Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The Inflammasome Adaptor ASC Induces Procaspase-8 Death Effector Domain Filaments.

The Journal of biological chemistry - 4 Dec 2015

Vajjhala Parimala R, Lu Alvin, Brown Darren L, Pang Siew Wai, Sagulenko Vitaliya, Sester David P, Cridland Simon O, Hill Justine M, Schroder Kate, Stow Jennifer L, Wu Hao, Stacey Katryn J

Abstract excerpt

Inflammasomes mediate inflammatory and cell death responses to pathogens and cellular stress signals via activation of procaspases-1 and -8. During inflammasome assembly, activated receptors of the NLR or PYHIN family recruit the adaptor protein ASC and initiate polymerization of its pyrin domain (PYD) into filaments. We show that ASC filaments in turn nucleate procaspase-8 death effector domain (DED) filaments...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to CARD Signaling Adaptor Proteins
Share to Caspase 1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Caspase 8

Share to Catalytic Domain

Share to Cell Death

Share to Cytoskeletal Proteins

Share to Inflammasomes

Share to Microscopy, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 26468282
DOI: 10.1074/jbc.M115.687731
PMCID: PMC4705927

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Inflammasome Adaptor ASC Induces Procaspase-8 Death Effector Domain Filaments.PMID 26468282Read ↗

ASC filament formation serves as a signal amplification mechanism for inflammasomes.Semantic proximity Read ↗

Identification of Multifaceted Binding Modes for Pyrin and ASC Pyrin Domains Gives Insights into Pyrin Inflammasome AssemblySemantic proximity Read ↗

Distinct interaction modes orchestrate the polymerization of ASC PYD and CARD domains into filamentous structures.Semantic proximity Read ↗

Structural basis for distinct inflammasome complex assembly by human NLRP1 and CARD8.Semantic proximity Read ↗

Distinct axial and lateral interactions within homologous filaments dictate the signaling specificity and order of the AIM2-ASC inflammasome.Semantic proximity Read ↗

Dynamics of in vivo ASC speck formation.Semantic proximity Read ↗

Pyrin activates the ASC pyroptosome in response to engagement by autoinflammatory PSTPIP1 mutants.Semantic proximity Read ↗

L-plastin enhances NLRP3 inflammasome assembly and bleomycin-induced lung fibrosisSemantic proximity Read ↗

Biochemical and structural aspects of the ATP‐binding domain in inflammasome‐forming human NLRP proteinsSemantic proximity Read ↗

The inflammasome adaptor protein ASC promotes amyloid deposition in Cryopyrin-associated Periodic SyndromesSemantic proximity Read ↗

C-terminal lysine residues localise NLRP10 at lipid compartments and govern NLRP10 oligomer formationSemantic proximity Read ↗

The pyrin domain of IFI16 forms a distinct filament structure important for IFI16-mediated enhancement of STING activation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.