Direct Proteolytic Cleavage of NLRP1B Is Necessary and Sufficient for Inflammasome Activation by Anthrax Lethal Factor
Published 2013 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Direct Proteolytic Cleavage of NLRP1B Is Necessary and Sufficient for Inflammasome Activation by Anthrax Lethal Factor
Authors
Keywords
-
Journal
PLoS Pathogens
Volume 9, Issue 6, Pages e1003452
Publisher
Public Library of Science (PLoS)
Online
2013-07-17
DOI
10.1371/journal.ppat.1003452
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Manipulation of small Rho GTPases is a pathogen-induced process detected by NOD1
- (2013) A. Marijke Keestra et al. NATURE
- Recognition of Bacteria by Inflammasomes
- (2012) Jakob von Moltke et al. Annual Review of Immunology
- Activation of the Nlrp1b Inflammasome by Reduction of Cytosolic ATP
- (2012) Kuo-Chieh Liao et al. INFECTION AND IMMUNITY
- Autolytic Proteolysis within the Function to Find Domain (FIIND) Is Required for NLRP1 Inflammasome Activity
- (2012) Joshua N. Finger et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Rapid induction of inflammatory lipid mediators by the inflammasome in vivo
- (2012) Jakob von Moltke et al. NATURE
- Anthrax Lethal Factor Cleaves Mouse Nlrp1b in Both Toxin-Sensitive and Toxin-Resistant Macrophages
- (2012) Kristina A. Hellmich et al. PLoS One
- Proteolytic Processing of Nlrp1b Is Required for Inflammasome Activity
- (2012) Bradley C. Frew et al. PLoS Pathogens
- Anthrax Lethal Factor Cleavage of Nlrp1 Is Required for Activation of the Inflammasome
- (2012) Jonathan L. Levinsohn et al. PLoS Pathogens
- Proteases as regulators of pathogenesis: Examples from the Apicomplexa
- (2011) Hao Li et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- Cysteine Protease Inhibitors: from Evolutionary Relationships to Modern Chemotherapeutic Design for the Treatment of Infectious Diseases
- (2011) E. C.Y. Toh et al. CURRENT PROTEIN & PEPTIDE SCIENCE
- Anthrax Toxin Induces Macrophage Death by p38 MAPK Inhibition but Leads to Inflammasome Activation via ATP Leakage
- (2011) Syed Raza Ali et al. IMMUNITY
- Pathogen-Derived Effectors Trigger Protective Immunity via Activation of the Rac2 Enzyme and the IMD or Rip Kinase Signaling Pathway
- (2011) Laurent Boyer et al. IMMUNITY
- The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus
- (2011) Yue Zhao et al. NATURE
- Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity
- (2011) Eric M. Kofoed et al. NATURE
- CARD8 and NLRP1 Undergo Autoproteolytic Processing through a ZU5-Like Domain
- (2011) Andrea D'Osualdo et al. PLoS One
- Secreted Bacterial Effectors That Inhibit Host Protein Synthesis Are Critical for Induction of the Innate Immune Response to Virulent Legionella pneumophila
- (2011) Mary F. Fontana et al. PLoS Pathogens
- Pattern Recognition Receptors and Inflammation
- (2010) Osamu Takeuchi et al. CELL
- Influenza virus activates inflammasomes via its intracellular M2 ion channel
- (2010) Takeshi Ichinohe et al. NATURE IMMUNOLOGY
- Inflammasome Sensor Nlrp1b-Dependent Resistance to Anthrax Is Mediated by Caspase-1, IL-1 Signaling and Neutrophil Recruitment
- (2010) Mahtab Moayeri et al. PLoS Pathogens
- Susceptibility to Anthrax Lethal Toxin-Induced Rat Death Is Controlled by a Single Chromosome 10 Locus That Includes rNlrp1
- (2010) Zachary L. Newman et al. PLoS Pathogens
- Patterns of Pathogenesis: Discrimination of Pathogenic and Nonpathogenic Microbes by the Innate Immune System
- (2009) Russell E. Vance et al. Cell Host & Microbe
- Expression of Nlrp1b Inflammasome Components in Human Fibroblasts Confers Susceptibility to Anthrax Lethal Toxin
- (2009) K.-C. Liao et al. INFECTION AND IMMUNITY
- Substrate Recognition of Anthrax Lethal Factor Examined by Combinatorial and Pre-steady-state Kinetic Approaches
- (2009) Maria Yu. Zakharova et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Cutting Edge: Resistance to Bacillus anthracis Infection Mediated by a Lethal Toxin Sensitive Allele of Nalp1b/Nlrp1b
- (2009) Jill K. Terra et al. JOURNAL OF IMMUNOLOGY
- AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
- (2009) Teresa Fernandes-Alnemri et al. NATURE
- AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
- (2009) Veit Hornung et al. NATURE
- An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome
- (2009) Tilmann Bürckstümmer et al. NATURE IMMUNOLOGY
- Pyroptosis: host cell death and inflammation
- (2009) Tessa Bergsbaken et al. NATURE REVIEWS MICROBIOLOGY
- HIN-200 Proteins Regulate Caspase Activation in Response to Foreign Cytoplasmic DNA
- (2009) T. L. Roberts et al. SCIENCE
- Killing of macrophages by anthrax lethal toxin: involvement of the N-end rule pathway
- (2008) Katherine E. Wickliffe et al. CELLULAR MICROBIOLOGY
- The NLR Gene Family: A Standard Nomenclature
- (2008) Jenny P.-Y. Ting et al. IMMUNITY
- Corruption of Innate Immunity by Bacterial Proteases
- (2008) Jan Potempa et al. Journal of Innate Immunity
- Critical function for Naip5 in inflammasome activation by a conserved carboxy-terminal domain of flagellin
- (2008) Karla L Lightfield et al. NATURE IMMUNOLOGY
- From Guard to Decoy: A New Model for Perception of Plant Pathogen Effectors
- (2008) R. A.L. van der Hoorn et al. PLANT CELL
- Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms
- (2008) S. L. Fink et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Type IV Secretion-Dependent Activation of Host MAP Kinases Induces an Increased Proinflammatory Cytokine Response to Legionella pneumophila
- (2008) Sunny Shin et al. PLoS Pathogens
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationBecome a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get Started