Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription. - sprookjes - yvandenbroek - TriplyDB

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription.

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription.

http://www.wikidata.org/entity/Q36535326

about

The Ubiquitination of NF-κB Subunits in the Control of Transcription The Regulation of NF-κB Subunits by Phosphorylation Regulation of Met1-linked polyubiquitin signalling by the deubiquitinase OTULIN Ubiquitin-dependent regulation of Foxp3 and Treg function Ubiquitin in the immune system Deubiquitinases: Novel Therapeutic Targets in Immune Surveillance?Modulation of the p53/MDM2 interplay by HAUSP inhibitors USP7 is a SUMO deubiquitinase essential for DNA replication Deubiquitination of Tip60 by USP7 determines the activity of the p53-dependent apoptotic pathway HSCARG downregulates NF-κB signaling by interacting with USP7 and inhibiting NEMO ubiquitination.Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).The Deubiquitinating Enzyme USP7 Regulates Androgen Receptor Activity by Modulating Its Binding to Chromatin.p97/VCP promotes Cullin-RING-ubiquitin-ligase/proteasome-dependent degradation of IκBα and the preceding liberation of RelA from ubiquitinated IκBα.Ubiquitination in the antiviral immune response Effects of radix curcumae-derived diterpenoid C on Helicobacter pylori-induced inflammation and nuclear factor kappa B signal pathways HAUSP deubiquitinates and stabilizes N-Myc in neuroblastoma.A proteomic perspective of Sirtuin 6 (SIRT6) phosphorylation and interactions and their dependence on its catalytic activity.Selective and reversible inhibitors of ubiquitin-specific protease 7: a patent evaluation (WO2013030218).Discovery of Therapeutic Deubiquitylase Effector Molecules: Current Perspectives.Regulation of NF-κB by TNF family cytokines.Cell death and deubiquitinases: perspectives in cancer.Modulation of NF-κB Signaling as a Therapeutic Target in Autoimmunity.Structural Characterization of Interaction between Human Ubiquitin-specific Protease 7 and Immediate-Early Protein ICP0 of Herpes Simplex Virus-1.Targeting Deubiquitinating Enzymes in Glioblastoma Multiforme: Expectations and Challenges.Chloroquine attenuates lipopolysaccharide-induced inflammatory responses through upregulation of USP25.The presence of C/EBPα and its degradation are both required for TRIB2-mediated leukaemia.Viral deubiquitinases: role in evasion of anti-viral innate immunity.Prospero-related homeobox 1 drives angiogenesis of hepatocellular carcinoma through selectively activating IL-8 expression.Ubiquitin-specific protease 14 regulates LPS-induced inflammation by increasing ERK1/2 phosphorylation and NF-κB activation.Regulation of NF-κB by PML and PML-RARα.Tumor suppressor cylindromatosis (CYLD) controls HIV transcription in an NF-κB-dependent manner.Mapping the Interaction of B Cell Leukemia 3 (BCL-3) and Nuclear Factor κB (NF-κB) p50 Identifies a BCL-3-mimetic Anti-inflammatory Peptide.Inhibition of transcription by B cell Leukemia 3 (Bcl-3) protein requires interaction with nuclear factor κB (NF-κB) p50.A High-Content RNAi Screen Identifies Ubiquitin Modifiers That Regulate TNF-Dependent Nuclear Accumulation of NF-κB.p300-mediated acetylation of COMMD1 regulates its stability, and the ubiquitylation and nucleolar translocation of the RelA NF-κB subunit.Deubiquitylating enzymes and drug discovery: emerging opportunities.Delineating Crosstalk Mechanisms of the Ubiquitin Proteasome System That Regulate Apoptosis.USP7/HAUSP: A SUMO deubiquitinase at the heart of DNA replication.Broad and diverse mechanisms used by deubiquitinase family members in regulating the type I interferon signaling pathway during antiviral responses.USP7 and USP47 deubiquitinases regulate NLRP3 inflammasome activation

P2860

Q26748938-0711457C-A47E-4958-8025-3046A4D3C1DE Q26752951-297AE56C-0657-4B2D-9F8A-83D689C2C262 Q26778774-B9E2DD1E-FFE1-4C19-BE3A-609D40378778 Q26863525-641CC34E-66E6-4793-B7CE-3483D744D3B7 Q26998711-32DAF38A-4FCC-467D-A9A6-9C834F2E199A Q28069021-A0175F29-9BA0-48BF-802B-9F4A076111F7 Q28075457-8621FFEC-6962-4EEB-AE86-97A8A37A5C34 Q28834083-8D7F60DE-E7F6-485B-AC4F-FCB62CE636AB Q30415089-0CF2753C-1CB9-4078-A44C-5C82C507D87C Q33720245-9C392C63-E5EB-43DB-BACF-334FDFFA92A2 Q35871790-D6551503-E6C1-49F4-9D8A-ACB94B247CE0 Q36065142-FBF9AC60-F80B-421D-A50F-596819C317C3 Q36476873-801E1C18-BBEA-41CE-87E3-5BF0E621AA90 Q36640618-4CB9B47C-8B50-40BC-9A9B-D5A73CB92A29 Q37102457-9445C4D9-7CDC-4201-AFCC-4712BF8D52CC Q37387937-9613F8EA-511E-4127-A501-0574B4735A01 Q37428821-467C402D-4440-468D-963F-53C9D3CAB8E2 Q38181181-CBCBB665-3B3B-4970-817F-29AF17F2D1A8 Q38196269-58E113C7-B37F-4B76-8B36-D90B4D9CF2B2 Q38222709-AC183A97-C724-49E1-BEA9-1C6B97558CA7 Q38239700-28161C60-9D6B-4F15-B3D4-2A5F6F9623C2 Q38644746-F77FFC18-5C89-49FD-BF2E-E913B186CB9C Q38847962-EF27B32E-3068-4B25-919A-97DD57977A6B Q38989377-4101EF9C-26A6-46FB-8434-A1DFA77429E8 Q38992369-0B9687DF-6836-48FF-8B53-2FA0156ABAF6 Q39903788-E5BFF36E-3DDD-4DDB-9F39-7A2909F8146A Q40051381-49795337-66B7-4F19-80FB-01C56ABFA601 Q40147252-B1E94898-398C-4661-9B96-736E5062938A Q40269812-803D2CBD-7A2E-4962-87DF-5A4A0A266FEB Q40288515-134CCD8F-271A-42B7-819E-5BCD0371ACEF Q40607338-F2A46AFF-2545-4EC8-8C5F-59C6E117A114 Q41002001-204775A4-429A-4B6F-9476-B0B3B955D166 Q42005971-BA67118A-1E6F-44DA-BA1F-761777C8E1D8 Q42075805-E0937A1F-73F2-4564-B587-DB9B51EC70E5 Q42852637-B5BA3E86-F4A3-4E21-989E-725D24862260 Q48265884-B78B9A27-2837-4C7F-BFC4-75C7FC30572F Q50316561-77E7D658-C9C6-4418-A670-4BBC20ED6BE8 Q51665623-62E496B8-1AC2-4145-A09E-AC0031B0460D Q54219640-7C48569F-4469-4C49-8253-643EBF6104D5 Q58749340-DB471968-FFBD-471B-BE72-791E2DE0EEB3

