The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor
about
Comparison of crystal structures of human androgen receptor ligand-binding domain complexed with various agonists reveals molecular determinants responsible for binding affinityModulation of Androgen Receptor Activation Function 2 by Testosterone and DihydrotestosteroneStructural characterization of the human androgen receptor ligand-binding domain complexed with EM5744, a rationally designed steroidal ligand bearing a bulky chain directed toward helix 12A surface on the androgen receptor that allosterically regulates coactivator bindingCommunication between the ERRalpha homodimer interface and the PGC-1alpha binding surface via the helix 8-9 loopIdentification of SRC3/AIB1 as a Preferred Coactivator for Hormone-activated Androgen ReceptorPeptidomimetic targeting of critical androgen receptor-coregulator interactions in prostate cancerDiscovery of antiandrogen activity of nonsteroidal scaffolds of marketed drugsQuantification of the vitamin D receptor-coregulator interactionAndrogen receptor mutations associated with androgen insensitivity syndrome: a high content analysis approach leading to personalized medicineHormone binding and co-regulator binding to the glucocorticoid receptor are allosterically coupled.Systematic structure-function analysis of androgen receptor Leu701 mutants explains the properties of the prostate cancer mutant L701H.Small molecule inhibitors targeting the "achilles' heel" of androgen receptor activityEffect of anabolic-androgenic steroids and glucocorticoids on the kinetics of hAR and hGR nucleocytoplasmic translocationAlternative inhibition of androgen receptor signaling: peptidomimetic pyrimidines as direct androgen receptor/coactivator disruptors.Structural basis for computational screening of non-steroidal androgen receptor ligands.Small molecule inhibitors as probes for estrogen and androgen receptor actionMechanism of androgen receptor antagonism by bicalutamide in the treatment of prostate cancerAlternatively spliced androgen receptor variantsSimilarities and Distinctions in Actions of Surface-Directed and Classic Androgen Receptor Antagonists.Androgen receptor: structure, role in prostate cancer and drug discovery.The androgen receptor and its use in biological assays: looking toward effect-based testing and its applications.Structure-based discovery of antagonists of nuclear receptor LRH-1.Posttranslational modification of the androgen receptor in prostate cancer.Deleted in breast cancer 1, a novel androgen receptor (AR) coactivator that promotes AR DNA-binding activity.Splicing of a novel androgen receptor exon generates a constitutively active androgen receptor that mediates prostate cancer therapy resistance.A novel androgen receptor amino terminal region reveals two classes of amino/carboxyl interaction-deficient variants with divergent capacity to activate responsive sites in chromatin.Structural and functional characterization of the interdomain interaction in the mineralocorticoid receptor.Structure of the homodimeric androgen receptor ligand-binding domainCoregulator control of androgen receptor action by a novel nuclear receptor-binding motif.Beyond the ligand-binding pocket: targeting alternate sites in nuclear receptors.Biological relevance of Hsp90-binding immunophilins in cancer development and treatment.Androgen receptor splice variant 7 in castration-resistant prostate cancer: Clinical considerations.Antiandrogens act as selective androgen receptor modulators at the proteome level in prostate cancer cells.Engineered repressors are potent inhibitors of androgen receptor activity.The three dimensional Quantitative Structure Activity Relationships (3D-QSAR) and docking studies of curcumin derivatives as androgen receptor antagonistsAllosteric conversation in the androgen receptor ligand-binding domain surfaces.Discovery of the first irreversible small molecule inhibitors of the interaction between the vitamin D receptor and coactivatorsNovel flufenamic acid analogues as inhibitors of androgen receptor mediated transcriptionRational design of novel antiandrogens for neutralizing androgen receptor function in hormone refractory prostate cancer.
