Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors. - Wikidata - awgldk - TriplyDB

Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors.

Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors.

http://www.wikidata.org/entity/Q35192645

about

Molecular aspects of thyroid hormone actions DACH1 inhibits transforming growth factor-beta signaling through binding Smad4 The aryl hydrocarbon receptor mediates degradation of estrogen receptor alpha through activation of proteasomes The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation Recruitment of the oncoprotein v-ErbA to aggresomes.Proteasome regulation of dynamic transcription factor occupancy on the GnRH-stimulated luteinizing hormone beta-subunit promoter SMRT and N-CoR corepressors are regulated by distinct kinase signaling pathways.Selective estrogen receptor modulators 4-hydroxytamoxifen and raloxifene impact the stability and function of SRC-1 and SRC-3 coactivator proteins.Cell cycle-dependent expression of thyroid hormone receptor-beta is a mechanism for variable hormone sensitivity.Automated yeast two-hybrid screening for nuclear receptor-interacting proteins.Selective estrogen receptor down-regulator and selective estrogen receptor modulators differentially regulate lactotroph proliferation MuRF1 mono-ubiquitinates TRα to inhibit T3-induced cardiac hypertrophy in vivo.Regulation of adipogenesis by natural and synthetic REV-ERB ligands.Oncogenic conversion of the thyroid hormone receptor by altered nuclear transport.Src-dependent phosphorylation at Y406 on the thyroid hormone receptor β confers the tumor suppressor activity Retinoid-related Orphan Receptors (RORs): Roles in Cellular Differentiation and Development.Retinoid-related orphan receptors (RORs): critical roles in development, immunity, circadian rhythm, and cellular metabolism In vivo regulation of human skeletal muscle gene expression by thyroid hormone.Aberrant accumulation of PTTG1 induced by a mutated thyroid hormone beta receptor inhibits mitotic progression.Estrogen receptor-dependent proteasomal degradation of the glucocorticoid receptor is coupled to an increase in mdm2 protein expression Thyroid Hormone Receptors Predict Prognosis in BRCA1 Associated Breast Cancer in Opposing Ways.Ubiquitylation of nuclear receptors: new linkages and therapeutic implications.Back to your heart: ubiquitin proteasome system-regulated signal transduction Desensitization and Incomplete Recovery of Hepatic Target Genes After Chronic Thyroid Hormone Treatment and Withdrawal in Male Adult Mice Thyroid hormone receptors and cancer.Thyroid hormone receptor β suppresses SV40-mediated tumorigenesis via novel nongenomic actions ERα phosphorylation at Y537 by Src triggers E6-AP-ERα binding, ERα ubiquitylation, promoter occupancy, and target gene expression.Upregulation of SIRT1 by 17β-estradiol depends on ubiquitin-proteasome degradation of PPAR-γ mediated by NEDD4-1.Degradation and beyond: control of androgen receptor activity by the proteasome system.Control of peroxisome proliferator-activated receptor fate by the ubiquitinproteasome system.Novel functions of thyroid hormone receptor mutants: beyond nucleus-initiated transcription.Hormone signaling through protein destruction: a lesson from plants The Ski protein can inhibit ligand induced RARalpha and HDAC3 degradation in the retinoic acid signaling pathway.Novel non-genomic signaling of thyroid hormone receptors in thyroid carcinogenesis.Involvement of proteasome in the dynamic assembly of the androgen receptor transcription complex.An array of positioned nucleosomes potentiates thyroid hormone receptor action in vivo.Expression of neddylation-related proteins in melanoma cell lines and the effect of neddylation on melanoma proliferation.Turning off estrogen receptor beta-mediated transcription requires estrogen-dependent receptor proteolysis.Impaired Repressor Function in SUMOylation-Defective Thyroid Hormone Receptor Isoforms Ligand-dependent degradation of retinoid X receptors does not require transcriptional activity or coactivator interactions.

