T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1. - Wikidata - awgldk - TriplyDB

T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1.

T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1.

http://www.wikidata.org/entity/Q34174201

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The paracaspase MALT1: biological function and potential for therapeutic inhibition RIPK-dependent necrosis and its regulation by caspases: a mystery in five acts PKCθ/β and CYLD are antagonistic partners in the NFκB and NFAT transactivation pathways in primary mouse CD3+ T lymphocytes Crystal structure of the mucosa-associated lymphoid tissue lymphoma translocation 1 (MALT1) paracaspase region Structural architecture of the CARMA1/Bcl10/MALT1 signalosome: nucleation-induced filamentous assembly.Structural analysis of phenothiazine derivatives as allosteric inhibitors of the MALT1 paracaspase Molecular basis for specificity of the Met1-linked polyubiquitin signal MALT1 is not alone after all: identification of novel paracaspases The paracaspase MALT1 mediates CARD14-induced signaling in keratinocytes Alternative splicing of MALT1 controls signalling and activation of CD4(+) T cells The CBM signalosome: potential therapeutic target for aggressive lymphoma?Pharmacological inhibition of MALT1 protease activity protects mice in a mouse model of multiple sclerosis.Mechanism and specificity of the human paracaspase MALT1.The CARD11-BCL10-MALT1 (CBM) signalosome complex: Stepping into the limelight of human primary immunodeficiency.MALT1 auto-proteolysis is essential for NF-κB-dependent gene transcription in activated lymphocytes.Cleavage of roquin and regnase-1 by the paracaspase MALT1 releases their cooperatively repressed targets to promote T(H)17 differentiation.Conversion of the LIMA1 tumour suppressor into an oncogenic LMO-like protein by API2-MALT1 in MALT lymphoma.The paracaspase MALT1 cleaves HOIL1 reducing linear ubiquitination by LUBAC to dampen lymphocyte NF-κB signalling.The API2-MALT1 fusion exploits TNFR pathway-associated RIP1 ubiquitination to promote oncogenic NF-κB signaling.Negative regulation of NF-κB signaling in T lymphocytes by the ubiquitin-specific protease USP34 Protein ubiquitination in lymphoid malignancies.Malt1 protease inactivation efficiently dampens immune responses but causes spontaneous autoimmunity.Monoubiquitination and activity of the paracaspase MALT1 requires glutamate 549 in the dimerization interface T cell receptor-dependent activation of mTOR signaling in T cells is mediated by Carma1 and MALT1, but not Bcl10.MALT1 Protease Activity Is Required for Innate and Adaptive Immune Responses.Insights into the Molecular Pathogenesis of Activated B-Cell-like Diffuse Large B-Cell Lymphoma and Its Therapeutic Implications.ADAP regulates cell cycle progression of T cells via control of cyclin E and Cdk2 expression through two distinct CARMA1-dependent signaling pathways.Two Antagonistic MALT1 Auto-Cleavage Mechanisms Reveal a Role for TRAF6 to Unleash MALT1 Activation.MALT1 is required for EGFR-induced NF-κB activation and contributes to EGFR-driven lung cancer progression BCL10GFP fusion protein as a substrate for analysis of determinants required for mucosa-associated lymphoid tissue 1 (MALT1)-mediated cleavage.Lymphomagenic CARD11/BCL10/MALT1 signaling drives malignant B-cell proliferation via cooperative NF-κB and JNK activation The Paracaspase MALT1.The HECTD3 E3 ubiquitin ligase suppresses cisplatin-induced apoptosis via stabilizing MALT1.CARMA1- and MyD88-dependent activation of Jun/ATF-type AP-1 complexes is a hallmark of ABC diffuse large B-cell lymphomas.A new look at T cell receptor signaling to nuclear factor-κB Role of the CARMA1/BCL10/MALT1 complex in lymphoid malignancies.MALT1 inhibitors prevent the development of DSS-induced experimental colitis in mice via inhibiting NF-κB and NLRP3 inflammasome activation.MALT1 small molecule inhibitors specifically suppress ABC-DLBCL in vitro and in vivo From MALT lymphoma to the CBM signalosome: three decades of discovery.MALT1 protease: a new therapeutic target in B lymphoma and beyond?

P2860

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P2860

T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1.

http://www.wikidata.org/entity/Q34174201

description

2011 nî lūn-bûn

@nan

2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

T-cell receptor-induced JNK ac ...... inactivation of CYLD by MALT1.

@ast

T-cell receptor-induced JNK ac ...... inactivation of CYLD by MALT1.

@en

T-cell receptor-induced JNK ac ...... inactivation of CYLD by MALT1.

@nl

type

label

T-cell receptor-induced JNK ac ...... inactivation of CYLD by MALT1.

@ast

T-cell receptor-induced JNK ac ...... inactivation of CYLD by MALT1.

@en

T-cell receptor-induced JNK ac ...... inactivation of CYLD by MALT1.

@nl

prefLabel

T-cell receptor-induced JNK ac ...... inactivation of CYLD by MALT1.

@ast

T-cell receptor-induced JNK ac ...... inactivation of CYLD by MALT1.

@en

T-cell receptor-induced JNK ac ...... inactivation of CYLD by MALT1.

@nl

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The EMBO Journal

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T-cell receptor-induced JNK ac ...... inactivation of CYLD by MALT1.

@en

P2093

Annelies Demeyer

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

David Muyllaert

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Tine Bekaert

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P2860

TAK1 is a ubiquitin-dependent kinase of MKK and IKK

The IRAK-1-BCL10-MALT1-TRAF6-TAK1 cascade mediates signaling to NF-kappaB from Toll-like receptor 4

T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-kappaB inhibitor A20

Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains

The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation

CARMA3/Bcl10/MALT1-dependent NF-kappaB activation mediates angiotensin II-responsive inflammatory signaling in nonimmune cells

Regulation of IkappaBalpha expression involves both NF-kappaB and the MAP kinase signaling pathways.

Signal transduction by the JNK group of MAP kinases

CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members

The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination

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1742-1752

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scholarly article

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10.1038/EMBOJ.2011.85

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P433

9

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30

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Petra Van Damme

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2011-03-29T00:00:00Z

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50907678

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21448133

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3101995

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