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The Pyrin Inflammasome in Health and Disease [PDF]

open access: yesFrontiers in Immunology, 2019
The pyrin inflammasome has evolved as an innate immune sensor to detect bacterial toxin-induced Rho guanosine triphosphatase (Rho GTPase)-inactivation, a process that is similar to the “guard” mechanism in plants. Rho GTPases act as molecular switches to
Oskar Schnappauf   +2 more
exaly   +6 more sources

Update on Pyrin Functions and Mechanisms of Familial Mediterranean Fever [PDF]

open access: yesFrontiers in Microbiology, 2016
Mutations in the MEFV gene, which encodes the protein named pyrin (also called marenostrin or TRIM20), are associated with the autoinflammatory disease familial Mediterranean fever (FMF).
Gayane Manukyan   +2 more
exaly   +6 more sources

Pyrin Modulates the Intracellular Distribution of PSTPIP1. [PDF]

open access: yesPLoS ONE, 2009
PSTPIP1 is a cytoskeleton-associated adaptor protein that links PEST-type phosphatases to their substrates. Mutations in PSTPIP1 cause PAPA syndrome (Pyogenic sterile Arthritis, Pyoderma gangrenosum, and Acne), an autoinflammatory disease.
Andrea L Waite   +11 more
doaj   +9 more sources

The pyrin inflammasome, a leading actor in pediatric autoinflammatory diseases

open access: yesFrontiers in Immunology, 2023
The activation of the pyrin inflammasome represents a highly intriguing mechanism employed by the innate immune system to effectively counteract pathogenic agents. Despite its key role in innate immunity, pyrin has also garnered significant attention due
Saverio La Bella   +2 more
exaly   +4 more sources

Pyrin- and CARD-only Proteins as Regulators of NLR Functions [PDF]

open access: yesFrontiers in Immunology, 2013
Upon activation Nod-like receptors (NLRs) assemble into multi-protein complexes such as the NODosome and inflammasome. This process relies upon homo-domain interactions between the structurally related Pyrin and caspase-recruitment (CARD) domains and ...
Hongnga T Le   +2 more
exaly   +5 more sources

Identification of Multifaceted Binding Modes for Pyrin and ASC Pyrin Domains Gives Insights into Pyrin Inflammasome Assembly [PDF]

open access: yesJournal of Biological Chemistry, 2014
Inflammasomes are macromolecular complexes that mediate inflammatory and cell death responses to pathogens and cellular stress signals. Dysregulated inflammasome activation is associated with autoinflammatory syndromes and several common diseases. During inflammasome assembly, oligomerized cytosolic pattern recognition receptors recruit procaspase-1 ...
Vajjhala, Parimala R.   +6 more
openaire   +7 more sources

Function and mechanism of the pyrin inflammasome [PDF]

open access: yesEuropean Journal of Immunology, 2017
AbstractPyrin, encoded by the MEFV gene, is an intracellular pattern recognition receptor that assembles inflammasome complexes in response to pathogen infections. Mutations in the MEFV gene have been linked to autoinflammatory diseases such as familial Mediterranean fever (FMF) or pyrin‐associated autoinflammation with neutrophilic dermatosis (PAAND).
Rosalie Heilig, Petr Broz
openaire   +5 more sources

Folding Pyrin into the Family [PDF]

open access: yesStructure, 2003
AbstractThe first structure of a pyrin domain confirms its membership in the death domain superfamily, reveals a local unfolding of the third of six helices, and suggests that the folding/unfolding transition of this helix may be an important determinant of the function and disease related dysfunction of this domain.
David Eliezer, Eliezer, David
openaire   +2 more sources

Phosphoprotein phosphatase activity positively regulates oligomeric pyrin to trigger inflammasome assembly in phagocytes

open access: yesmBio, 2023
Pyrin is a pattern-recognition receptor in phagocytes that triggers caspase-1 inflammasome assembly in response to bacterial toxins and effectors that inactivate RhoA.
Haleema S. Malik   +6 more
doaj   +2 more sources

The Yersinia pestis Effector YopM Inhibits Pyrin Inflammasome Activation. [PDF]

open access: yesPLoS Pathogens, 2016
Type III secretion systems (T3SS) are central virulence factors for many pathogenic Gram-negative bacteria, and secreted T3SS effectors can block key aspects of host cell signaling.
Dmitry Ratner   +12 more
doaj   +4 more sources

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