Výsledky vyhledávání - "Lee E. Faber"

Potentiation of Progesterone Receptor-Mediated Transcription by the Immunosuppressant FK506

Autor: Hong Chang, Donald P. McDonnell, Ping-Kaung Ku Tai, Lee E. Faber, Stuart L. Schreiber, Mark W. Albers

Publikováno v: Biochemistry. 33:10666-10671

The nontransformed steroid receptors contain several non-steroid binding proteins, such as hsp90, hsp70, and p59. Recently, we and others have shown that p59 (FKBP59) is an immunophilin which binds two potent immunosuppressants, FK506 and rapamycin.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a76d812973faccfa400a3000a319b79
https://doi.org/10.1021/bi00201a014

Zobrazit plný text záznamu

P59 (FK506 binding protein 59) interaction with heat shock proteins is highly conserved and may involve proteins other than steroid receptors

Autor: Mark W. Albers, Hong Chang, David O. Toft, Stuart L. Schreiber, Ping Kaung K. Tai, Lee E. Faber

Publikováno v: Biochemistry. 32:8842-8847

P59 (also known as FK506 binding protein 59 (FKBP59) or heat shock protein 56 (hsp56)l and heat shock proteins 90 and 70 (hsp90 and hsp70) associate with steroid receptors and are believed to maintain the receptors in an inactive state. Recently, we

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35369f324747b48920ce4cbf2ec90715
https://doi.org/10.1021/bi00085a015

Zobrazit plný text záznamu

Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex

Autor: Mark W. Albers, Hong Chang, Ping-Kaung Ku Tai, Lee E. Faber, Stuart L. Schreiber

Publikováno v: Science. 256:1315-1318

Immunophilins, a family of proteins that exhibit rotamase (peptidyl-prolyl cis-trans isomerase) activity in vitro, are expressed in many organisms and most tissues. Although some immunophilins can mediate the immunosuppressive actions of FK506, rapam

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c213debe1e4703babffd96765de3e2a
https://doi.org/10.1126/science.1376003

Zobrazit plný text záznamu

Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins

Autor: David O. Toft, Lee E. Faber, David F. Smith

Publikováno v: Journal of Biological Chemistry. 265:3996-4003

Progesterone receptor complexes were purified from crude cytosol in a rapid, gentle, one-step procedure using anti-receptor monoclonal antibodies covalently attached to an agarose resin. Five nonreceptor proteins specifically co-purified with unactiv

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0526cee84a3a0b7d4e672dffca81ca71
https://doi.org/10.1016/s0021-9258(19)39693-0

Zobrazit plný text záznamu

Nuclear localization of two steroid receptor-associated proteins, hsp90 and p59

Autor: Jean-Marie Gasc, Jack-Michel Renoir, Lee E. Faber, Francine Delahaye, Etienne-Emile Baulieu

Publikováno v: Experimental Cell Research. 186:362-367

It has been proposed that the unliganded nontransformed form of steroid hormone receptor is a heterooligomer comprising, in addition to the hormone-binding subunit, two associated proteins: a heat shock protein of MW 90,000 (hsp90) and another protei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59d3210fd17c38e91682c31c1c427c56
https://doi.org/10.1016/0014-4827(90)90317-4

Zobrazit plný text záznamu

Use of FK506 and Its Analogs in Studying Progesterone Signaling

Autor: Lee E. Faber, Ping-Kaung Ku Tai

Publikováno v: Estrogens, Progestins, and Their Antagonists ISBN: 9781461273776

Acting through their receptors, steroids play important roles in the regulation of growth, differentiation, reproduction, and metabolism. In the absence of hormone, receptors are complexed with several nonsteroid binding proteins. Included among thes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ee75a3da5556ede14486ae112fe36b70
https://doi.org/10.1007/978-1-4612-2004-6_9

Zobrazit plný text záznamu

Rabbit FKBP59-heat shock protein binding immunophillin (HBI) is a calmodulin binding protein

Autor: Jack-Michel Renoir, Lee E. Faber, Etienne-Emile Baulieu, Marie-Claire Lebeau, Nelly Massol

Publikováno v: Biochemical and biophysical research communications. 187(3)

FKBP59-HBI, a heat shock protein hsp90-binding immunophilin that was originally detected in heterooligomer forms of steroid receptors, is retained on Calmodulin (CAM)-Sepharose 4B in the presence of 2 mM Ca2+ and is eluted by EGTA, demonstrating a sp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be569eb5e7b8cabd90b8f6e830909703
https://pubmed.ncbi.nlm.nih.gov/1384470

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání