| Year |
Citation |
Score |
| 2022 |
Morishima Y, Lau M, Pratt WB, Osawa Y. Dynamic cycling with a unique Hsp90/Hsp70-dependent chaperone machinery and GAPDH is needed for heme insertion and activation of neuronal NO synthase. The Journal of Biological Chemistry. 102856. PMID 36596358 DOI: 10.1016/j.jbc.2022.102856 |
0.54 |
|
| 2020 |
Mehta RK, Pal S, Kondapi K, Sitto M, Dewar C, Devasia T, Schipper MJ, Thomas DG, Basrur V, Pai MP, Morishima Y, Osawa Y, Pratt WB, Lawrence TS, Nyati MK. Low dose Hsp90 inhibitor selectively radiosensitizes HNSCC and Pancreatic xenografts. Clinical Cancer Research : An Official Journal of the American Association For Cancer Research. PMID 32718999 DOI: 10.1158/1078-0432.Ccr-19-3102 |
0.415 |
|
| 2019 |
Davis AK, Pratt WB, Lieberman AP, Osawa Y. Targeting Hsp70 facilitated protein quality control for treatment of polyglutamine diseases. Cellular and Molecular Life Sciences : Cmls. PMID 31552448 DOI: 10.1007/S00018-019-03302-2 |
0.515 |
|
| 2018 |
Morishima Y, Mehta RK, Yoshimura M, Lau M, Southworth DR, Lawrence TS, Pratt WB, Nyati MK, Osawa Y. Chaperone Activity and Dimerization Properties of Hsp90α and Hsp90β in Glucocorticoid Receptor Activation by the Multiprotein Hsp90/Hsp70-Dependent Chaperone Machinery. Molecular Pharmacology. PMID 29941666 DOI: 10.1124/Mol.118.112516 |
0.547 |
|
| 2016 |
Elaimy AL, Ahsan A, Marsh K, Pratt WB, Ray D, Lawrence TS, Nyati MK. ATM is the primary kinase responsible for phosphorylation of Hsp90α after ionizing radiation. Oncotarget. PMID 27738310 DOI: 10.18632/Oncotarget.12557 |
0.355 |
|
| 2015 |
Pratt WB, Gestwicki JE, Osawa Y, Lieberman AP. Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases. Annual Review of Pharmacology and Toxicology. 55: 353-71. PMID 25292434 DOI: 10.1146/Annurev-Pharmtox-010814-124332 |
0.512 |
|
| 2014 |
Pratt WB, Morishima Y, Gestwicki JE, Lieberman AP, Osawa Y. A model in which heat shock protein 90 targets protein-folding clefts: rationale for a new approach to neuroprotective treatment of protein folding diseases. Experimental Biology and Medicine (Maywood, N.J.). 239: 1405-13. PMID 24990484 DOI: 10.1177/1535370214539444 |
0.508 |
|
| 2014 |
Ahsan A, Ramanand SG, Bergin IL, Zhao L, Whitehead CE, Rehemtulla A, Ray D, Pratt WB, Lawrence TS, Nyati MK. Efficacy of an EGFR-specific peptide against EGFR-dependent cancer cell lines and tumor xenografts. Neoplasia (New York, N.Y.). 16: 105-14. PMID 24709418 DOI: 10.1593/Neo.14182 |
0.391 |
|
| 2013 |
Ahsan A, Ray D, Ramanand SG, Hegde A, Whitehead C, Rehemtulla A, Morishima Y, Pratt WB, Osawa Y, Lawrence TS, Nyati MK. Destabilization of the epidermal growth factor receptor (EGFR) by a peptide that inhibits EGFR binding to heat shock protein 90 and receptor dimerization. The Journal of Biological Chemistry. 288: 26879-86. PMID 23897823 DOI: 10.1074/Jbc.M113.492280 |
0.457 |
|
| 2013 |
Wang AM, Miyata Y, Klinedinst S, Peng HM, Chua JP, Komiyama T, Li X, Morishima Y, Merry DE, Pratt WB, Osawa Y, Collins CA, Gestwicki JE, Lieberman AP. Activation of Hsp70 reduces neurotoxicity by promoting polyglutamine protein degradation. Nature Chemical Biology. 9: 112-8. PMID 23222885 DOI: 10.1038/Nchembio.1140 |
0.593 |
|
| 2012 |
Ahsan A, Ramanand SG, Whitehead C, Hiniker SM, Rehemtulla A, Pratt WB, Jolly S, Gouveia C, Truong K, Van Waes C, Ray D, Lawrence TS, Nyati MK. Wild-type EGFR is stabilized by direct interaction with HSP90 in cancer cells and tumors. Neoplasia (New York, N.Y.). 14: 670-7. PMID 22952420 DOI: 10.1593/Neo.12986 |
0.409 |
|
| 2012 |
Peng HM, Morishima Y, Pratt WB, Osawa Y. Modulation of heme/substrate binding cleft of neuronal nitric-oxide synthase (nNOS) regulates binding of Hsp90 and Hsp70 proteins and nNOS ubiquitination. The Journal of Biological Chemistry. 287: 1556-65. PMID 22128174 DOI: 10.1074/Jbc.M111.323295 |
0.585 |
|
| 2011 |
Morishima Y, Lau M, Peng HM, Miyata Y, Gestwicki JE, Pratt WB, Osawa Y. Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleft. Biochemistry. 50: 7146-56. PMID 21755988 DOI: 10.1021/Bi200751T |
0.459 |
|
| 2011 |
Lieberman AP, Pratt WB. Regulation of the Polyglutamine Androgen Receptor by the Hsp90/Hsp70-Based Chaperone Machinery Protein Chaperones and Protection From Neurodegenerative Diseases. 211-233. DOI: 10.1002/9781118063903.ch6 |
0.513 |
|
| 2010 |
Clapp KM, Peng HM, Morishima Y, Lau M, Walker VJ, Pratt WB, Osawa Y. C331A mutant of neuronal nitric-oxide synthase is labilized for Hsp70/CHIP (C terminus of HSC70-interacting protein)-dependent ubiquitination. The Journal of Biological Chemistry. 285: 33642-51. PMID 20729196 DOI: 10.1074/Jbc.M110.159178 |
0.428 |
|
| 2010 |
Pratt WB, Morishima Y, Peng HM, Osawa Y. Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage. Experimental Biology and Medicine (Maywood, N.J.). 235: 278-89. PMID 20404045 DOI: 10.1258/Ebm.2009.009250 |
0.579 |
|
| 2010 |
Wang AM, Morishima Y, Clapp KM, Peng HM, Pratt WB, Gestwicki JE, Osawa Y, Lieberman AP. Inhibition of hsp70 by methylene blue affects signaling protein function and ubiquitination and modulates polyglutamine protein degradation. The Journal of Biological Chemistry. 285: 15714-23. PMID 20348093 DOI: 10.1074/Jbc.M109.098806 |
0.643 |
|
| 2009 |
Peng HM, Morishima Y, Clapp KM, Lau M, Pratt WB, Osawa Y. Dynamic cycling with Hsp90 stabilizes neuronal nitric oxide synthase through calmodulin-dependent inhibition of ubiquitination. Biochemistry. 48: 8483-90. PMID 19642705 DOI: 10.1021/Bi901058G |
0.561 |
|
| 2008 |
