Mapping of POP1-binding site on pyrin domain of ASC - Test2 - elhamkhani - TriplyDB

Mapping of POP1-binding site on pyrin domain of ASC

Mapping of POP1-binding site on pyrin domain of ASC

http://www.wikidata.org/entity/Q28395594

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Evaluation of Nod-like receptor (NLR) effector domain interactions Pyrin- and CARD-only Proteins as Regulators of NLR Functions Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy.Three-dimensional Structure of the NLRP7 Pyrin Domain: INSIGHT INTO PYRIN-PYRIN-MEDIATED EFFECTOR DOMAIN SIGNALING IN INNATE IMMUNITY Structural and Functional Analysis of the NLRP4 Pyrin Domain Crystal Structure of NALP3 Protein Pyrin Domain (PYD) and Its Implications in Inflammasome Assembly The NLRP12 Pyrin Domain: Structure, Dynamics, and Functional Insights Three-Dimensional Structure of Human NLRP10/PYNOD Pyrin Domain Reveals a Homotypic Interaction Site Distinct from Its Mouse Homologue Activation and assembly of the inflammasomes through conserved protein domain families Inhibiting the inflammasome: one domain at a time Uncoupling of Pyrin-only protein 2 (POP2)-mediated dual regulation of NF-κB and the inflammasome Differential splicing of the apoptosis-associated speck like protein containing a caspase recruitment domain (ASC) regulates inflammasomes The tandem CARDs of NOD2: intramolecular interactions and recognition of RIP2.An updated view on the structure and function of PYRIN domains.Multiple binding sites on the pyrin domain of ASC protein allow self-association and interaction with NLRP3 protein.PYRIN domains and their interactions in the apoptosis and inflammation signaling pathway.CARD- and pyrin-only proteins regulating inflammasome activation and immunity.POP1 might be recruiting its type-Ia interface for NLRP3-mediated PYD-PYD interaction: Insights from MD simulation.Assembly and regulation of ASC specks.ASC Pyrin Domain Self-associates and Binds NLRP3 Protein Using Equivalent Binding Interfaces.Sequence-specific solid-state NMR assignments of the mouse ASC PYRIN domain in its filament form.COPs and POPs Patrol Inflammasome Activation.The Canonical Inflammasome: A Macromolecular Complex Driving Inflammation.

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P2860

Mapping of POP1-binding site on pyrin domain of ASC

http://www.wikidata.org/entity/Q28395594

description

2008 nî lūn-bûn

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2008 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի մայիսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

@zh-hk

2008年論文

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2008年論文

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2008年论文

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name

Mapping of POP1-binding site on pyrin domain of ASC

@ast

Mapping of POP1-binding site on pyrin domain of ASC

@en

Mapping of POP1-binding site on pyrin domain of ASC

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type

label

Mapping of POP1-binding site on pyrin domain of ASC

@ast

Mapping of POP1-binding site on pyrin domain of ASC

@en

Mapping of POP1-binding site on pyrin domain of ASC

@nl

prefLabel

Mapping of POP1-binding site on pyrin domain of ASC

@ast

Mapping of POP1-binding site on pyrin domain of ASC

@en

Mapping of POP1-binding site on pyrin domain of ASC

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Journal of Biological Chemistry

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Mapping of POP1-binding site on pyrin domain of ASC

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P2093

Helen Chang

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

Hong Cheng

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

Rachel L Dubas

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

Sheila L Robbins

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

Thiagarajan Srimathi

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

Young Chul Park

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

P2860

Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1

ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells

A Shope Fibroma virus PYRIN-only protein modulates the host immune response

Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome

PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-kappa B and caspase-1-dependent cytokine processing

Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes

The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-kappa B and pro-caspase-1 regulation

Pyrin-only protein 2 modulates NF-kappaB and disrupts ASC:CLR interactions

NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder

The PAAD/PYRIN-family protein ASC is a dual regulator of a conserved step in nuclear factor kappaB activation pathways

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scholarly article

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10.1074/JBC.M801589200

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22

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283

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2008-03-24T00:00:00Z

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18362139

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