| Year |
Citation |
Score |
| 2014 |
Hinds TD, Stechschulte LA, Elkhairi F, Sanchez ER. Analysis of FK506, timcodar (VX-853) and FKBP51 and FKBP52 chaperones in control of glucocorticoid receptor activity and phosphorylation. Pharmacology Research & Perspectives. 2: e00076. PMID 25505617 DOI: 10.1002/prp2.76 |
0.348 |
|
| 2014 |
Stechschulte LA, Hinds TD, Ghanem SS, Shou W, Najjar SM, Sanchez ER. FKBP51 reciprocally regulates GRα and PPARγ activation via the Akt-p38 pathway. Molecular Endocrinology (Baltimore, Md.). 28: 1254-64. PMID 24933248 DOI: 10.1210/Me.2014-1023 |
0.366 |
|
| 2012 |
Sanchez ER. Chaperoning steroidal physiology: lessons from mouse genetic models of Hsp90 and its cochaperones. Biochimica Et Biophysica Acta. 1823: 722-9. PMID 22155719 DOI: 10.1016/j.bbamcr.2011.11.006 |
0.43 |
|
| 2011 |
Banasavadi-Siddegowda YK, Mai J, Fan Y, Bhattacharya S, Giovannucci DR, Sanchez ER, Fischer G, Wang X. FKBP38 peptidylprolyl isomerase promotes the folding of cystic fibrosis transmembrane conductance regulator in the endoplasmic reticulum. The Journal of Biological Chemistry. 286: 43071-80. PMID 22030396 DOI: 10.1074/Jbc.M111.269993 |
0.303 |
|
| 2011 |
Hinds TD, Stechschulte LA, Cash HA, Whisler D, Banerjee A, Yong W, Khuder SS, Kaw MK, Shou W, Najjar SM, Sanchez ER. Protein phosphatase 5 mediates lipid metabolism through reciprocal control of glucocorticoid receptor and peroxisome proliferator-activated receptor-γ (PPARγ). The Journal of Biological Chemistry. 286: 42911-22. PMID 21994940 DOI: 10.1074/Jbc.M111.311662 |
0.398 |
|
| 2011 |
Stechschulte LA, Sanchez ER. FKBP51-a selective modulator of glucocorticoid and androgen sensitivity. Current Opinion in Pharmacology. 11: 332-7. PMID 21565552 DOI: 10.1016/j.coph.2011.04.012 |
0.37 |
|
| 2010 |
Chen H, Yong W, Hinds TD, Yang Z, Zhou Y, Sanchez ER, Shou W. Fkbp52 regulates androgen receptor transactivation activity and male urethra morphogenesis. The Journal of Biological Chemistry. 285: 27776-84. PMID 20605780 DOI: 10.1074/Jbc.M110.156091 |
0.334 |
|
| 2010 |
Periyasamy S, Hinds T, Shemshedini L, Shou W, Sanchez ER. FKBP51 and Cyp40 are positive regulators of androgen-dependent prostate cancer cell growth and the targets of FK506 and cyclosporin A. Oncogene. 29: 1691-701. PMID 20023700 DOI: 10.1038/Onc.2009.458 |
0.313 |
|
| 2009 |
Wolf IM, Periyasamy S, Hinds T, Yong W, Shou W, Sanchez ER. Targeted ablation reveals a novel role of FKBP52 in gene-specific regulation of glucocorticoid receptor transcriptional activity. The Journal of Steroid Biochemistry and Molecular Biology. 113: 36-45. PMID 19073255 DOI: 10.1016/j.jsbmb.2008.11.006 |
0.472 |
|
| 2008 |
Hinds TD, Sánchez ER. Protein phosphatase 5. The International Journal of Biochemistry & Cell Biology. 40: 2358-62. PMID 17951098 DOI: 10.1016/j.biocel.2007.08.010 |
0.451 |
|
| 2007 |
Heitzer MD, Wolf IM, Sanchez ER, Witchel SF, DeFranco DB. Glucocorticoid receptor physiology. Reviews in Endocrine & Metabolic Disorders. 8: 321-30. PMID 18049904 DOI: 10.1007/S11154-007-9059-8 |
0.393 |
|
| 2007 |
Yong W, Yang Z, Periyasamy S, Chen H, Yucel S, Li W, Lin LY, Wolf IM, Cohn MJ, Baskin LS, Sánchez ER, Shou W. Essential role for Co-chaperone Fkbp52 but not Fkbp51 in androgen receptor-mediated signaling and physiology. The Journal of Biological Chemistry. 282: 5026-36. PMID 17142810 DOI: 10.1074/Jbc.M609360200 |
0.342 |
|
| 2006 |