Morishima Y, Wang AM, Yu Z, Pratt WB, Osawa Y, Lieberman AP. CHIP deletion reveals functional redundancy of E3 ligases in promoting degradation of both signaling proteins and expanded glutamine proteins. Human Molecular Genetics. 17: 3942-52. PMID 18784277 DOI: 10.1093/Hmg/Ddn296 |
0.557 |
|
| 2008 |
Pratt WB, Morishima Y, Osawa Y. The Hsp90 chaperone machinery regulates signaling by modulating ligand binding clefts. The Journal of Biological Chemistry. 283: 22885-9. PMID 18515355 DOI: 10.1074/Jbc.R800023200 |
0.622 |
|
| 2006 |
Thomas M, Harrell JM, Morishima Y, Peng HM, Pratt WB, Lieberman AP. Pharmacologic and genetic inhibition of hsp90-dependent trafficking reduces aggregation and promotes degradation of the expanded glutamine androgen receptor without stress protein induction. Human Molecular Genetics. 15: 1876-83. PMID 16644868 DOI: 10.1093/Hmg/Ddl110 |
0.83 |
|
| 2006 |
Pratt WB, Morishima Y, Murphy M, Harrell M. Chaperoning of glucocorticoid receptors. Handbook of Experimental Pharmacology. 111-38. PMID 16610357 DOI: 10.1007/3-540-29717-0-5 |
0.609 |
|
| 2005 |
Morishima Y, Peng HM, Lin HL, Hollenberg PF, Sunahara RK, Osawa Y, Pratt WB. Regulation of cytochrome P450 2E1 by heat shock protein 90-dependent stabilization and CHIP-dependent proteasomal degradation. Biochemistry. 44: 16333-40. PMID 16331994 DOI: 10.1021/Bi0515570 |
0.492 |
|
| 2005 |
Murphy PJ, Morishima Y, Kovacs JJ, Yao TP, Pratt WB. Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation/deacetylation of the chaperone. The Journal of Biological Chemistry. 280: 33792-9. PMID 16087666 DOI: 10.1074/Jbc.M506997200 |
0.616 |
|
| 2005 |
Kovacs JJ, Murphy PJ, Gaillard S, Zhao X, Wu JT, Nicchitta CV, Yoshida M, Toft DO, Pratt WB, Yao TP. HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Molecular Cell. 18: 601-7. PMID 15916966 DOI: 10.1016/J.Molcel.2005.04.021 |
0.629 |
|
| 2004 |
Galigniana MD, Morishima Y, Gallay PA, Pratt WB. Cyclophilin-A is bound through its peptidylprolyl isomerase domain to the cytoplasmic dynein motor protein complex. The Journal of Biological Chemistry. 279: 55754-9. PMID 15496417 DOI: 10.1074/Jbc.M406259200 |
0.507 |
|
| 2004 |
Harrell JM, Murphy PJ, Morishima Y, Chen H, Mansfield JF, Galigniana MD, Pratt WB. Evidence for glucocorticoid receptor transport on microtubules by dynein. The Journal of Biological Chemistry. 279: 54647-54. PMID 15485845 DOI: 10.1074/Jbc.M406863200 |
0.799 |
|
| 2004 |
Peng HM, Morishima Y, Jenkins GJ, Dunbar AY, Lau M, Patterson C, Pratt WB, Osawa Y. Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase. The Journal of Biological Chemistry. 279: 52970-7. PMID 15466472 DOI: 10.1074/Jbc.M406926200 |
0.35 |
|
| 2004 |
Pratt WB, Galigniana MD, Morishima Y, Murphy PJ. Role of molecular chaperones in steroid receptor action. Essays in Biochemistry. 40: 41-58. PMID 15242338 DOI: 10.1042/Bse0400041 |
0.642 |
|
| 2004 |
Pratt WB, Galigniana MD, Harrell JM, DeFranco DB. Role of hsp90 and the hsp90-binding immunophilins in signalling protein movement. Cellular Signalling. 16: 857-72. PMID 15157665 DOI: 10.1016/J.Cellsig.2004.02.004 |
0.851 |
|
| 2004 |
Billecke SS, Draganov DI, Morishima Y, Murphy PJ, Dunbar AY, Pratt WB, Osawa Y. The role of hsp90 in heme-dependent activation of apo-neuronal nitric-oxide synthase. The Journal of Biological Chemistry. 279: 30252-8. PMID 15155759 DOI: 10.1074/Jbc.M403864200 |
0.524 |
|
| 2004 |
Gerges NZ, Tran IC, Backos DS, Harrell JM, Chinkers M, Pratt WB, Esteban JA. Independent functions of hsp90 in neurotransmitter release and in the continuous synaptic cycling of AMPA receptors. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 24: 4758-66. PMID 15152036 DOI: 10.1523/Jneurosci.0594-04.2004 |
0.793 |
|
| 2004 |
Murphy PJ, Galigniana MD, Morishima Y, Harrell JM, Kwok RP, Ljungman M, Pratt WB. Pifithrin-alpha inhibits p53 signaling after interaction of the tumor suppressor protein with hsp90 and its nuclear translocation. The Journal of Biological Chemistry. 279: 30195-201. PMID 15145929 DOI: 10.1074/Jbc.M403539200 |
0.806 |
|
| 2004 |
Galigniana MD, Harrell JM, Housley PR, Patterson C, Fisher SK, Pratt WB. Retrograde transport of the glucocorticoid receptor in neurites requires dynamic assembly of complexes with the protein chaperone hsp90 and is linked to the CHIP component of the machinery for proteasomal degradation. Brain Research. Molecular Brain Research. 123: 27-36. PMID 15046863 DOI: 10.1016/J.Molbrainres.2003.12.015 |
0.812 |
|
| 2004 |
Galigniana MD, Harrell JM, O'Hagen HM, Ljungman M, Pratt WB. Hsp90-binding immunophilins link p53 to dynein during p53 transport to the nucleus. The Journal of Biological Chemistry. 279: 22483-9. PMID 15004035 DOI: 10.1074/Jbc.M402223200 |
0.813 |
|
| 2004 |
Thomas M, Dadgar N, Aphale A, Harrell JM, Kunkel R, Pratt WB, Lieberman AP. Androgen receptor acetylation site mutations cause trafficking defects, misfolding, and aggregation similar to expanded glutamine tracts. The Journal of Biological Chemistry. 279: 8389-95. PMID 14670946 DOI: 10.1074/Jbc.M311761200 |
0.817 |
|
| 2003 |
Kanelakis KC, Pratt WB. Regulation of glucocorticoid receptor ligand-binding activity by the hsp90/hsp70-based chaperone machinery. Methods in Enzymology. 364: 159-73. PMID 14631845 DOI: 10.1016/S0076-6879(03)64010-3 |
0.843 |
|
| 2003 |
Morishima Y, Kanelakis KC, Murphy PJ, Lowe ER, Jenkins GJ, Osawa Y, Sunahara RK, Pratt WB. 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. The Journal of Biological Chemistry. 278: 48754-63. PMID 14507910 DOI: 10.1074/Jbc.M309814200 |
0.851 |
|
| 2003 |
