Proteolytic processing of Nlrp1b is required for inflammasome activity.
about
Biochemical and structural aspects of the ATP-binding domain in inflammasome-forming human NLRP proteinsAn Update on PYRIN Domain-Containing Pattern Recognition Receptors: From Immunity to PathologyMechanisms of inflammasome activation: recent advances and novel insightsRecognition of Extracellular Bacteria by NLRs and Its Role in the Development of Adaptive ImmunityPolicing the cytosol--bacterial-sensing inflammasome receptors and pathwaysThe cell biology of inflammasomes: Mechanisms of inflammasome activation and regulationLinear ubiquitination in immunityActivation of the Nlrp1b inflammasome by reduction of cytosolic ATPNLRP1-dependent pyroptosis leads to acute lung injury and morbidity in miceActivation and regulation of the inflammasomesDistinct regions of NLRP1B are required to respond to anthrax lethal toxin and metabolic inhibition.Beyond canonical inflammasomes: emerging pathways in IL-1-mediated autoinflammatory diseaseBoth lethal and edema toxins of Bacillus anthracis disrupt the human dendritic cell chemokine network.Anthrax lethal factor cleaves mouse nlrp1b in both toxin-sensitive and toxin-resistant macrophages.Inflammasomes as polyvalent cell death platforms.Transcriptional analysis of the three Nlrp1 paralogs in mice.Direct proteolytic cleavage of NLRP1B is necessary and sufficient for inflammasome activation by anthrax lethal factor.Regulation of inflammasome activation.Autolytic proteolysis within the function to find domain (FIIND) is required for NLRP1 inflammasome activity.Functional and Evolutionary Analyses Identify Proteolysis as a General Mechanism for NLRP1 Inflammasome Activation.Functions of NOD-Like Receptors in Human Diseases.New insights into mechanisms controlling the NLRP3 inflammasome and its role in lung disease.Anthrax lethal toxin inhibits translation of hypoxia-inducible factor 1α and causes decreased tolerance to hypoxic stressActivation of the NLRP1b inflammasome independently of ASC-mediated caspase-1 autoproteolysis and speck formationRegulation where autophagy intersects the inflammasome.Mechanisms of NOD-like receptor-associated inflammasome activation.General Strategies in Inflammasome Biology.The NLRP3 and Pyrin Inflammasomes: Implications in the Pathophysiology of Autoinflammatory Diseases.Mechanisms governing inflammasome activation, assembly and pyroptosis induction.Anthrax lethal toxin rapidly reduces c-Jun levels by inhibiting c-Jun gene transcription and promoting c-Jun protein degradation.Listeria monocytogenes and Shigella flexneri activate the NLRP1B inflammasome.Multiple Cathepsins Promote Pro-IL-1β Synthesis and NLRP3-Mediated IL-1β ActivationInflammasome activation and assembly at a glance.Inhibition of Dpp8/9 Activates the Nlrp1b Inflammasome.
P2860
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P2860
Proteolytic processing of Nlrp1b is required for inflammasome activity.
description
2012 nî lūn-bûn
@nan
2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
name
Proteolytic processing of Nlrp1b is required for inflammasome activity.
@ast
Proteolytic processing of Nlrp1b is required for inflammasome activity.
@en
Proteolytic processing of Nlrp1b is required for inflammasome activity.
@nl
type
label
Proteolytic processing of Nlrp1b is required for inflammasome activity.
@ast
Proteolytic processing of Nlrp1b is required for inflammasome activity.
@en
Proteolytic processing of Nlrp1b is required for inflammasome activity.
@nl
prefLabel
Proteolytic processing of Nlrp1b is required for inflammasome activity.
@ast
Proteolytic processing of Nlrp1b is required for inflammasome activity.
@en
Proteolytic processing of Nlrp1b is required for inflammasome activity.
@nl
P2093
P2860
P1433
P1476
Proteolytic processing of Nlrp1b is required for inflammasome activity.
@en
P2093
Bradley C Frew
Jeremy Mogridge
Vineet R Joag
P2860
P304
P356
10.1371/JOURNAL.PPAT.1002659
P577
2012-04-19T00:00:00Z