P2860

Q22306217-BECDB3A7-51FA-4FA0-A3D8-55C5E188AB56 Q24296908-197B505D-3A69-4FB6-9F71-F51120674818 Q24550565-884DA472-FA39-42FE-8DD1-6D0E89AC8628 Q24623615-ED34AF7C-CD08-41B8-AC35-CB9544F6679E Q27308854-0C92C98E-5F4D-43D5-837C-852352C798D4 Q30437232-0D6A21D8-796C-426D-98D3-4D47B0602A30 Q30440069-F281801D-15C7-4137-8D8E-6B2736CFEFAC Q30450954-C343F830-E8F3-49A7-8D4F-C2AEC6F641D4 Q33197526-7742AE9C-A6FF-42BE-823E-AF172399E590 Q33209988-FB3F963A-F67A-42CA-9855-E8FA37499CCB Q33564204-D9178DF8-5955-4CD2-A892-18E969649A58 Q33752237-9EDFA45B-3460-4CD1-A031-ED70A365F1D8 Q33993896-68ACBA59-E726-45E0-A181-C32F0C90AAF7 Q34652178-10F9CA74-6BB3-413E-A980-ACB6040732FD Q34654368-F43A7755-B082-45B9-ABE5-CD3C8AE88F08 Q34770626-2B6CAE30-8A69-4440-A2D3-C384F71D2A88 Q34976906-98587EFF-76F4-47EA-B775-1BDC4350480D Q35003916-D7438E86-5BA3-4141-98C8-289217E568F7 Q35070405-6EC2B901-CE81-4EB4-820B-B465BD865EC9 Q35169767-829A7EA2-93F0-49CD-9324-19A4BAE3B7C4 Q35647617-3C21FF34-10BD-40C3-AB0B-72494B02B64B Q35688891-7E13AEBD-400D-4A4B-909A-D0B59DE32A71 Q35803035-854AAF33-3DED-46CE-BC05-90101FB11992 Q35920671-9CDACDEF-D167-47EC-9201-C2ADB497F2B6 Q36120590-1843942B-C32D-4970-A61F-0522AB8DCDCD Q36206509-8D1A2E41-C993-4048-99EA-2948DE77DBE3 Q36210983-4204ED20-7600-48A5-AAD3-A8AAE9C61B10 Q36437294-979DA965-A1F5-45BF-8A20-3283516EA941 Q36539137-55BAA769-47AF-4B5F-AEAA-BA3F9BB88221 Q36659845-B6244076-D76A-4A61-B316-D6BF1DA91B14 Q36684230-D178A5C3-712A-4B60-A92A-62BDB3D062C3 Q37102876-2DE59895-5848-4AB2-8415-780C50590D19 Q37225648-7235D895-BE6B-4ACF-8B0B-22DF4DD5252B Q37347113-3CFF9034-0AEA-42FE-A59E-73E8D3863375 Q38362060-66731F2D-F1A6-4226-87A3-C4889929B5CF Q38471807-82271156-891F-4F69-AA6D-2AD47035FCBA Q38933296-9DC0BDD7-461B-43C2-9561-4695727A3E4C Q39125264-3621F95A-C7AD-429F-B1A1-21304EC4B355 Q39187959-996840B7-E6B5-49AF-9682-AC130FA087D3 Q39460366-AA939E35-E2C8-4B12-9CFA-A660D90EBD12

P2860

Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors.

http://www.wikidata.org/entity/Q35192645

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

Hormone binding induces rapid ...... of thyroid hormone receptors.

@ast

Hormone binding induces rapid ...... of thyroid hormone receptors.

@en

type

label

Hormone binding induces rapid ...... of thyroid hormone receptors.

@ast

Hormone binding induces rapid ...... of thyroid hormone receptors.

@en

prefLabel

Hormone binding induces rapid ...... of thyroid hormone receptors.

@ast

Hormone binding induces rapid ...... of thyroid hormone receptors.