Murphy PJ, Morishima Y, Chen H, Galigniana MD, Mansfield JF, Simons SS, Pratt WB. Visualization and mechanism of assembly of a glucocorticoid receptor.Hsp70 complex that is primed for subsequent Hsp90-dependent opening of the steroid binding cleft. The Journal of Biological Chemistry. 278: 34764-73. PMID 12807878 DOI: 10.1074/Jbc.M304469200 |
0.662 |
|
| 2003 |
Pratt WB, Toft DO. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Experimental Biology and Medicine (Maywood, N.J.). 228: 111-33. PMID 12563018 DOI: 10.1177/153537020322800201 |
0.666 |
|
| 2002 |
Galigniana MD, Harrell JM, Murphy PJ, Chinkers M, Radanyi C, Renoir JM, Zhang M, Pratt WB. Binding of hsp90-associated immunophilins to cytoplasmic dynein: direct binding and in vivo evidence that the peptidylprolyl isomerase domain is a dynein interaction domain. Biochemistry. 41: 13602-10. PMID 12427021 DOI: 10.1021/Bi020399Z |
0.812 |
|
| 2002 |
Kaul S, Murphy PJ, Chen J, Brown L, Pratt WB, Simons SS. Mutations at positions 547-553 of rat glucocorticoid receptors reveal that hsp90 binding requires the presence, but not defined composition, of a seven-amino acid sequence at the amino terminus of the ligand binding domain. The Journal of Biological Chemistry. 277: 36223-32. PMID 12145311 DOI: 10.1074/Jbc.M206748200 |
0.526 |
|
| 2002 |
Kanelakis KC, Shewach DS, Pratt WB. Nucleotide binding states of hsp70 and hsp90 during sequential steps in the process of glucocorticoid receptor.hsp90 heterocomplex assembly. The Journal of Biological Chemistry. 277: 33698-703. PMID 12093808 DOI: 10.1074/Jbc.M204164200 |
0.831 |
|
| 2002 |
Harrell JM, Kurek I, Breiman A, Radanyi C, Renoir JM, Pratt WB, Galigniana MD. All of the protein interactions that link steroid receptor.hsp90.immunophilin heterocomplexes to cytoplasmic dynein are common to plant and animal cells. Biochemistry. 41: 5581-7. PMID 11969419 DOI: 10.1021/Bi020073Q |
0.848 |
|
| 2002 |
Billecke SS, Bender AT, Kanelakis KC, Murphy PJ, Lowe ER, Kamada Y, Pratt WB, Osawa Y. hsp90 is required for heme binding and activation of apo-neuronal nitric-oxide synthase: geldanamycin-mediated oxidant generation is unrelated to any action of hsp90. The Journal of Biological Chemistry. 277: 20504-9. PMID 11923316 DOI: 10.1074/Jbc.M201940200 |
0.793 |
|
| 2001 |
Guo Y, Guettouche T, Fenna M, Boellmann F, Pratt WB, Toft DO, Smith DF, Voellmy R. Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. The Journal of Biological Chemistry. 276: 45791-9. PMID 11583998 DOI: 10.1074/Jbc.M105931200 |
0.373 |
|
| 2001 |
Murphy PJ, Kanelakis KC, Galigniana MD, Morishima Y, Pratt WB. Stoichiometry, abundance, and functional significance of the hsp90/hsp70-based multiprotein chaperone machinery in reticulocyte lysate. The Journal of Biological Chemistry. 276: 30092-8. PMID 11404358 DOI: 10.1074/Jbc.M103773200 |
0.838 |
|
| 2001 |
Galigniana MD, Radanyi C, Renoir JM, Housley PR, Pratt WB. Evidence that the Peptidylprolyl Isomerase Domain of the hsp90-binding Immunophilin FKBP52 is Involved in Both Dynein Interaction and Glucocorticoid Receptor Movement to the Nucleus Journal of Biological Chemistry. 276: 14884-14889. PMID 11278753 DOI: 10.1074/Jbc.M010809200 |
0.507 |
|
| 2001 |
Pratt WB, Krishna P, Olsen LJ. Hsp90-binding immunophilins in plants: The protein movers Trends in Plant Science. 6: 54-58. PMID 11173288 DOI: 10.1016/S1360-1385(00)01843-4 |
0.549 |
|
| 2001 |
Morishima Y, Kanelakis KC, Murphy PJ, Shewach DS, Pratt WB. Evidence for iterative ratcheting of receptor-bound hsp70 between its ATP and ADP conformations during assembly of glucocorticoid receptor.hsp90 heterocomplexes. Biochemistry. 40: 1109-16. PMID 11170435 DOI: 10.1021/Bi002399+ |
0.83 |
|
| 2000 |
Kanelakis KC, Murphy PJ, Galigniana MD, Morishima Y, Takayama S, Reed JC, Toft DO, Pratt WB. 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: 14314-21. PMID 11087380 DOI: 10.1021/Bi001671C |
0.82 |
|
| 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 |
0.651 |
|
| 2000 |
Morishima Y, Kanelakis KC, Silverstein AM, Dittmar KD, Estrada L, Pratt WB. The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system. The Journal of Biological Chemistry. 275: 6894-900. PMID 10702249 DOI: 10.1074/Jbc.275.10.6894 |
0.844 |
|
| 1999 |
Pratt WB, Silverstein AM, Galigniana MD. A model for the cytoplasmic trafficking of signalling proteins involving the hsp90-binding immunophilins and p50(cdc37) Cellular Signalling. 11: 839-851. PMID 10659992 DOI: 10.1016/S0898-6568(99)00064-9 |
0.59 |
|
| 1999 |
Silverstein AM, Galigniana MD, Kanelakis KC, Radanyi C, Renoir JM, Pratt WB. Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein. The Journal of Biological Chemistry. 274: 36980-6. PMID 10601253 DOI: 10.1074/Jbc.274.52.36980 |
0.836 |
|
| 1999 |
Giannoukos G, Silverstein AM, Pratt WB, Simons SS. The seven amino acids (547-553) of rat glucocorticoid receptor required for steroid and Hsp90 binding contain a functionally independent LXXLL motif that is critical for steroid binding Journal of Biological Chemistry. 274: 36527-36536. PMID 10593951 DOI: 10.1074/Jbc.274.51.36527 |
0.524 |
|
| 1999 |
Kanelakis KC, Morishima Y, Dittmar KD, Galigniana MD, Takayama S, Reed JC, Pratt WB. Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery. The Journal of Biological Chemistry. 274: 34134-40. PMID 10567384 DOI: 10.1074/Jbc.274.48.34134 |
0.844 |
|
| 1999 |
Galigniana MD, Housley PR, DeFranco DB, Pratt WB. Inhibition of glucocorticoid receptor nucleocytoplasmic shuttling by okadaic acid requires intact cytoskeleton Journal of Biological Chemistry. 274: 16222-16227. PMID 10347177 DOI: 10.1074/Jbc.274.23.16222 |