Yang Z, Wolf IM, Chen H, Periyasamy S, Chen Z, Yong W, Shi S, Zhao W, Xu J, Srivastava A, Sánchez ER, Shou W. FK506-binding protein 52 is essential to uterine reproductive physiology controlled by the progesterone receptor A isoform. Molecular Endocrinology (Baltimore, Md.). 20: 2682-94. PMID 16873445 DOI: 10.1210/Me.2006-0024 |
0.494 |
|
| 2005 |
Li D, Sánchez ER. Glucocorticoid receptor and heat shock factor 1: novel mechanism of reciprocal regulation. Vitamins and Hormones. 71: 239-62. PMID 16112270 DOI: 10.1016/S0083-6729(05)71008-6 |
0.657 |
|
| 2005 |
Davies TH, Ning YM, Sánchez ER. Differential control of glucocorticoid receptor hormone-binding function by tetratricopeptide repeat (TPR) proteins and the immunosuppressive ligand FK506. Biochemistry. 44: 2030-8. PMID 15697228 DOI: 10.1021/bi048503v |
0.383 |
|
| 2004 |
Jones TJ, Li D, Wolf IM, Wadekar SA, Periyasamy S, Sánchez ER. Enhancement of glucocorticoid receptor-mediated gene expression by constitutively active heat shock factor 1. Molecular Endocrinology (Baltimore, Md.). 18: 509-20. PMID 14673135 DOI: 10.1210/Me.2003-0366 |
0.67 |
|
| 2004 |
Wadekar SA, Li D, Sánchez ER. Agonist-activated glucocorticoid receptor inhibits binding of heat shock factor 1 to the heat shock protein 70 promoter in vivo. Molecular Endocrinology (Baltimore, Md.). 18: 500-8. PMID 14673132 DOI: 10.1210/Me.2003-0215 |
0.693 |
|
| 2002 |
Periyasamy S, Sánchez ER. Antagonism of glucocorticoid receptor transactivity and cell growth inhibition by transforming growth factor-beta through AP-1-mediated transcriptional repression. The International Journal of Biochemistry & Cell Biology. 34: 1571-85. PMID 12379279 DOI: 10.1016/S1357-2725(02)00057-2 |
0.354 |
|
| 2002 |
Li Calzi S, Periyasamy S, Li DP, Sánchez ER. Vanadate increases glucocorticoid receptor-mediated gene expression: a novel mechanism for potentiation of a steroid receptor. The Journal of Steroid Biochemistry and Molecular Biology. 80: 35-47. PMID 11867262 DOI: 10.1016/S0960-0760(01)00180-7 |
0.732 |
|
| 2002 |
Davies TH, Ning YM, Sánchez ER. A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins. The Journal of Biological Chemistry. 277: 4597-600. PMID 11751894 DOI: 10.1074/Jbc.C100531200 |
0.478 |
|
| 2001 |
Wadekar SA, Li D, Periyasamy S, Sánchez ER. Inhibition of heat shock transcription factor by GR. Molecular Endocrinology (Baltimore, Md.). 15: 1396-410. PMID 11463862 DOI: 10.1210/Mend.15.8.0674 |
0.686 |
|
| 2000 |
Li DP, Periyasamy S, Jones TJ, Sánchez ER. Heat and chemical shock potentiation of glucocorticoid receptor transactivation requires heat shock factor (HSF) activity. Modulation of HSF by vanadate and wortmannin. The Journal of Biological Chemistry. 275: 26058-65. PMID 10862623 DOI: 10.1074/Jbc.M004502200 |
0.67 |
|
| 2000 |
Morishima Y, Murphy PJ, Li DP, Sanchez ER, Pratt WB. Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket. The Journal of Biological Chemistry. 275: 18054-60. PMID 10764743 DOI: 10.1074/Jbc.M000434200 |
0.425 |
|
| 1999 |
Li DP, Li Calzi S, Sánchez ER. Inhibition of heat shock factor activity prevents heat shock potentiation of glucocorticoid receptor-mediated gene expression. Cell Stress & Chaperones. 4: 223-34. PMID 10590836 DOI: 10.1379/1466-1268(1999)004<0223:Iohsfa>2.3.Co;2 |
0.695 |
|
| 1996 |
