-binding immunophilin FKBP51 is the common cause of glucocorticoid resistance in three New World primates
-
Scammell J.G., et al. Overexpression of the FK506-binding immunophilin FKBP51 is the common cause of glucocorticoid resistance in three New World primates. Gen. Comp. Endocrinol. 124 (2001) 152-165
-
(2001)
Gen. Comp. Endocrinol.
, vol.124
, pp. 152-165
-
-
Scammell, J.G.1
-
42
-
-
0037416154
-
The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
-
Riggs D.L., et al. The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo. EMBO J. 22 (2003) 1158-1167
-
(2003)
EMBO J.
, vol.22
, pp. 1158-1167
-
-
Riggs, D.L.1
-
43
-
-
14244262261
-
FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells
-
Wochnik G.M., et al. FK506-binding proteins 51 and 52 differentially regulate dynein interaction and nuclear translocation of the glucocorticoid receptor in mammalian cells. J. Biol. Chem. 280 (2005) 4609-4616
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 4609-4616
-
-
Wochnik, G.M.1
-
44
-
-
2442537231
-
Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement
-
Pratt W.B., et al. Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement. Cell. Signal. 16 (2004) 857-872
-
(2004)
Cell. Signal.
, vol.16
, pp. 857-872
-
-
Pratt, W.B.1
-
45
-
-
22344451728
-
Physiological role for the cochaperone FKBP52 in androgen receptor signaling
-
Cheung-Flynn J., et al. Physiological role for the cochaperone FKBP52 in androgen receptor signaling. Mol. Endocrinol. 19 (2005) 1654-1666
-
(2005)
Mol. Endocrinol.
, vol.19
, pp. 1654-1666
-
-
Cheung-Flynn, J.1
-
46
-
-
26444475400
-
Cochaperone immunophilin FKBP52 is critical to uterine receptivity for embryo implantation
-
Tranguch S., et al. Cochaperone immunophilin FKBP52 is critical to uterine receptivity for embryo implantation. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 14326-14331
-
(2005)
Proc. Natl. Acad. Sci. U. S. A.
, vol.102
, pp. 14326-14331
-
-
Tranguch, S.1
-
47
-
-
2342573676
-
Protein phosphatase 5 is a negative regulator of estrogen receptor-mediated transcription
-
Ikeda K., et al. Protein phosphatase 5 is a negative regulator of estrogen receptor-mediated transcription. Mol. Endocrinol. 18 (2004) 1131-1143
-
(2004)
Mol. Endocrinol.
, vol.18
, pp. 1131-1143
-
-
Ikeda, K.1
-
48
-
-
31444454302
-
The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90
-
Wandinger S.K., et al. The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90. EMBO J. 25 (2006) 367-376
-
(2006)
EMBO J.
, vol.25
, pp. 367-376
-
-
Wandinger, S.K.1
-
49
-
-
0042026348
-
p23, a simple protein with complex activities
-
Felts S.J., and Toft D.O. p23, a simple protein with complex activities. Cell Stress Chaperones 8 (2003) 108-113
-
(2003)
Cell Stress Chaperones
, vol.8
, pp. 108-113
-
-
Felts, S.J.1
Toft, D.O.2
-
50
-
-
0032915424
-
Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction
-
Knoblauch R., and Garabedian M.J. Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction. Mol. Cell. Biol. 19 (1999) 3748-3759
-
(1999)
Mol. Cell. Biol.
, vol.19
, pp. 3748-3759
-
-
Knoblauch, R.1
Garabedian, M.J.2
-
51
-
-
0034102339
-
The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
-
Freeman B.C., et al. The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. Genes Dev. 14 (2000) 422-434
-
(2000)
Genes Dev.
, vol.14
, pp. 422-434
-
-
Freeman, B.C.1
-
52
-
-
1342286829
-
Inhibition of GR-mediated transcription by p23 requires interaction with Hsp90
-
Wochnik G.M., et al. Inhibition of GR-mediated transcription by p23 requires interaction with Hsp90. FEBS Lett. 560 (2004) 35-38
-
(2004)
FEBS Lett.