0.515 |
|
| 1999 |
Bender AT, Silverstein AM, Demady DR, Kanelakis KC, Noguchi S, Pratt WB, Osawa Y. Neuronal nitric-oxide synthase is regulated by the Hsp90-based chaperone system in vivo. The Journal of Biological Chemistry. 274: 1472-8. PMID 9880522 DOI: 10.1074/Jbc.274.3.1472 |
0.821 |
|
| 1998 |
Pratt WB, Dittmar KD. Studies with Purified Chaperones Advance the Understanding of the Mechanism of Glucocorticoid Receptor-hsp90 Heterocomplex Assembly. Trends in Endocrinology and Metabolism: Tem. 9: 244-52. PMID 18406276 DOI: 10.1016/S1043-2760(98)00059-9 |
0.657 |
|
| 1998 |
Galigniana MD, Scruggs JL, Herrington J, Welsh MJ, Carter-Su C, Housley PR, Pratt WB. Heat shock protein 90-dependent (geldanamycin-inhibited) movement of the glucocorticoid receptor through the cytoplasm to the nucleus requires intact cytoskeleton. Molecular Endocrinology (Baltimore, Md.). 12: 1903-13. PMID 9849964 DOI: 10.1210/Mend.12.12.0204 |
0.58 |
|
| 1998 |
Caamaño CA, Morano MI, Dalman FC, Pratt WB, Akil H. A conserved proline in the hsp90 binding region of the glucocorticoid receptor is required for hsp90 heterocomplex stabilization and receptor signaling. The Journal of Biological Chemistry. 273: 20473-80. PMID 9685402 DOI: 10.1074/Jbc.273.32.20473 |
0.62 |
|
| 1998 |
Silverstein AM, Grammatikakis N, Cochran BH, Chinkers M, Pratt WB. p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site. The Journal of Biological Chemistry. 273: 20090-5. PMID 9685350 DOI: 10.1074/Jbc.273.32.20090 |
0.58 |
|
| 1998 |
Xu M, Dittmar KD, Giannoukos G, Pratt WB, Simons SS. Binding of hsp90 to the glucocorticoid receptor requires a specific 7- amino acid sequence at the amino terminus of the hormone-binding domain Journal of Biological Chemistry. 273: 13918-13924. PMID 9593740 DOI: 10.1074/Jbc.273.22.13918 |
0.616 |
|
| 1998 |
Pratt WB. The hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors Proceedings of the Society For Experimental Biology and Medicine. 217: 420-434. PMID 9521088 DOI: 10.3181/00379727-217-44252 |
0.651 |
|
| 1998 |
Dittmar KD, Banach M, Galigniana MD, Pratt WB. The role of DnaJ-like proteins in glucocorticoid receptor·hsp90 Heterocomplex assembly by the reconstituted hsp90·p60·hsp70 Foldosome complex Journal of Biological Chemistry. 273: 7358-7366. PMID 9516432 DOI: 10.1074/Jbc.273.13.7358 |
0.631 |
|
| 1997 |
Dittmar KD, Demady DR, Stancato LF, Krishna P, Pratt WB. 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 Journal of Biological Chemistry. 272: 21213-21220. PMID 9261129 DOI: 10.1074/Jbc.272.34.21213 |
0.636 |
|
| 1997 |
Czar MJ, Galigniana MD, Silverstein AM, Pratt WB. Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus Biochemistry. 36: 7776-7785. PMID 9201920 DOI: 10.1021/Bi970648X |
0.588 |
|
| 1997 |
Silverstein AM, Galigniana MD, Chen MS, Owens-Grillo JK, Chinkers M, Pratt WB. Protein phosphatase 5 is a major component of glucocorticoid receptor·hsp90 complexes with properties of an FK506-binding immunophilin Journal of Biological Chemistry. 272: 16224-16230. PMID 9195923 DOI: 10.1074/Jbc.272.26.16224 |
0.589 |
|
| 1997 |
Pratt WB, Toft DO. Steroid receptor interactions with heat shock protein and immunophilin chaperones Endocrine Reviews. 18: 306-360. PMID 9183567 DOI: 10.1210/Edrv.18.3.0303 |
0.653 |
|
| 1997 |
Dittmar KD, Pratt WB. Folding of the glucocorticoid receptor by the reconstituted hsp90-based chaperone machinery. The initial hsp90·p60·hsp70-dependent step is sufficient for creating the steroid binding conformation Journal of Biological Chemistry. 272: 13047-13054. PMID 9148915 DOI: 10.1074/Jbc.272.20.13047 |
0.637 |
|
| 1997 |
Pratt WB. The role of the hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via map kinase Annual Review of Pharmacology and Toxicology. 37: 297-326. PMID 9131255 DOI: 10.1146/Annurev.Pharmtox.37.1.297 |
0.6 |
|
| 1997 |
Stancato LF, Silverstein AM, Owens-Grillo JK, Chow YH, Jove R, Pratt WB. The hsp90-binding antibiotic geldanamycin decreases Raf levels and epidermal growth factor signaling without disrupting formation of signaling complexes or reducing the specific enzymatic activity of Raf kinase Journal of Biological Chemistry. 272: 4013-4020. PMID 9020108 DOI: 10.1074/Jbc.272.7.4013 |
0.444 |
|
| 1996 |
Owens-Grillo JK, Stancato LF, Hoffmann K, Pratt WB, Krishna P. 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. PMID 8952474 DOI: 10.1021/Bi9615349 |
0.596 |
|
| 1996 |
Chen MS, Silverstein AM, Pratt WB, Chinkers M. The tetratricopeptide repeat domain of protein phosphatase 5 mediates binding to glucocorticoid receptor heterocomplexes and acts as a dominant negative mutant Journal of Biological Chemistry. 271: 32315-32320. PMID 8943293 DOI: 10.1074/Jbc.271.50.32315 |
0.591 |
|
| 1996 |
Czar MJ, Welsh MJ, Pratt WB. Immunofluorescence localization of the 90-kDa heat-shock protein to cytoskeleton. European Journal of Cell Biology. 70: 322-30. PMID 8864660 |
0.424 |
|
| 1996 |
Pratt WB, Gehring U, Toft DO. Molecular chaperoning of steroid hormone receptors Exs. 77: 79-95. PMID 8856970 |
0.566 |
|
| 1996 |
Hutchison KA, Dittmar KD, Stancato LF, Pratt WB. Ability of various members of the hsp70 family of chaperones to promote assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90. The Journal of Steroid Biochemistry and Molecular Biology. 58: 251-8. PMID 8836160 DOI: 10.1016/0960-0760(96)00038-6 |
0.685 |
|
| 1996 |