@en

P1433

Q35192645-638F5A2E-6864-4B2F-9B35-1D6DFA84BFF2

P1476

Q35192645-CEE5B599-63E7-4D78-9083-77A49BE7DE4C

P2093

Q35192645-03B0CE4C-58EA-4032-B6CA-F33092E7A1A6

Q35192645-17F5D745-881A-4C4E-A2E5-3E864031C4C8

Q35192645-59D9CE21-6E32-484C-BEFF-96D5B0247077

Q35192645-5D1C5A49-07B7-4F50-B2D8-E91FF7471672

Q35192645-60ED65C9-6866-499A-A94D-8DCDD2D8E964

Q35192645-7E80EA6C-D312-428A-9DD5-9C9637216412

Q35192645-7F05DC50-BCB1-459F-A0B0-B35ED604C962

Q35192645-9BF47AF7-8689-4657-9BD0-9C3D8E5AD089

Q35192645-DA1BACAC-D04C-4B76-93BB-E593C4156A26

P2860

Q35192645-0095C361-220C-4B89-AD32-6305CA6203A8

Q35192645-011F789C-42FD-4A8E-A06B-D5C271709C69

Q35192645-1833C286-8DBC-4C3C-AB6B-19267CB195EB

Q35192645-1EBB7C7A-AAE2-49FC-AD74-BDD6F9DEE618

Q35192645-2054030B-1E72-4D94-9768-1B996445C5B3

Q35192645-21FB4C82-AD90-4DE8-911D-6AA55116D9DA

Q35192645-2A73A812-4674-4E3B-97F1-729C95EB612F

Q35192645-38C33A28-8796-4941-90EC-0B14A28608B3

Q35192645-42312677-803A-4182-A69C-EA15082CF0B2

Q35192645-4C5E9116-300E-45CA-8820-65ECE7F4A7EA

P304

Q35192645-CED88994-4123-4F81-B4B6-4B54B9C08711

P31

Q35192645-2BCE823D-98AA-450D-8368-E8994FE61836

P356

Q35192645-1DD9B05E-E06B-4A2F-84B6-2DD24E879F2A

P407

Q35192645-29665EDE-3570-435C-982F-D40860E198D1

P433

Q35192645-2631A31B-859E-4835-A028-C647AC4A38E6

P478

Q35192645-358D7C84-8A3C-40EE-809C-E62E0FDABC7B

P577

Q35192645-DE5507DC-87F2-4AC3-A86A-2243E2F85CE4

P5875

Q35192645-E1C2C7AD-31AB-45F8-B9F4-2BE1076B18C8

P698

Q35192645-E75CB01E-49A4-43BB-A1B2-F1851F8A28CF

P932

Q35192645-4757B392-54ED-4797-B576-C2ED36D6A321

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Hormone binding induces rapid ...... of thyroid hormone receptors.

@en

P2093

Cheng S

http://www.w3.org/2001/XMLSchema#string

Dace A

http://www.w3.org/2001/XMLSchema#string

Furuno T

http://www.w3.org/2001/XMLSchema#string

Hanover JA

http://www.w3.org/2001/XMLSchema#string

Nakanishi M

http://www.w3.org/2001/XMLSchema#string

Park KS

http://www.w3.org/2001/XMLSchema#string

Takamura N

http://www.w3.org/2001/XMLSchema#string

West BL

http://www.w3.org/2001/XMLSchema#string

Zhao L

http://www.w3.org/2001/XMLSchema#string

P2860

Characterization of seven novel mutations of the c-erbA beta gene in unrelated kindreds with generalized thyroid hormone resistance. Evidence for two "hot spot" regions of the ligand binding domain

The ubiquitin system

Ubiquitin-dependent protein degradation

Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin

Nuclear receptor coregulators: cellular and molecular biology

The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B

Proteasome inhibitors: valuable new tools for cell biologists

Interaction of thyroid hormone nuclear receptor with antibody: characterization of the thyroid hormone binding site.

Differential expression of mutant and normal beta T3 receptor alleles in kindreds with generalized resistance to thyroid hormone.

Interaction of human beta 1 thyroid hormone receptor and its mutants with DNA and retinoid X receptor beta. T3 response element-dependent dominant negative potency

P304

8985-8990

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.160257997

http://www.w3.org/2001/XMLSchema#string

P407

P433

16

http://www.w3.org/2001/XMLSchema#string

P478

97

http://www.w3.org/2001/XMLSchema#string

P577

2000-08-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

12410134

http://www.w3.org/2001/XMLSchema#string

P698

10908671

http://www.w3.org/2001/XMLSchema#string

P932

16808

http://www.w3.org/2001/XMLSchema#string