Direct and distinguishable inhibitory roles for SUMO isoforms in the control of transcriptional synergy. - Wikidata - awgldk - TriplyDB

Direct and distinguishable inhibitory roles for SUMO isoforms in the control of transcriptional synergy.

Direct and distinguishable inhibitory roles for SUMO isoforms in the control of transcriptional synergy.

http://www.wikidata.org/entity/Q34791472

about

Lens epithelium-derived growth factor deSumoylation by Sumo-specific protease-1 regulates its transcriptional activation of small heat shock protein and the cellular response Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors.Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1 Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modifications NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression Role for SUMO modification in facilitating transcriptional repression by BKLF.SUMO protease SENP1 induces isomerization of the scissile peptide bond RSUME enhances glucocorticoid receptor SUMOylation and transcriptional activity Sumoylated NHR-25/NR5A regulates cell fate during C. elegans vulval development Sumoylation of MITF and its related family members TFE3 and TFEB Sumoylation of CCAAT/enhancer-binding protein alpha and its functional roles in hepatocyte differentiation SUMO-specific protease 1 (SENP1) reverses the hormone-augmented SUMOylation of androgen receptor and modulates gene responses in prostate cancer cells.Small ubiquitin-like modifier (SUMO) modification of the androgen receptor attenuates polyglutamine-mediated aggregation PIAS1 is a GATA4 SUMO ligase that regulates GATA4-dependent intestinal promoters independent of SUMO ligase activity and GATA4 sumoylation.Progesterone receptors act as sensors for mitogenic protein kinases in breast cancer models.Signaling inputs to progesterone receptor gene regulation and promoter selectivity.Protein kinases mediate ligand-independent derepression of sumoylated progesterone receptors in breast cancer cells.The human glucocorticoid receptor: molecular basis of biologic function Phosphorylation-dependent sumoylation regulates estrogen-related receptor-alpha and -gamma transcriptional activity through a synergy control motif.Differential effects of sumoylation on transcription and alternative splicing by transcription elongation regulator 1 (TCERG1).The biology of the glucocorticoid receptor: new signaling mechanisms in health and disease The DEAD-box protein DP103 (Ddx20 or Gemin-3) represses orphan nuclear receptor activity via SUMO modification.Kaposi's sarcoma-associated herpesvirus K-bZIP represses gene transcription via SUMO modification.SUMO functions in constitutive transcription and during activation of inducible genes in yeast.A small ubiquitin-related modifier-interacting motif functions as the transcriptional activation domain of Krüppel-like factor 4.Control of progesterone receptor transcriptional synergy by SUMOylation and deSUMOylation.Pregnane X receptor is SUMOylated to repress the inflammatory response.Sumoylation modulates transcriptional activity of MITF in a promoter-specific manner Differential regulation of c-Jun-dependent transcription by SUMO-specific proteases.Repression of SOX6 transcriptional activity by SUMO modification.Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: a proteomic analysis.Cellular processing of the glucocorticoid receptor gene and protein: new mechanisms for generating tissue-specific actions of glucocorticoids.PIASγ enhanced SUMO-2 modification of Nurr1 activation-function-1 domain limits Nurr1 transcriptional synergy Binding of pleomorphic adenoma gene-like 2 to the tumor necrosis factor (TNF)-alpha-responsive region of the NCF2 promoter regulates p67(phox) expression and NADPH oxidase activity.Polo-like kinase 1-mediated phosphorylation of Forkhead box protein M1b antagonizes its SUMOylation and facilitates its mitotic function.SUMO modification regulates inactivation of the voltage-gated potassium channel Kv1.5.The proteins of human chromosome 21.Controlling a master switch of adipocyte development and insulin sensitivity: covalent modifications of PPARγ Multiple mechanisms of growth hormone-regulated gene transcription.Small ubiquitin-like modifier (SUMO) modification mediates function of the inhibitory domains of developmental regulators FOXC1 and FOXC2

P2860

Q24339376-27EC47F1-37C4-40E2-B1AE-9A06B3F56878 Q24519076-A3BE1553-5D36-4EA2-AA26-85D2A3419B8C Q24528161-745D16C9-B750-49C3-8AB2-20CADCEF8014 Q24545952-87AF9FFE-7961-49D4-9C77-C892350EF5F8 Q24547306-6ECFD9A4-77D9-4990-969A-1010510BD273 Q24556900-83568E67-4B00-4DC7-8D28-D139B8AF0ADC Q24596746-E184B18A-2BDD-4566-B28F-EBB70388D8BE Q24629429-95440E4F-5B5E-4533-9DCB-2169843582BB Q27318485-860B1984-7E52-4BD9-9466-95ABFD5C8761 Q28118825-FE23E5EC-ABFC-49A8-A83F-22FBDBA70E4C Q28569405-76443D01-BCDE-459F-8501-4D240824A4B8 Q30352713-A7221245-4A3B-4211-ABCE-8EB28566754D Q30377831-995CD0CF-EF6B-492A-8EB0-38ADC3CC2D3F Q31060298-AB38487A-3D21-4CEF-92E2-CB58FCE8EE03 Q33428469-90CAF881-1403-48ED-95B0-D8861E71923F Q33473070-E7CBB6EA-2728-43FC-8B49-AF0F0BE33433 Q33496645-B5DC2A8F-96C8-4FBB-92B2-AFB85BA59A28 Q33620765-424FCC03-2711-475C-B340-3067F3076F50 Q33643260-1091D6F8-24E0-40A2-8A19-2E2D53461FA8 Q33832763-30A05D90-307E-461E-B46A-CD9B7F9DC607 Q33854747-A9DF9E45-35CB-45D7-9693-BFF0DA771026 Q33861451-AF450274-CB5E-418F-8F22-0F2E2138214E Q33908645-106E4E74-95DD-42A9-8684-94E405FF53EE Q33913182-CBF1E411-AC20-46DA-B206-AE2719DA0C4F Q34107480-715FB0E6-105F-47FE-8945-1898DC533740 Q34206915-0D45960E-F691-4583-83B2-417753EEF2EB Q34257576-52B2E2BE-4F4F-4863-A814-ED92AB63F62A Q34312986-57D567FC-CD65-4B90-A5AF-399E186CEB69 Q34392520-CE7FB955-618B-48BD-9DAF-E2F739E20AC7 Q34489010-7CCAC26A-A015-4A6D-9B0C-07EFBD9B9CFB Q34513152-377F8741-54E3-4EFD-AFFE-E56AFADB4116 Q34536741-90150156-D69F-4242-90FC-640CF301A4A6 Q34565891-73B6CEB4-88CE-4F9F-A717-1850684926C9 Q34623316-D9D4E3F3-94CA-42E9-A37F-04EFD19034A5 Q35055612-D850EF3C-6802-493A-BAF2-E917D9C4A1BA Q35629481-FE11B338-D796-4890-B46E-49D7ADFC01BB Q35821700-77527E53-B1B2-4541-ACD5-1E044B697740 Q35969865-54F777A0-A7DD-46D7-8BBE-C988EC6E08EF Q36002736-322121ED-7FBE-4416-B41A-0596135A8215 Q36003002-4FD3C801-A355-40A2-97F9-F84FF1F577E2