Gralinski MR, Black SC, Stancato LF, Kilgore KS, Campau PA, Park JL, Ozeck MJ, Pratt WB, Lucchesi BR. Heat stress protects the perfused rabbit heart from complement-mediated injury. The American Journal of Physiology. 271: H571-8. PMID 8770098 DOI: 10.1152/Ajpheart.1996.271.2.H571 |
0.342 |
|
| 1996 |
Owens-Grillo JK, Czar MJ, Hutchison KA, Hoffmann K, Perdew GH, Pratt WB. A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains. The Journal of Biological Chemistry. 271: 13468-75. PMID 8662874 DOI: 10.1074/Jbc.271.23.13468 |
0.66 |
|
| 1996 |
Dittmar KD, Hutchison KA, Owens-Grillo JK, Pratt WB. Reconstitution of the steroid receptor.hsp90 heterocomplex assembly system of rabbit reticulocyte lysate. The Journal of Biological Chemistry. 271: 12833-9. PMID 8662785 DOI: 10.1074/Jbc.271.22.12833 |
0.631 |
|
| 1996 |
Stancato LF, David M, Carter-Su C, Larner AC, Pratt WB. Preassociation of STAT1 with STAT2 and STAT3 in separate signalling complexes prior to cytokine stimulation Journal of Biological Chemistry. 271: 4134-4137. PMID 8626752 DOI: 10.1074/Jbc.271.8.4134 |
0.357 |
|
| 1996 |
Stancato LF, Silverstein AM, Gitler C, Groner B, Pratt WB. Use of the thiol-specific derivatizing agent N-iodoacetyl-3-[125I]iodotyrosine to demonstrate conformational differences between the unbound and hsp90-bound glucocorticoid receptor hormone binding domain Journal of Biological Chemistry. 271: 8831-8836. PMID 8621522 DOI: 10.1074/Jbc.271.15.8831 |
0.607 |
|
| 1996 |
Stancato LF, Hutchison KA, Krishna P, Pratt WB. Animal and plant cell lysates share a conserved chaperone system that assembles the glucocorticoid receptor into a functional heterocomplex with hsp90. Biochemistry. 35: 554-61. PMID 8555227 DOI: 10.1021/Bi9511649 |
0.655 |
|
| 1995 |
Czar MJ, Lyons RH, Welsh MJ, Renoir JM, Pratt WB. Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus. Molecular Endocrinology (Baltimore, Md.). 9: 1549-60. PMID 8584032 DOI: 10.1210/Mend.9.11.8584032 |
0.664 |
|
| 1995 |
Owens-Grillo JK, Hoffmann K, Hutchison KA, Yem AW, Deibel MR, Handschumacher RE, Pratt WB. 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. The Journal of Biological Chemistry. 270: 20479-84. PMID 7657624 DOI: 10.1074/Jbc.270.35.20479 |
0.665 |
|
| 1995 |
Simons SS, Pratt WB. Glucocorticoid receptor thiols and steroid-binding activity. Methods in Enzymology. 251: 406-22. PMID 7651222 DOI: 10.1016/0076-6879(95)51144-X |
0.498 |
|
| 1995 |
Hutchison KA, Stancato LF, Owens-Grillo JK, Johnson JL, Krishna P, Toft DO, Pratt WB. 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. The Journal of Biological Chemistry. 270: 18841-7. PMID 7642537 DOI: 10.1074/Jbc.270.32.18841 |
0.611 |
|
| 1995 |
Caamaño CA, Morano MI, Dalman FC, Hoversten MT, Watson SJ, Pratt WB, Akil H. Point mutations in the 90-kDa heat shock protein binding region of the glucocorticoid receptor affect the functional characteristics of the receptor. Annals of the New York Academy of Sciences. 761: 403-4. PMID 7625747 DOI: 10.1111/J.1749-6632.1995.Tb31403.X |
0.65 |
|
| 1994 |
Hutchison KA, Dittmar KD, Czar MJ, Pratt WB. Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90. The Journal of Biological Chemistry. 269: 5043-9. PMID 8106480 |
0.585 |
|
| 1994 |
Hutchison KA, Dittmar KD, Pratt WB. All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome". The Journal of Biological Chemistry. 269: 27894-9. PMID 7961721 |
0.602 |
|
| 1994 |
Pratt WB, Welsh MJ. Chaperone functions of the heat shock proteins associated with steroid receptors. Seminars in Cell Biology. 5: 83-93. PMID 7915146 DOI: 10.1006/Scel.1994.1012 |
0.614 |
|
| 1994 |
Caamaño CA, Morano MI, Watson SJ, Dalman FC, Pratt WB, Akil H. The functional relevance of the heteromeric structure of corticosteroid receptors. Annals of the New York Academy of Sciences. 746: 68-77; discussion 77. PMID 7825922 DOI: 10.1111/J.1749-6632.1994.Tb39213.X |
0.353 |
|
| 1994 |
Czar MJ, Owens-Grillo JK, Yem AW, Leach KL, Deibel MR, Welsh MJ, Pratt WB. The hsp56 immunophilin component of untransformed steroid receptor complexes is localized both to microtubules in the cytoplasm and to the same nonrandom regions within the nucleus as the steroid receptor. Molecular Endocrinology (Baltimore, Md.). 8: 1731-41. PMID 7708060 DOI: 10.1210/Mend.8.12.7708060 |
0.624 |
|
| 1993 |
Pratt WB, Czar MJ, Stancato LF, Owens JK. The hsp56 immunophilin component of steroid receptor heterocomplexes: Could this be the elusive nuclear localization signal-binding protein? Journal of Steroid Biochemistry and Molecular Biology. 46: 269-279. PMID 9831475 DOI: 10.1016/0960-0760(93)90216-J |
0.654 |
|
| 1993 |
Scherrer LC, Picard D, Massa E, Harmon JM, Simons SS, Yamamoto KR, Pratt WB. Evidence that the hormone binding domain of steroid receptors confers hormonal control on chimeric proteins by determining their hormone-regulated binding to heat-shock protein 90. Biochemistry. 32: 5381-6. PMID 8499442 DOI: 10.1021/Bi00071A013 |
0.599 |
|
| 1993 |
Stancato LF, Hutchison KA, Chakraborti PK, Simons SS, Pratt WB. Differential effects of the reversible thiol-reactive agents arsenite and methyl methanethiosulfonate on steroid binding by the glucocorticoid receptor. Biochemistry. 32: 3729-36. PMID 8466913 DOI: 10.1021/Bi00065A027 |
0.501 |
|
| 1993 |
Stancato LF, Chow YH, Hutchison KA, Perdew GH, Jove R, Pratt WB. Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. The Journal of Biological Chemistry. 268: 21711-6. PMID 8408024 |
0.443 |
|
| 1993 |
Pratt WB. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor Journal of Biological Chemistry. 268: 21455-21458. PMID 8407992 |
