Autolytic proteolysis within the function to find domain (FIIND) is required for NLRP1 inflammasome activity. - Wikidata - awgldk - TriplyDB

Autolytic proteolysis within the function to find domain (FIIND) is required for NLRP1 inflammasome activity.

Autolytic proteolysis within the function to find domain (FIIND) is required for NLRP1 inflammasome activity.

http://www.wikidata.org/entity/Q36127206

about

Biochemical and structural aspects of the ATP-binding domain in inflammasome-forming human NLRP proteins An Update on PYRIN Domain-Containing Pattern Recognition Receptors: From Immunity to Pathology A clear and present danger: inflammasomes DAMPing down disorders of pregnancy Pyroptotic cell death defends against intracellular pathogens The cell biology of inflammasomes: Mechanisms of inflammasome activation and regulation International Union of Basic and Clinical Pharmacology. XCVI. Pattern recognition receptors in health and disease The Biophysical Characterisation and SAXS Analysis of Human NLRP1 Uncover a New Level of Complexity of NLR Proteins Activation and regulation of the inflammasomes Distinct regions of NLRP1B are required to respond to anthrax lethal toxin and metabolic inhibition.An ancient autoproteolytic domain found in GAIN, ZU5 and Nucleoporin98 NLRP1 inflammasome activation induces pyroptosis of hematopoietic progenitor cells.Direct proteolytic cleavage of NLRP1B is necessary and sufficient for inflammasome activation by anthrax lethal factor.Emerging significance of NLRs in inflammatory bowel disease.Regulation of inflammasome activation.Functional and Evolutionary Analyses Identify Proteolysis as a General Mechanism for NLRP1 Inflammasome Activation.NLRP1 haplotypes associated with vitiligo and autoimmunity increase interleukin-1β processing via the NLRP1 inflammasome New insights into mechanisms controlling the NLRP3 inflammasome and its role in lung disease.NLRP1 is an inflammasome sensor for Toxoplasma gondii.Activation and regulation of cellular inflammasomes: gaps in our knowledge for central nervous system injury.A Biologically-Based Computational Approach to Drug Repurposing for Anthrax Infection.Mechanisms of NOD-like receptor-associated inflammasome activation.Pattern recognition receptors and central nervous system repair.NLR-regulated pathways in cancer: opportunities and obstacles for therapeutic interventions.Evasion and interference: intracellular pathogens modulate caspase-dependent inflammatory responses.General Strategies in Inflammasome Biology.Intracellular innate immune surveillance devices in plants and animals.NLRP3 inflammasome: Its regulation and involvement in atherosclerosis.Posttranslational Modification as a Critical Determinant of Cytoplasmic Innate Immune Recognition.Listeria monocytogenes and Shigella flexneri activate the NLRP1B inflammasome.Associations of interactions between NLRP3 SNPs and HLA mismatch with acute and extensive chronic graft-versus-host diseases.Multiple Cathepsins Promote Pro-IL-1β Synthesis and NLRP3-Mediated IL-1β Activation NLRP1 Overexpression Is Correlated with the Tumorigenesis and Proliferation of Human Breast Tumor.Regulation and Sensing of Inflammasomes and Their Impact on Intestinal Health.Inflammasome activation and assembly at a glance.Inflammasomes, the eye and anti-inflammasome therapy.Inhibition of Dpp8/9 Activates the Nlrp1b Inflammasome.Inflammatory cell death in intestinal pathologies.The Canonical Inflammasome: A Macromolecular Complex Driving Inflammation.Novel aspects of the assembly and activation of inflammasomes with focus on the NLRC4 inflammasome.The Emerging Role of Inflammasomes as Central Mediators in Inflammatory Bladder Pathology.

P2860

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P2860

Autolytic proteolysis within the function to find domain (FIIND) is required for NLRP1 inflammasome activity.

http://www.wikidata.org/entity/Q36127206

description

2012 nî lūn-bûn

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Autolytic proteolysis within t ...... r NLRP1 inflammasome activity.

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Autolytic proteolysis within t ...... r NLRP1 inflammasome activity.

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Autolytic proteolysis within t ...... r NLRP1 inflammasome activity.

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Autolytic proteolysis within t ...... r NLRP1 inflammasome activity.

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Autolytic proteolysis within t ...... r NLRP1 inflammasome activity.

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Autolytic proteolysis within t ...... r NLRP1 inflammasome activity.

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JBC.M112.378323

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Journal of Biological Chemistry

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Autolytic proteolysis within t ...... r NLRP1 inflammasome activity.

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P2093

Chaya Duraiswami

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John Bertin

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John D Lich

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Joshua N Finger

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Kristin K Brown

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Lauren C Dare

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Michael N Cook

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Peter J Gough

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P2860

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

Human CARD12 is a novel CED4/Apaf-1 family member that induces apoptosis

Identification of Ipaf, a human caspase-1-activating protein related to Apaf-1

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

CATERPILLER: a novel gene family important in immunity, cell death, and diseases

The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta

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

Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway

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

Inflammasomes: too big to miss

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25030-25037

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10.1074/JBC.M112.378323

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30

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287

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22665479

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3408201

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