P2860

Direct and distinguishable inhibitory roles for SUMO isoforms in the control of transcriptional synergy.

http://www.wikidata.org/entity/Q34791472

description

2003 nî lūn-bûn

@nan

2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年学术文章

@wuu

2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

name

Direct and distinguishable inh ...... ol of transcriptional synergy.

@ast

Direct and distinguishable inh ...... ol of transcriptional synergy.

@en

Direct and distinguishable inh ...... ol of transcriptional synergy.

@nl

type

label

Direct and distinguishable inh ...... ol of transcriptional synergy.

@ast

Direct and distinguishable inh ...... ol of transcriptional synergy.

@en

Direct and distinguishable inh ...... ol of transcriptional synergy.

@nl

prefLabel

Direct and distinguishable inh ...... ol of transcriptional synergy.

@ast

Direct and distinguishable inh ...... ol of transcriptional synergy.

@en

Direct and distinguishable inh ...... ol of transcriptional synergy.

@nl

P1433

Q34791472-C2F9112C-B1EC-4E74-9BCB-7AE0A9992944

P1476

Q34791472-05DAA0F3-32B8-473E-B046-C4F7C2E2907F

P2093

Q34791472-3ABCB4D3-57FF-42F9-9BB7-4D7FF5AA9BF8

Q34791472-4AB8170F-2E10-41BF-AAD8-B10C970D2177

Q34791472-99524960-A5E3-4FA6-B00E-584206DAE075

P2860

Q34791472-10DA9779-E9C8-4558-893A-5C286ABF36D1

Q34791472-19C16035-407C-4C19-B41D-88D709835016

Q34791472-1E78AAC7-16C5-495A-9C10-F46DD8EDFC20

Q34791472-3D1A8960-CC36-461A-B52B-F377FF910A0A

Q34791472-3E28577A-F19C-4E0A-8C24-CF8D0283EB34

Q34791472-43E47B07-3123-4EAE-A60F-91B6568D025D

Q34791472-68AF3AB2-0D68-4896-8454-C10DCF6D817E

Q34791472-6ABECBE8-7131-48ED-9410-19AB84765827

Q34791472-788167DA-021C-4EE4-A3A8-3C957B4E8D52

Q34791472-7CE85D96-2CA1-49EE-8644-FFBFD6E0D389

P304

Q34791472-02F1823C-A4B2-4CE9-86A9-81AE4B043B0B

P31

Q34791472-A4A2D4F4-9B80-402B-8F87-3062AF7B66C7

P356

Q34791472-C2D049CF-E737-48F8-AC62-A55301919700

P407

Q34791472-345B1C7D-F682-444C-862E-E3AB7053DD76

P433

Q34791472-372FDFD1-306F-42FF-B8F6-97DE658F7C17

P478

Q34791472-CBAA1439-A75A-4099-98DF-06D4286A7F86

P577

Q34791472-6FEC385B-C256-4C75-813C-3A737A0A234E

P5875

Q34791472-EEA25FD0-1C14-4835-A2FB-361AD8FA4765

P698

Q34791472-A07E1D48-0353-4F0B-9A31-C655B0EAE7A5

P932

Q34791472-3F1C07E4-1663-432D-9AB1-3D6372924122

P356

PNAS.2136933100

P1433

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

P1476

Direct and distinguishable inh ...... ol of transcriptional synergy.

@en

P2093

Jorge A Iñiguez-Lluhi

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

Mary E Van Antwerp

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

Sam Holmstrom

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

P2860

Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus.

Transcription factor Sp3 is silenced through SUMO modification by PIAS1

Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition

Structure determination of the small ubiquitin-related modifier SUMO-1

Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes

Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9.

The polycomb protein Pc2 is a SUMO E3

Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3

A synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein alpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3

Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation

P304

15758-15763

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

P31

scholarly article

P356

10.1073/PNAS.2136933100

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

P407

P433

26

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

P478

100

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

P577

2003-12-08T00:00:00Z

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

P5875

8970223

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

P698

14663148

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

P932

307641

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