Hu JL, Guan XJ, Sánchez ER. Enhancement of glucocorticoid receptor-mediated gene expression by cellular stress: evidence for the involvement of a heat shock-initiated factor or process during recovery from stress. Cell Stress & Chaperones. 1: 197-205. PMID 9222605 DOI: 10.1379/1466-1268(1996)001<0197:EOGRMG>2.3.CO;2 |
0.568 |
|
| 1996 |
Ning YM, Sánchez ER. In vivo evidence for the generation of a glucocorticoid receptor-heat shock protein-90 complex incapable of binding hormone by the calmodulin antagonist phenoxybenzamine. Molecular Endocrinology (Baltimore, Md.). 10: 14-23. PMID 8838141 DOI: 10.1210/Mend.10.1.8838141 |
0.629 |
|
| 1996 |
Sánchez ER, Ning Y. Immunophilins, Heat Shock Proteins, and Glucocorticoid Receptor Actionsin Vivo Methods. 9: 188-200. PMID 8812667 DOI: 10.1006/Meth.1996.0025 |
0.611 |
|
| 1995 |
Ning YM, Sánchez ER. Evidence for a functional interaction between calmodulin and the glucocorticoid receptor. Biochemical and Biophysical Research Communications. 208: 48-54. PMID 7887964 DOI: 10.1006/bbrc.1995.1303 |
0.367 |
|
| 1995 |
Renoir JM, Mercier-Bodard C, Hoffmann K, Le Bihan S, Ning YM, Sanchez ER, Handschumacher RE, Baulieu EE. Cyclosporin A potentiates the dexamethasone-induced mouse mammary tumor virus-chloramphenicol acetyltransferase activity in LMCAT cells: A possible role for different heat shock protein-binding immunophilins in glucocorticosteroid receptor-mediated gene expression Proceedings of the National Academy of Sciences of the United States of America. 92: 4977-4981. PMID 7539138 DOI: 10.1073/pnas.92.11.4977 |
0.586 |
|
| 1995 |
Ning YM, Sanchez ER. Stabilization in vitro of the untransformed glucocorticoid receptor complex of S49 lymphocytes by the immunophilin ligand FK506. The Journal of Steroid Biochemistry and Molecular Biology. 52: 187-94. PMID 7532989 DOI: 10.1016/0960-0760(94)00162-F |
0.531 |
|
| 1994 |
Sanchez ER, Hu JL, Zhong S, Shen P, Greene MJ, Housley PR. Potentiation of glucocorticoid receptor-mediated gene expression by heat and chemical shock. Molecular Endocrinology (Baltimore, Md.). 8: 408-21. PMID 8052262 DOI: 10.1210/Mend.8.4.8052262 |
0.672 |
|
| 1993 |
Shen P, Xie ZJ, Li H, Sánchez ER. Glucocorticoid receptor conversion to high affinity nuclear binding and transcription enhancement activity in Chinese hamster ovary cells subjected to heat and chemical stress. The Journal of Steroid Biochemistry and Molecular Biology. 47: 55-64. PMID 8274442 DOI: 10.1016/0960-0760(93)90057-4 |
0.698 |
|
| 1993 |
Hutchison KA, Scherrer LC, Czar MJ, Ning Y, Sanchez ER, Leach KL, Deibel MR, Pratt WB. FK506 binding to the 56-kilodalton immunophilin (Hsp56) in the glucocorticoid receptor heterocomplex has no effect on receptor folding or function. Biochemistry. 32: 3953-7. PMID 7682438 DOI: 10.1021/Bi00066A015 |
0.437 |
|
| 1992 |
Scherrer LC, Hutchison KA, Sanchez ER, Randall SK, Pratt WB. A heat shock protein complex isolated from rabbit reticulocyte lysate can reconstitute a functional glucocorticoid receptor-Hsp90 complex. Biochemistry. 31: 7325-9. PMID 1510923 DOI: 10.1021/Bi00147A017 |
0.414 |
|
| 1992 |
Sanchez ER. Heat shock induces translocation to the nucleus of the unliganded glucocorticoid receptor. Journal of Biological Chemistry. 267: 17-20. DOI: 10.1016/S0021-9258(18)48448-7 |
0.509 |
|
| 1990 |
Sanchez ER, Faber LE, Henzel WJ, Pratt WB. The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins. Biochemistry. 29: 5145-52. PMID 2378870 DOI: 10.1021/Bi00473A021 |
0.385 |
|
| 1990 |