, vol.560
, pp. 35-38
-
-
Wochnik, G.M.1
-
53
-
-
0035338418
-
Continuous recycling: a mechanism for modulatory signal transduction
-
Freeman B.C., and Yamamoto K.R. Continuous recycling: a mechanism for modulatory signal transduction. Trends Biochem. Sci. 26 (2001) 285-290
-
(2001)
Trends Biochem. Sci.
, vol.26
, pp. 285-290
-
-
Freeman, B.C.1
Yamamoto, K.R.2
-
54
-
-
0030907634
-
Subnuclear trafficking of glucocorticoid receptors in vitro: chromatin recycling and nuclear export
-
Yang J., et al. Subnuclear trafficking of glucocorticoid receptors in vitro: chromatin recycling and nuclear export. J. Cell Biol. 137 (1997) 523-538
-
(1997)
J. Cell Biol.
, vol.137
, pp. 523-538
-
-
Yang, J.1
-
55
-
-
0032915842
-
Chromatin recycling of glucocorticoid receptors: implications for multiple roles of heat shock protein 90
-
Liu J., and DeFranco D.B. Chromatin recycling of glucocorticoid receptors: implications for multiple roles of heat shock protein 90. Mol. Endocrinol. 13 (1999) 355-365
-
(1999)
Mol. Endocrinol.
, vol.13
, pp. 355-365
-
-
Liu, J.1
DeFranco, D.B.2
-
56
-
-
0033555947
-
Nucleocytoplasmic trafficking of steroid-free glucocorticoid receptor
-
Haché R.J., et al. Nucleocytoplasmic trafficking of steroid-free glucocorticoid receptor. J. Biol. Chem. 274 (1999) 1432-1439
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 1432-1439
-
-
Haché, R.J.1
-
57
-
-
1142297674
-
Regulation of nuclear retention of glucocorticoid receptor by nuclear Hsp90
-
Tago K., et al. Regulation of nuclear retention of glucocorticoid receptor by nuclear Hsp90. Mol. Cell. Endocrinol. 213 (2004) 131-138
-
(2004)
Mol. Cell. Endocrinol.
, vol.213
, pp. 131-138
-
-
Tago, K.1
-
58
-
-
1542267822
-
Molecular chaperones function as steroid receptor nuclear mobility factors
-
Elbi C., et al. Molecular chaperones function as steroid receptor nuclear mobility factors. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 2876-2881
-
(2004)
Proc. Natl. Acad. Sci. U. S. A.
, vol.101
, pp. 2876-2881
-
-
Elbi, C.1
-
59
-
-
12144290835
-
Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes
-
Stavreva D.A., et al. Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes. Mol. Cell. Biol. 24 (2004) 2682-2697
-
(2004)
Mol. Cell. Biol.
, vol.24
, pp. 2682-2697
-
-
Stavreva, D.A.1
-
60
-
-
0037150683
-
Disassembly of transcriptional regulatory complexes by molecular chaperones
-
Freeman B.C., and Yamamoto K.R. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296 (2002) 2232-2235
-
(2002)
Science
, vol.296
, pp. 2232-2235
-
-
Freeman, B.C.1
Yamamoto, K.R.2
-
61
-
-
28344446376
-
Intracellular dynamics of the Hsp90 co-chaperone p23 is dictated by Hsp90
-
Picard D. Intracellular dynamics of the Hsp90 co-chaperone p23 is dictated by Hsp90. Exp. Cell Res. 312 (2006) 198-204
-
(2006)
Exp. Cell Res.