0.422 |
|
| 1993 |
Hutchison KA, Scherrer LC, Czar MJ, Stancato LF, Chow YH, Jove R, Pratt WB. Regulation of glucocorticoid receptor function through assembly of a receptor-heat shock protein complex. Annals of the New York Academy of Sciences. 684: 35-48. PMID 8317846 DOI: 10.1111/J.1749-6632.1993.Tb32269.X |
0.638 |
|
| 1993 |
Hutchison KA, Dalman FC, Hoeck W, Groner B, Pratt WB. Localization of the approximately 12 kDa M(r) discrepancy in gel migration of the mouse glucocorticoid receptor to the major phosphorylated cyanogen bromide fragment in the transactivating domain. The Journal of Steroid Biochemistry and Molecular Biology. 46: 681-6. PMID 8274402 DOI: 10.1016/0960-0760(93)90309-K |
0.435 |
|
| 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 |
0.616 |
|
| 1992 |
Pratt WB, Hutchison KA, Scherrer LC. Steroid receptor folding by heat-shock proteins and composition of the receptor heterocomplex. Trends in Endocrinology and Metabolism: Tem. 3: 326-33. PMID 18407118 DOI: 10.1016/1043-2760(92)90111-D |
0.603 |
|
| 1992 |
Hutchison KA, Czar MJ, Pratt WB. Evidence that the hormone-binding domain of the mouse glucocorticoid receptor directly represses DNA binding activity in a major portion of receptors that are "misfolded" after removal of hsp90. The Journal of Biological Chemistry. 267: 3190-5. PMID 1737773 |
0.344 |
|
| 1992 |
Hutchison KA, Czar MJ, Scherrer LC, Pratt WB. Monovalent cation selectivity for ATP-dependent association of the glucocorticoid receptor with hsp70 and hsp90. The Journal of Biological Chemistry. 267: 14047-53. PMID 1629204 |
0.545 |
|
| 1992 |
Hutchison KA, Stancato LF, Jove R, Pratt WB. The protein-protein complex between pp60v-src and hsp90 is stabilized by molybdate, vanadate, tungstate, and an endogenous cytosolic metal. The Journal of Biological Chemistry. 267: 13952-7. PMID 1629193 |
0.397 |
|
| 1992 |
Scherrer LC, Pratt WB. Association of the transformed glucocorticoid receptor with a cytoskeletal protein complex Journal of Steroid Biochemistry and Molecular Biology. 41: 719-721. PMID 1562545 DOI: 10.1016/0960-0760(92)90411-B |
0.481 |
|
| 1992 |
Hutchison KA, Matić G, Czar MJ, Pratt WB. DNA-binding and non-DNA-binding forms of the transformed glucocorticoid receptor. The Journal of Steroid Biochemistry and Molecular Biology. 41: 715-8. PMID 1562544 DOI: 10.1016/0960-0760(92)90410-K |
0.43 |
|
| 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 |
0.6 |
|
| 1992 |
Pratt WB, Scherrer LC, Hutchison KA, Dalman FC. A model of glucocorticoid receptor unfolding and stabilization by a heat shock protein complex. The Journal of Steroid Biochemistry and Molecular Biology. 41: 223-9. PMID 1373296 DOI: 10.1016/0960-0760(92)90348-M |
0.639 |
|
| 1992 |
Pratt WB. Control of steroid receptor function and cytoplasmic-Nuclear transport by heat shock proteins Bioessays. 14: 841-848. PMID 1365900 DOI: 10.1002/Bies.950141209 |
0.643 |
|
| 1992 |
Scherrer LC, Pratt WB. Energy-dependent conversion of transformed cytosolic glucocorticoid receptors from soluble to particulate-bound form Biochemistry. 31: 10879-10886. PMID 1358199 DOI: 10.1021/Bi00159A031 |
0.537 |
|
| 1992 |
Hutchison KA, Brott BK, De Leon JH, Perdew GH, Jove R, Pratt WB. Reconstitution of the multiprotein complex of pp60src, hsp90, and p50 in a cell-free system. The Journal of Biological Chemistry. 267: 2902-8. PMID 1310678 |
0.431 |
|
| 1991 |
Martins VR, Pratt WB, Terracio L, Hirst MA, Ringold GM, Housley PR. Demonstration by confocal microscopy that unliganded overexpressed glucocorticoid receptors are distributed in a nonrandom manner throughout all planes of the nucleus Molecular Endocrinology. 5: 217-225. PMID 2038343 DOI: 10.1210/Mend-5-2-217 |
0.497 |
|
| 1991 |
Dalman FC, Scherrer LC, Taylor LP, Akil H, Pratt WB. Localization of the 90-kDa heat shock protein-binding site within the hormone-binding domain of the glucocorticoid receptor by peptide competition Journal of Biological Chemistry. 266: 3482-3490. PMID 1995612 |
0.511 |
|
| 1991 |
Meshinchi S, Stancato LF, Gordon BM, Jones KW, Pratt WB. Purification of the endogenous glucocorticoid receptor stabilizing factor. Biochemistry. 30: 8617-22. PMID 1888725 DOI: 10.1021/Bi00099A018 |
0.367 |
|
| 1991 |
Hutchison KA, Matić G, Meshinchi S, Bresnick EH, Pratt WB. Redox manipulation of DNA binding activity and BuGR epitope reactivity of the glucocorticoid receptor. The Journal of Biological Chemistry. 266: 10505-9. PMID 1709934 |
0.591 |
|
| 1991 |
Pratt WB. Retinoic acid receptor belongs to a subclass of nuclear receptors that do not form "docking" complexes with hsp90 Biochemistry. 30: 5605-5608. PMID 1645195 DOI: 10.1021/Bi00236A038 |
0.551 |
|
| 1990 |
Bresnick EH, Dalman FC, Pratt WB. Direct stoichiometric evidence that the untransformed Mr 300 000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex Biochemistry. 29: 520-527. PMID 2405907 DOI: 10.1021/Bi00454A028 |
0.713 |
|
| 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 |
0.538 |
|
| 1990 |
Housley PR, Sanchez ER, Danielsen M, Ringold GM, Pratt WB. Evidence that the conserved region in the steroid binding domain of the glucocorticoid receptor is required for both optimal binding of hsp90 and protection from proteolytic cleavage. A two-site model for hsp90 binding to the steroid binding domain. The Journal of Biological Chemistry. 265: 12778-81. PMID 2376573 |
0.452 |
|
| 1990 |