P2860

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription.

http://www.wikidata.org/entity/Q36535326

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription.

@ast

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription.

@en

type

label

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription.

@ast

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription.

@en

prefLabel

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription.

@ast

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription.

@en

P1433

Q36535326-DC526E02-2248-4F9E-BFBC-ADBE8B2B2498

P1476

Q36535326-F84D6AB0-5096-4435-9168-65153F53FF52

P2093

Q36535326-08EBB5E8-0C2A-4EE7-9259-751753C9D337

Q36535326-0CE15E5D-D45C-40E8-B231-B3C5A860D929

Q36535326-2DFB0806-3F0B-4505-B881-9186CDA33FEE

Q36535326-31F4EE9C-6171-44C5-9BA4-0C9EB68A4FA9

Q36535326-436BDA2D-51A0-4C57-9957-D8FD27423590

Q36535326-84EA0E88-00D2-483F-BC65-176E336E73D9

Q36535326-B9F7009F-BB7B-4E37-8D8E-A0D8759213A9

Q36535326-DFD069DC-2CF0-47A5-818D-3DE2B2EA2578

Q36535326-FDF7C1C9-1569-4386-8E04-91F378494D58

P2860

Q36535326-08AD8695-6DEF-4160-B5E9-8C7D23C9C8C0

Q36535326-0D1172AE-DD88-4E2E-91D6-4FD627F09BC7

Q36535326-128BF130-C237-49C1-A063-23B94BAE63D7

Q36535326-24204A19-065D-4A54-A18B-D125ACAD32E9

Q36535326-25F0E8DD-7885-41CD-AD3E-D906F0CECB9B

Q36535326-3165E7F4-9E15-42B7-B577-A1810BCCEDD0

Q36535326-319921E1-EB57-4B12-A873-652F933741EB

Q36535326-3FD072FF-443D-4A4D-B3F6-AD810577FDBC

Q36535326-40C8BE31-0F7A-4096-BE97-BBFF021CB58B

Q36535326-4586A63F-0DDB-416B-AA24-DD892D1CBFA8

P304

Q36535326-D426A27E-93A0-4FAF-8F29-F93614C788C9

P31

Q36535326-145B42F4-9936-4C0F-ACB6-EC4133AD49B5

P356

Q36535326-19FD78F7-B876-446F-9ADD-75EBF475369B

P407

Q36535326-3DD10495-331F-42BC-829E-0C7B00E7E617

P433

Q36535326-C80C052F-DCC8-45FE-A868-E863CB91831E

P478

Q36535326-B9601BEC-A883-4D56-A9F6-B07C43F6BD3F

P577

Q36535326-D6C3BD4C-6B1E-408C-9916-73D88E9753D8

P5875

Q36535326-E8D04F9A-0F73-4F77-889B-9BFA9A00B6F1

P698

Q36535326-CBB4B186-7DB3-489D-B74B-A574C83E2485

P921

Q36535326-B7B9A310-2910-44E7-A0F5-4E72D3DBA12C

P932

Q36535326-9542C687-24C7-4703-81FB-34ED77DD3CFB

P356

PNAS.1208446110

P1433

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

P1476

Deubiquitination of NF-κB by Ubiquitin-Specific Protease-7 promotes transcription.

@en

P2093

Abrar Ahmed

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

Amy Colleran

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

Bettina McManus

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

Christine O'Carroll

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

Ezra Burstein

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

Patricia E Collins

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

Patrick A Kiely

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

Ruaidhrí J Carmody

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

Xicheng Mao

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

P2860

Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization

USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product

FOXO4 transcriptional activity is regulated by monoubiquitination and USP7/HAUSP

Defining the human deubiquitinating enzyme interaction landscape

TSPYL5 suppresses p53 levels and function by physical interaction with USP7

Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor

COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase

A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein

Breaking the chains: structure and function of the deubiquitinases

Tumour suppression: disruption of HAUSP gene stabilizes p53

P304

618-623

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

P31

scholarly article

P356

10.1073/PNAS.1208446110

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

P407

P433

2

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

P478

110

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

P577

2012-12-24T00:00:00Z

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

P5875

233984566

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

P698

23267096

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

P921

P932

3545798

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