, vol.312
, pp. 198-204
-
-
Picard, D.1
-
63
-
-
22844432021
-
Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90
-
Bali P., et al. Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90. J. Biol. Chem. 280 (2005) 26729-26734
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 26729-26734
-
-
Bali, P.1
-
64
-
-
21144444486
-
HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor
-
Kovacs J.J., et al. HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Mol. Cell 18 (2005) 601-607
-
(2005)
Mol. Cell
, vol.18
, pp. 601-607
-
-
Kovacs, J.J.1
-
65
-
-
26644473193
-
Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone
-
Murphy P.J., et al. Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone. J. Biol. Chem. 280 (2005) 33792-33799
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 33792-33799
-
-
Murphy, P.J.1
-
66
-
-
0037351881
-
Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling
-
Reid G., et al. Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling. Mol. Cell 11 (2003) 695-707
-
(2003)
Mol. Cell
, vol.11
, pp. 695-707
-
-
Reid, G.1
-
67
-
-
23744495968
-
Multiple mechanisms induce transcriptional silencing of a subset of genes, including oestrogen receptor α, in response to deacetylase inhibition by valproic acid and trichostatin A
-
Reid G., et al. Multiple mechanisms induce transcriptional silencing of a subset of genes, including oestrogen receptor α, in response to deacetylase inhibition by valproic acid and trichostatin A. Oncogene 24 (2005) 4894-4907
-
(2005)
Oncogene
, vol.24
, pp. 4894-4907
-
-
Reid, G.1
-
68
-
-
27844569881
-
Opposite effects of histone deacetylase inhibitors on glucocorticoid and estrogen signaling in human endometrial Ishikawa cells
-
Rocha W., et al. Opposite effects of histone deacetylase inhibitors on glucocorticoid and estrogen signaling in human endometrial Ishikawa cells. Mol. Pharmacol. 68 (2005) 1852-1862
-
(2005)
Mol. Pharmacol.
, vol.68
, pp. 1852-1862
-
-
Rocha, W.1
-
69
-
-
0027211066
-
Nuclear progesterone receptor is mainly heat shock protein 90-free in vivo
-
Tuohimaa P., et al. Nuclear progesterone receptor is mainly heat shock protein 90-free in vivo. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 5848-5852
-
(1993)
Proc. Natl. Acad. Sci. U. S. A.
, vol.90
, pp. 5848-5852
-
-
Tuohimaa, P.1
-
70
-
-
0034817258
-
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 6 (2001) 256-262
-
(2001)
Cell Stress Chaperones
, vol.6
, pp. 256-262
-
-
Haverinen, M.1
-
71
-
-
18744414176
-
A dynamic structural model for estrogen receptor-α activation by ligands, emphasizing the role of interactions between distant A and E domains
-
Métivier R., et al. A dynamic structural model for estrogen receptor-α activation by ligands, emphasizing the role of interactions between distant A and E domains. Mol. Cell 10 (2002) 1019-1032
-
(2002)
Mol. Cell
, vol.10
, pp. 1019-1032
-
-
Métivier, R.1
-
72
-
-
0026639953
-
Examination of the DNA-binding ability of estrogen receptor in whole cells: implications for hormone-independent transactivation and the actions of antiestrogens
-
Reese J.C., and Katzenellenbogen B.S. Examination of the DNA-binding ability of estrogen receptor in whole cells: implications for hormone-independent transactivation and the actions of antiestrogens. Mol. Cell. Biol. 12 (1992) 4531-4538
-
(1992)
Mol. Cell. Biol.
, vol.12
, pp. 4531-4538
-
-
Reese, J.C.1
Katzenellenbogen, B.S.2
-
73
-
-
0033637703
-
Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
-
Shang Y., et al. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 103 (2000) 843-852
-
(2000)
Cell
, vol.103
, pp. 843-852
-
-
Shang, Y.1
-
74
-
-
20844451181
-
Transcriptional complexes engaged by apo-estrogen receptor-α isoforms have divergent outcomes
-
Métivier R., et al. Transcriptional complexes engaged by apo-estrogen receptor-α isoforms have divergent outcomes. EMBO J. 23 (2004) 3653-3666
-
(2004)
EMBO J.
, vol.23
, pp. 3653-3666
-
-
Métivier, R.1
-
75
-
-
32444436779
-
Distinct roles of unliganded and liganded estrogen receptors in transcriptional repression
-
Cvoro A., et al. Distinct roles of unliganded and liganded estrogen receptors in transcriptional repression. Mol. Cell 21 (2006) 555-564
-
(2006)
Mol. Cell
, vol.21
, pp. 555-564
-
-
Cvoro, A.1
-
76
-
-
0027484097
-
Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes
-
Smith D.F. Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol. Endocrinol. 7 (1993) 1418-1429
-
(1993)
Mol. Endocrinol.
, vol.7
, pp. 1418-1429
-
-
Smith, D.F.1
|