Meshinchi S, Matić G, Hutchison KA, Pratt WB. Selective molybdate-directed covalent modification of sulfhydryl groups in the steroid-binding versus the DNA-binding domain of the glucocorticoid receptor. The Journal of Biological Chemistry. 265: 11643-9. PMID 2365690 |
0.462 |
|
| 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. The Journal of Biological Chemistry. 265: 4863-70. PMID 2318869 |
0.418 |
|
| 1990 |
Dalman FC, Koenig RJ, Perdew GH, Massa E, Pratt WB. In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90 Journal of Biological Chemistry. 265: 3615-3618. PMID 2303466 |
0.512 |
|
| 1990 |
Pratt WB, Dalman FC, Meshinchi S, Scherrer LC. The relationship between glucocorticoid receptor binding to Hsp90 and receptor function Nippon Naibunpi Gakkai Zasshi. 66: 1185-1197. PMID 2292310 DOI: 10.1507/Endocrine1927.66.12_1185 |
0.581 |
|
| 1990 |
Scherrer LC, Dalman FC, Massa E, Meshinchi S, Pratt WB. Structural and functional reconstitution of the glucocorticoid receptor-Hsp90 complex Journal of Biological Chemistry. 265: 21397-21400. PMID 2254299 |
0.506 |
|
| 1990 |
Pratt WB. Interaction of hsp90 with steroid receptors: organizing some diverse observations and presenting the newest concepts Molecular and Cellular Endocrinology. 74. PMID 2178103 DOI: 10.1016/0303-7207(90)90198-H |
0.353 |
|
| 1989 |
Redmond T, Sanchez ER, Bresnick EH, Schlesinger MJ, Toft DO, Pratt WB, Welsh MJ. Immunofluorescence colocalization of the 90-kDa heat-shock protein and microtubules in interphase and mitotic mammalian cells. European Journal of Cell Biology. 50: 66-75. PMID 2693091 |
0.581 |
|
| 1989 |
Pratt WB, Sanchez ER, Bresnick EH, Meshinchi S, Scherrer LC, Dalman FC, Welsh MJ. Interaction of the glucocorticoid receptor with the Mr 90,000 heat shock protein: an evolving model of ligand-mediated receptor transformation and translocation. Cancer Research. 49: 2222s-2229s. PMID 2649237 |
0.682 |
|
| 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. The Journal of Biological Chemistry. 264: 4992-7. PMID 2647745 |
0.727 |
|
| 1989 |
Meshinchi S, Pratt WB. Evidence that removal of an endogenous metal that stabilizes the untransformed glucocorticoid receptor in cytosol allows ligand-independent receptor transformation Journal of Steroid Biochemistry. 34: 315-317. PMID 2626024 DOI: 10.1016/0022-4731(89)90100-3 |
0.422 |
|
| 1989 |
Dalman FC, Bresnick EH, Patel PD, Perdew GH, Watson SJ, Pratt WB. Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro. The Journal of Biological Chemistry. 264: 19815-21. PMID 2584195 |
0.699 |
|
| 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 |
0.657 |
|
| 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 |
0.744 |
|
| 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. The Journal of Biological Chemistry. 263: 16809-17. PMID 3182813 |
0.611 |
|
| 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 |
0.635 |
|
| 1988 |
Dalman FC, Sanchez ER, Lin AL, Perini F, Pratt WB. Localization of phosphorylation sites with respect to the functional domains of the mouse L cell glucocorticoid receptor. The Journal of Biological Chemistry. 263: 12259-67. PMID 3045115 |
0.371 |
|
| 1987 |
Tienrungroj W, Sanchez ER, Housley PR, Harrison RW, Pratt WB. Glucocorticoid receptor phosphorylation, transformation, and DNA binding. The Journal of Biological Chemistry. 262: 17342-9. PMID 3693356 |
0.385 |
|
| 1987 |
Tienruggroj W, Pratt SE, Grippo JF, Holmgren A, Pratt WB. The heat-stable cytosolic factor that promotes glucocorticoid receptor binding to DNA is neither thioredoxin nor ribonuclease Journal of Steroid Biochemistry. 28: 449-457. PMID 3682813 DOI: 10.1016/0022-4731(87)90501-2 |
0.48 |
|
| 1987 |
Tienrungroj W, Meshinchi S, Sanchez ER, Pratt SE, Grippo JF, Holmgren A, Pratt WB. The role of sulfhydryl groups in permitting transformation and DNA binding of the glucocorticoid receptor. The Journal of Biological Chemistry. 262: 6992-7000. PMID 3584105 |
0.411 |
|
| 1987 |
Pratt WB. Transformation of glucocorticoid and progesterone receptors to the DNA-binding state Journal of Cellular Biochemistry. 35: 51-68. PMID 3312247 DOI: 10.1002/Jcb.240350105 |
0.548 |
|
| 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. The Journal of Biological Chemistry. 262: 6986-91. PMID 3294824 |
0.525 |
|
| 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 |
0.575 |
|
| 1986 |
Sanchez ER, Pratt WB. Phosphorylation of L-cell glucocorticoid receptors in immune complexes: evidence that the receptor is not a protein kinase. Biochemistry. 25: 1378-82. PMID 3964681 DOI: 10.1021/Bi00354A028 |
0.496 |
|
| 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 |
0.592 |
|
| 1985 |
Grippo JF, Holmgren A, Pratt WB. Proof that the endogenous, heat-stable glucocorticoid receptor-activating factor is thioredoxin Journal of Biological Chemistry. 260: 93-97. PMID 3965467 |
0.408 |
|
| 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. The Journal of Biological Chemistry. 260: 12398-401. PMID 3900074 |
0.492 |
|
| 1985 |
Housley PR, Sanchez ER, Westphal HM, Beato M, Pratt WB. The molybdate-stabilized L-cell glucocorticoid receptor isolated by affinity chromatography or with a monoclonal antibody is associated with a 90-92-kDa nonsteroid-binding phosphoprotein. The Journal of Biological Chemistry. 260: 13810-7. PMID 3840483 |
0.381 |
|
| 1985 |
Dahmer MK, Tienrungroj W, Pratt WB. Purification and preliminary characterization of a macromolecular inhibitor of glucocorticoid receptor binding to DNA Journal of Biological Chemistry. 260: 7705-7715. PMID 3838991 |
0.385 |
|
| 1985 |
