The PYRIN domain: a member of the death domain-fold superfamily - Wikidata - thesis-toulmin - TriplyDB

The PYRIN domain: a member of the death domain-fold superfamily

The PYRIN domain: a member of the death domain-fold superfamily

http://www.wikidata.org/entity/Q24644648

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PYPAF1, a PYRIN-containing Apaf1-like protein that assembles with ASC and regulates activation of NF-kappa B The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-kappa B and pro-caspase-1 regulation De novo CIAS1 mutations, cytokine activation, and evidence for genetic heterogeneity in patients with neonatal-onset multisystem inflammatory disease (NOMID): a new member of the expanding family of pyrin-associated autoinflammatory diseases The PAAD/PYRIN-family protein ASC is a dual regulator of a conserved step in nuclear factor kappaB activation pathways Horror autoinflammaticus: the molecular pathophysiology of autoinflammatory disease (*)Pyrin- and CARD-only Proteins as Regulators of NLR Functions NLRC5: a newly discovered MHC class I transactivator (CITA)Rapid Folding and Unfolding of Apaf-1 CARD Structure of the Absent in Melanoma 2 (AIM2) Pyrin Domain Provides Insights into the Mechanisms of AIM2 Autoinhibition and Inflammasome Assembly Nod2: A Critical Regulator of Ileal Microbiota and Crohn's Disease Requirement of IFI16 for the maximal activation of p53 induced by ionizing radiation The PYRIN domain in signal transduction Co-regulation of NF-kappaB and inflammasome-mediated inflammatory responses by myxoma virus pyrin domain-containing protein M013 Inhibiting the inflammasome: one domain at a time Uncoupling of Pyrin-only protein 2 (POP2)-mediated dual regulation of NF-κB and the inflammasome Complex and dynamic redistribution of NF-kappaB signaling intermediates in response to T cell receptor stimulation Automated protein structure modeling with SWISS-MODEL Workspace and the Protein Model Portal.Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3.Functional screening of five PYPAF family members identifies PYPAF5 as a novel regulator of NF-kappaB and caspase-1.Nod2: a key regulator linking microbiota to intestinal mucosal immunity.PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-kappaB and caspase-1 activation in macrophages.The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1beta production An updated view on the structure and function of PYRIN domains.N-terminal and C-terminal domains of calmodulin mediate FADD and TRADD interaction The protein structures that shape caspase activity, specificity, activation and inhibition.Proteomic characterization of skin and epidermis in response to environmental agents.Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICK NLR proteins: integral members of innate immunity and mediators of inflammatory diseases.Muramyl dipeptide and its derivatives: peptide adjuvant in immunological disorders and cancer therapy.High frequency of inherited variants in the MEFV gene in patients with hematologic neoplasms: a genetic susceptibility?Structure and function of the SPRY/B30.2 domain proteins involved in innate immunity.The tumor necrosis factor alpha-dependent activation of the human mediterranean fever (MEFV) promoter is mediated by a synergistic interaction between C/EBP beta and NF kappaB p65.Myeloid nuclear differentiation antigen, neutrophil apoptosis and sepsis The SPRY domain of Pyrin, mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing.Human Antiviral Protein IFIX Suppresses Viral Gene Expression during Herpes Simplex Virus 1 (HSV-1) Infection and Is Counteracted by Virus-induced Proteasomal Degradation.Association of mutations in the NALP3/CIAS1/PYPAF1 gene with a broad phenotype including recurrent fever, cold sensitivity, sensorineural deafness, and AA amyloidosis.Homology modeling provides insights into the binding mode of the PAAD/DAPIN/pyrin domain, a fourth member of the CARD/DD/DED domain family.Structural localization of disease-associated sequence variations in the NACHT and LRR domains of PYPAF1 and NOD2.Caspy, a zebrafish caspase, activated by ASC oligomerization is required for pharyngeal arch development.Kinetic traps in the folding/unfolding of procaspase-1 CARD domain.

P2860

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P2860

The PYRIN domain: a member of the death domain-fold superfamily

http://www.wikidata.org/entity/Q24644648

description

2001 nî lūn-bûn

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2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2001年の論文

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2001年論文

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2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

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2001年论文

@wuu

name

The PYRIN domain: a member of the death domain-fold superfamily

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The PYRIN domain: a member of the death domain-fold superfamily

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The PYRIN domain: a member of the death domain-fold superfamily

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type

label

The PYRIN domain: a member of the death domain-fold superfamily

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The PYRIN domain: a member of the death domain-fold superfamily

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The PYRIN domain: a member of the death domain-fold superfamily

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prefLabel

The PYRIN domain: a member of the death domain-fold superfamily

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The PYRIN domain: a member of the death domain-fold superfamily

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The PYRIN domain: a member of the death domain-fold superfamily

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Protein Science

P1476

The PYRIN domain: a member of the death domain-fold superfamily

@en

P2093

E W Humke

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

J P Yin

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

K M O'Rourke

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

M A Starovasnik

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

N C Gordon

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

V M Dixit

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

W J Fairbrother

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

P2860

Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-kappaB

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

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

ICEBERG: a novel inhibitor of interleukin-1beta generation

Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins

A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain

FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis

CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP

Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3

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1911-8

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

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scholarly article

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3435724

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P356

10.1110/PS.13801

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P407

P433

9

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10

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2001-09-01T00:00:00Z

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P5875

11830286

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11514682

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2253208

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