Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.
about
The Mediator subunit MED1/TRAP220 is required for optimal glucocorticoid receptor-mediated transcription activationActivation of TRAP/mediator subunit TRAP220/Med1 is regulated by mitogen-activated protein kinase-dependent phosphorylationA coregulatory role for the TRAP-mediator complex in androgen receptor-mediated gene expressionMED1 phosphorylation promotes its association with mediator: implications for nuclear receptor signalingQuantitative proteomics of the thyroid hormone receptor-coregulator interactionsDomain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation.Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo.Arginine and glutamate-rich 1 (ARGLU1) interacts with mediator subunit 1 (MED1) and is required for estrogen receptor-mediated gene transcription and breast cancer cell growthMED19 and MED26 are synergistic functional targets of the RE1 silencing transcription factor in epigenetic silencing of neuronal gene expressionLinking dioxins to diabetes: epidemiology and biologic plausibilityMediator-dependent nuclear receptor functionStructural considerations of vitamin D signalingRB18A regulates p53-dependent apoptosisThe Med1 subunit of transcriptional mediator plays a central role in regulating CCAAT/enhancer-binding protein-beta-driven transcription in response to interferon-gammaKey roles for MED1 LxxLL motifs in pubertal mammary gland development and luminal-cell differentiationStructural and functional organization of TRAP220, the TRAP/mediator subunit that is targeted by nuclear receptorsCore LXXLL motif sequences in CREB-binding protein, SRC1, and RIP140 define affinity and selectivity for steroid and retinoid receptors.Cyclin-dependent kinase 8 positively cooperates with Mediator to promote thyroid hormone receptor-dependent transcriptional activationSegmentation gene product Fushi tarazu is an LXXLL motif-dependent coactivator for orphan receptor FTZ-F1Drosophila Med6 is required for elevated expression of a large but distinct set of developmentally regulated genesUnderstanding large multiprotein complexes: applying a multiple allosteric networks model to explain the function of the Mediator transcription complex.Survey of the year 2000 commercial optical biosensor literature.Med1 regulates meiotic progression during spermatogenesis in miceGene expression profiles in human and mouse primary cells provide new insights into the differential actions of vitamin D3 metabolites.Dynamic interactions and cooperative functions of PGC-1alpha and MED1 in TRalpha-mediated activation of the brown-fat-specific UCP-1 geneMicroRNA 146 (Mir146) modulates spermatogonial differentiation by retinoic acid in mice.Med1 plays a critical role in the development of tamoxifen resistance.Coactivation of estrogen receptor alpha (ER alpha)/Sp1 by vitamin D receptor interacting protein 150 (DRIP150).Coregulator interactions with the thyroid hormone receptor.Androgen receptor: structure, role in prostate cancer and drug discovery.Coactivator recruitment is enhanced by thyroid hormone receptor trimers.Transcription in four dimensions: nuclear receptor-directed initiation of gene expressionAlternative mechanisms by which mediator subunit MED1/TRAP220 regulates peroxisome proliferator-activated receptor gamma-stimulated adipogenesis and target gene expression.Vitamin D-interacting protein 205 (DRIP205) coactivation of estrogen receptor alpha (ERalpha) involves multiple domains of both proteins.Plant Mediator complex and its critical functions in transcription regulation.ERK and AKT signaling drive MED1 overexpression in prostate cancer in association with elevated proliferation and tumorigenicity.Regulation of androgen receptor-dependent transcription by coactivator MED1 is mediated through a newly discovered noncanonical binding motif.Identification of DRIP205 as a coactivator for the Farnesoid X receptor.Role of mediator in transcriptional activation by the aryl hydrocarbon receptor.CaMKII regulates retinoic acid receptor transcriptional activity and the differentiation of myeloid leukemia cells.
P2860
Q24293098-9A221920-26E3-4701-ABDA-E934BA003A23Q24297166-D914E106-857C-4501-8ED1-5B6FF7800513Q24306297-D8D402A6-8F0A-47A6-9B17-945AEEED2D62Q24317446-595874EA-426A-4578-91F7-AAFB06BEB690Q24337435-E308E03E-EDC0-4529-9070-DC7C28027D39Q24514479-D87D0707-864C-4939-91B6-B6BE14811687Q24534347-9AB121B9-4534-4116-B7C3-C5F77D274FE7Q24634157-AC016C52-9C54-4AB1-B9E5-65D43662A08BQ24644562-BAEE889D-A4E8-4168-95A6-4BEFB0CF9812Q24810578-CEC1A87B-477A-49F4-9C95-09B9E7C483DAQ26995848-E60E9D4F-F07A-48BB-B151-C5E8BC73E94BQ27022483-C3ACFBE2-3BF7-49D3-A49C-5CC212794CF2Q28200741-25398417-AFA5-4440-B3C7-4F4B60AA9FD9Q28590973-647881DA-9F4F-4635-B580-A0465C807044Q28594146-2C1FDFB2-FB66-4677-8C51-9920A5F12219Q28594313-F845D12F-3137-425F-99C5-5149A17AA576Q31568030-BA5C1230-A7ED-41CA-AC57-72C27208C519Q33826498-AD43C98F-522F-46F9-BD8F-DF1C480BDF91Q33947738-F447C883-553C-4A4B-A70E-882C9456E672Q33969120-E86D9344-32F9-4358-89C5-3AC419341573Q34195277-0185CB81-BDD3-4E58-B5C6-E05103A0A732Q34464911-8D7386A6-A44E-4206-89F2-8B03BA295284Q34467453-6653A4BA-70D6-404D-ABD1-FC0EC526478BQ35014417-B259B6C2-99E7-4AFC-A87B-BF32AB5736D1Q35553824-6410F60E-AFC8-4EBF-9894-ECE2333E6F36Q35617113-44141BEF-E8F5-41FB-88EF-659043441D73Q35883606-8D372981-543F-4F7F-8C8C-AA8A35EAA5CFQ35994983-2BC2F2AA-0ABB-48C7-9D8B-1FA57DC9EECBQ36013037-25F7D1FE-2FF9-4ECD-8708-104189FA3634Q36063723-2D332F65-6C1B-4576-8111-1D7C2DDF9183Q36378300-4B8B87D6-F553-42FF-B521-6733E9B5D6C6Q36384441-F7C4E1AA-F0C8-48B5-BDDE-4EB55712EF0DQ36421347-7D363AA1-0619-425C-97CC-A77F68DB0B23Q38335656-D35C8735-250F-42ED-84EB-291D80F0B920Q38546777-78D80EAC-EEC7-4F44-83AD-E33CD4258784Q39173954-4288F190-1D7B-4FAB-AED6-2B1FF6B67210Q39439753-6EF78AF3-0FF6-4DCD-B071-5319B1844D85Q40547550-E6F41B18-5A66-480C-A7F8-A39FA3093B28Q40598216-D1AFEB12-EE2A-4950-9FEF-053FECD949CDQ42130829-07CFF6A0-8C1B-4C4B-B8E7-739577AB32F2
P2860
Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.
description
2000 nî lūn-bûn
@nan
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.
@ast
Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.
@en
type
label
Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.
@ast
Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.
@en
prefLabel
Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.
@ast
Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.
@en
P2093
P2860
P1476
Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.
@en
P2093
P2860
P304
P356
10.1128/MCB.20.15.5433-5446.2000
P407
P577
2000-08-01T00:00:00Z