Housley PR, Sanchez ER, Pratt WB. A non-steroid binding 90-92K phosphoprotein associated with the molybdate-stabilized glucocorticoid receptor Federation Proceedings. 44. |
0.321 |
|
| 1984 |
Liu SL, Grippo JF, Erickson RP, Pratt WB. Murine glucocorticoid receptors and the H-2 locus--a reappraisal. Journal of Steroid Biochemistry. 21: 633-7. PMID 6527531 DOI: 10.1016/0022-4731(84)90023-2 |
0.415 |
|
| 1984 |
Dahmer MK, Housley PR, Pratt WB. Effects of molybdate and endogenous inhibitors on steroid-receptor inactivation, transformation, and translocation Annual Review of Physiology. 46: 67-81. PMID 6370122 DOI: 10.1146/Annurev.Ph.46.030184.000435 |
0.519 |
|
| 1984 |
Housley PR, Grippo JF, Dahmer MK, Pratt WB. CHAPTER 12 – Inactivation, Activation, and Stabilization of Glucocorticoid Receptors Biochemical Actions of Hormones. 347-376. DOI: 10.1016/B978-0-12-452811-6.50017-7 |
0.387 |
|
| 1984 |
Dahmer MK, Pratt WB. Purification and characterization of the macromolecular inhibitor of glycocorticoid receptor translocation Federation Proceedings. 43. |
0.311 |
|
| 1983 |
Leach KL, Dahmer MK, Pratt WB. Glucocorticoid receptor stabilization: Relative effects of molybdate ion on inactivation by alkaline phosphatase and phospholipase A2 Journal of Steroid Biochemistry. 18: 105-107. PMID 6865402 DOI: 10.1016/0022-4731(83)90337-0 |
0.356 |
|
| 1983 |
Grippo JF, Tienrungroj W, Dahmer MK, Housley PR, Pratt WB. Evidence that the endogenous heat-stable glucocorticoid receptor-activating factor is thioredoxin Journal of Biological Chemistry. 258: 13658-13664. PMID 6643445 |
0.412 |
|
| 1982 |
Leach KL, Erickson RP, Pratt WB. The endogenous heat-stable glucocorticoid receptor stabilizing factor and the H-2 locus. Journal of Steroid Biochemistry. 17: 121-3. PMID 7109587 DOI: 10.1016/0022-4731(82)90602-1 |
0.335 |
|
| 1982 |
Leach KL, Grippo JF, Housley PR, Dahmer MK, Salive ME, Pratt WB. Characteristics of an endogenous glucocorticoid receptor stabilizing factor Journal of Biological Chemistry. 257: 381-388. PMID 7053376 |
0.38 |
|
| 1982 |
Housley PR, Dahmer MK, Pratt WB. Inactivation of glucocorticoid-binding capacity by protein phosphatases in the presence of molybdate and complete reactivation by dithiothreitol Journal of Biological Chemistry. 257: 8615-8618. PMID 6284738 |
0.372 |
|
| 1981 |
Wheeler RH, Leach KL, la Forest AC, O'Toole TE, Wagner R, Pratt WB. Glucocorticoid receptor activation and inactivation in cultured human lymphocytes Journal of Biological Chemistry. 256: 434-441. PMID 7451447 |
0.395 |
|
| 1981 |
Dahmer MK, Quasney MW, Bissen ST, Pratt WB. Molybdate permits resolution of untransformed glucocorticoid receptors from the transformed state Journal of Biological Chemistry. 256: 9401-9405. PMID 7287692 |
0.305 |
|
| 1979 |
Sando JJ, Hammond ND, Stratford CA, Pratt WB. Activation of thymocyte glucocorticoid receptors to the steroid binding form. The roles of reducing agents, ATP, and heat-stable factors Journal of Biological Chemistry. 254: 4779-4789. PMID 438214 |
0.385 |
|
| 1979 |
Pratt WB, Sando JJ, Nielsen CJ. Glucocorticoid receptor inactivation and activation by phosphorylation mechanisms Advances in Experimental Medicine and Biology. 117: 343-356. PMID 224677 DOI: 10.1007/978-1-4757-6589-2_19 |
0.491 |
|
| 1979 |
Sando JJ, La Forest AC, Pratt WB. ATP-dependent activation of L cell glucocorticoid receptors to the steroid binding form Journal of Biological Chemistry. 254: 4772-4778. PMID 108283 |
0.352 |
|
| 1978 |
Butley MS, Erickson RP, Pratt WB. Hepatic glucocorticoid receptors and the H-2 locus [18] Nature. 275: 136-138. PMID 692681 DOI: 10.1038/275136A0 |
0.426 |
|
| 1978 |
Pratt WB. The mechanism of glucocorticoid effects in fibroblasts Journal of Investigative Dermatology. 71: 24-35. PMID 355565 DOI: 10.1111/1523-1747.Ep12543774 |
0.437 |
|
| 1977 |
El Masry AH, Braun VC, Nielsen CJ, Pratt WB. Synthesis and biological action of two glucocorticoid alkylating agents Journal of Medicinal Chemistry. 20: 1134-1139. PMID 926113 DOI: 10.1002/Chin.197752357 |
0.345 |
|
| 1977 |
Nielsen CJ, Sando JJ, Pratt WB. Evidence that dephosphorylation inactivates glucocorticoid receptors Proceedings of the National Academy of Sciences of the United States of America. 74: 1398-1402. PMID 266181 DOI: 10.1073/Pnas.74.4.1398 |
0.473 |
|
| 1976 |
Schulte HF, Nielsen CJ, Sando JJ, Pratt WB. Evidence for a phospholipid requirement in the specific binding of glucocorticoids to receptors of fibroblasts and thymic lymphocytes Journal of Biological Chemistry. 251: 2279-2289. PMID 177409 |
0.418 |
|
| 1975 |
Pratt WB, Kaine JL, Pratt DV. The kinetics of glucocorticoid binding to the soluble specific binding protein of mouse fibroblasts Journal of Biological Chemistry. 250: 4584-4591. PMID 166997 |
0.312 |
|
| 1975 |
Nielsen CJ, Schulte HF, Pratt WB. Evidence that phospholipid may be required for the specific binding of glucocorticoids to fibroblast receptors Pharmacologist. 17. |
0.395 |
|
| 1974 |
Kaine JL, Pratt WB. Does the binding of glucocorticoids to the L cell receptor involve a two step mechanism? Pharmacologist. 16. |
0.33 |
|
| 1972 |
Ishii DN, Pratt WB, Aronow L. Steady-state level of the specific glucocorticoid binding component in mouse fibroblasts Biochemistry. 11: 3896-3904. PMID 4673055 |
0.338 |
|
| 1971 |
Hackney JF, Pratt WB. Characterization and partial purification of the specific glucocorticoid-binding component from mouse fibroblasts Biochemistry. 10: 3002-3008. PMID 4331329 |
0.356 |
|
| 1970 |
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| Show low-probability matches. |