P2860
Q24647922-E32C8B0E-FA8E-4796-828D-651F4B895AB6Q27646416-F38711E0-EDFB-429E-BA39-420F2D2E3742Q27647445-5AB8960A-DD6A-4630-A515-7828EF8D820CQ27648698-476E830D-D984-4D5E-8344-AC3C1DD79D0DQ27650466-381F8B3F-C8F7-44E5-9EAD-AA2DA3D4FFD9Q27659041-13536167-91B0-4CD7-9993-FDFDBAACABD0Q28291526-93A30077-CB30-42CB-A63A-A9603D2BE05EQ33289718-9AA8531A-2DAA-4C23-A104-08C9F9B95A93Q33404382-2BBA3AC4-D025-4BD6-AA73-1CB27A6A0479Q33518450-5FF6B8B3-B9A9-4E69-AF15-E5E09BBCBC4AQ33545556-CAA1394D-6040-49EF-9AF0-B86137A35FEBQ33717757-ACC7CB8D-29FA-4D42-ACA7-4A8F812D76B7Q33810134-F26E1B12-F871-4C2E-B8A4-D6E84E7161D2Q33901050-76AB1892-321E-4039-B236-BA6A34BC64C6Q34140002-9D154788-C308-478E-88AE-2CB4D24064AFQ34289773-E475B41B-1EF8-4917-82E5-8ADBD882E449Q34575905-DAB00ED9-646D-446F-B84C-44685E03069DQ34996358-5A93FBE5-B4A2-4816-B9F1-5BD985A94F11Q35606969-0C66FCEA-0ED4-4BB2-9140-A426B9409A89Q35762232-015953C8-FDEB-40D0-937E-98F0A72AE200Q36063723-409518A9-CB09-454B-B059-1BD7E64F43B6Q36509830-3D0339D3-1F48-47E7-8FD3-04B635B896FEQ37000608-EFADC279-72D0-4D63-A2CE-BB759BA54E52Q37092022-1A8C0BB1-A59A-4F95-B1AA-C96D48213918Q37119749-F4763F1D-D60F-4D1B-9553-F4BFDBB0ACE4Q37145531-DA3C110F-ECB2-4E72-A5F4-6637FE6ECB2EQ37210787-FED556CB-FF95-4143-8885-759CD0A82D0FQ37332443-B54886CB-4ED8-4176-A581-490089FFAA7EQ37637859-F6E5D0C5-E595-421D-9ACA-CA306D5ACCA9Q37691685-DA307767-9290-4CC1-9E99-BBE5B5F83A5EQ38076345-2E6E6138-0E11-45BF-90AC-1400DA36A5B9Q38371280-D46537B0-7FD1-49EF-B701-D0C7780F4CCEQ38852008-2CAFF357-361E-4A44-B0F2-EA2611AE4D13Q38908290-8400769E-D8CA-487B-9561-ED694E0F3666Q39012681-E6489B2D-2B1A-42B3-AF8C-BF08BCB74C3FQ39320831-6D600674-082B-4689-B2E1-F9DEB0E0FB5AQ39338812-05115700-2770-4E37-AD85-505099B308B5Q39352690-945098CF-F594-4E15-BA05-045898B61F52Q39818559-B39217CC-DF30-49DD-8E49-BEF55FD3DF38Q39955570-290418AA-9B82-4B0C-9906-65F3A7F36F1D
P2860
The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor
description
2005 nî lūn-bûn
@nan
2005 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մարտին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
name
The molecular mechanisms of co ...... ation by the androgen receptor
@ast
The molecular mechanisms of co ...... ation by the androgen receptor
@en
The molecular mechanisms of co ...... ation by the androgen receptor
@en-gb
The molecular mechanisms of co ...... ation by the androgen receptor
@nl
type
label
The molecular mechanisms of co ...... ation by the androgen receptor
@ast
The molecular mechanisms of co ...... ation by the androgen receptor
@en
The molecular mechanisms of co ...... ation by the androgen receptor
@en-gb
The molecular mechanisms of co ...... ation by the androgen receptor
@nl
prefLabel
The molecular mechanisms of co ...... ation by the androgen receptor
@ast
The molecular mechanisms of co ...... ation by the androgen receptor
@en
The molecular mechanisms of co ...... ation by the androgen receptor
@en-gb
The molecular mechanisms of co ...... ation by the androgen receptor
@nl
P2093
P2860
P50
P356
P1476
The molecular mechanisms of co ...... ation by the androgen receptor
@en
P2093
Edson Delgado-Rodrigues
Ellena Mar
Jamie M R Moore
John D Baxter
Phuong Nguyen
Robert J Fletterick
P2860
P304
P356
10.1074/JBC.M407046200
P407
P577
2004-11-24T00:00:00Z