Meshinchi S, Sanchez ER, Martell KJ, Pratt WB. Elimination and reconstitution of the requirement for hormone in promoting temperature-dependent transformation of cytosolic glucocorticoid receptors to the DNA-binding state. Journal of Biological Chemistry. 265: 4863-4870. DOI: 10.1016/s0021-9258(19)34054-2 |
0.301 |
|
| 1990 |
Sanchez ER. Hsp56: a novel heat shock protein associated with untransformed steroid receptor complexes. Journal of Biological Chemistry. 265: 22067-22070. DOI: 10.1016/s0021-9258(18)45667-0 |
0.506 |
|
| 1989 |
Bresnick EH, Dalman FC, Sanchez ER, Pratt WB. Evidence That the 90-kDa Heat Shock Protein Is Necessary for the Steroid Binding Conformation of the L Cell Glucocorticoid Receptor Journal of Biological Chemistry. 264: 4992-4997. DOI: 10.1016/s0021-9258(18)83689-4 |
0.499 |
|
| 1988 |
Bresnick EH, Sanchez ER, Harrison RW, Pratt WB. Hydrogen peroxide stabilizes the steroid-binding state of rat liver glucocorticoid receptors by promoting disulfide bond formation. Biochemistry. 27: 2866-72. PMID 3401453 DOI: 10.1021/Bi00408A030 |
0.301 |
|
| 1988 |
Bresnick EH, Sanchez ER, Pratt WB. Relationship between glucocorticoid receptor steroid-binding capacity and association of the Mr 90,000 heat shock protein with the unliganded receptor. Journal of Steroid Biochemistry. 30: 267-9. PMID 3386251 DOI: 10.1016/0022-4731(88)90104-5 |
0.495 |
|
| 1988 |
Sanchez ER, Redmond T, Scherrer LC, Bresnick EH, Welsh MJ, Pratt WB. Evidence that the 90-kilodalton heat shock protein is associated with tubulin-containing complexes in L cell cytosol and in intact PtK cells. Molecular Endocrinology (Baltimore, Md.). 2: 756-60. PMID 3062385 DOI: 10.1210/Mend-2-8-756 |
0.303 |
|
| 1988 |
Meshinchi S, Grippo JF, Sanchez ER, Bresnick EH, Pratt WB. Evidence that the endogenous heat-stable glucocorticoid receptor stabilizing factor is a metal component of the untransformed receptor complex. Journal of Biological Chemistry. 263: 16809-16817. DOI: 10.1016/s0021-9258(18)37463-5 |
0.337 |
|
| 1987 |
Sanchez ER, Tienrungroj W, Dalman FC, Lin AL. Glucocorticoid receptor phosphorylation in mouse L-cells. Journal of Steroid Biochemistry. 27: 215-25. PMID 3320532 DOI: 10.1016/0022-4731(87)90313-X |
0.391 |
|
| 1987 |
Sanchez ER, Meshinchi S, Schlesinger MJ, Pratt WB. Demonstration that the 90-kilodalton heat shock protein is bound to the glucocorticoid receptor in its 9S nondeoxynucleic acid binding form. Molecular Endocrinology (Baltimore, Md.). 1: 908-12. PMID 3153469 DOI: 10.1210/Mend-1-12-908 |
0.421 |
|
| 1987 |
Sanchez ER, Meshinchi S, Tienrungroj W, Schlesinger MJ, Toft DO, Pratt WB. Relationship of the 90-kDa murine heat shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor. Journal of Biological Chemistry. 262: 6986-6991. DOI: 10.1016/s0021-9258(18)48191-4 |
0.429 |
|
| 1986 |
Sanchez ER, Housley PR, Pratt WB. The molybdate-stabilized glucocorticoid binding complex of L-cells contains a 98-100 kdalton steroid binding phosphoprotein and a 90 kdalton nonsteroid-binding phosphoprotein that is part of the murine heat-shock complex. Journal of Steroid Biochemistry. 24: 9-18. PMID 3517499 DOI: 10.1016/0022-4731(86)90025-7 |
0.43 |
|
| 1985 |
Sanchez ER, Toft DO, Schlesinger MJ, Pratt WB. Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. Journal of Biological Chemistry. 260: 12398-12401. DOI: 10.1016/s0021-9258(17)38886-5 |
0.466 |
|
| Show low-probability matches. |