Evidence map›Paper›PMID 31152698›Full record

ReviewArchives of biochemistry and biophysics2019

Structure, interactions and self-assembly of ASC-dependent inflammasomes.

Eva de Alba

Open access · greenAbstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

45 citing papers in PubMed, 1 synthesis or guideline pooled it, 72 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Eva de AlbaDepartment of Bioengineering. School of Engineering. University of California, Merced, 5200 North Lake Road, Merced, CA, 95343, USA. Electronic address: edealbabastarrechea@ucmerced.edu.
University of California, Merced · US

Funding

800 MHz NMR Spectrometer and Helium CryoprobeS10OD018455 · OD · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI MILLHAUSER, GLENN L · 2015 to 2015
$2.0M
Molecular Bases of Inflammasome Regulation Mediated by ASC IsoformsR15AI146780 · NIAID · UNIVERSITY OF CALIFORNIA, MERCED · PI DE ALBA BASTARRECHEA, EVA · 2019 to 2020
$580k
NIAID NIH HHS R15 AI146780NIH HHS S10 OD018455
6 · The paper itself

Abstract

The inflammasome is a multi-protein platform that assembles upon the presence of cues derived from infection or tissue damage, and triggers the inflammatory response. Inflammasome components include sensor proteins that detect danger signals, procaspase 1 and the adapter ASC (apoptosis-associated speck-like protein containing a CARD) tethering these molecules together. Upon inflammasome assembly, procaspase 1 self-activates and renders functional cytokines to arbitrate in the defense mechanism. This assembly is mediated by self-association and protein interactions via Death Domains. The inflammasome plays a critical role in innate immunity and its dysregulation is the culprit of many autoimmune disorders. An in-depth understanding of the factors involved in inflammasome assembly could help fight these conditions. This review describes our current knowledge on the biophysical aspects of inflammasome formation from the perspective of ASC. The specific characteristics of the three-dimensional solution structure and interdomain dynamics of ASC are explained in relation to its function in inflammasome assembly. Additionally, the review elaborates on the identification of ASC interacting surfaces at the amino acid level using NMR techniques. Finally, the macrostructures formed by full-length ASC and its two Death Domains studied with Transmission Electron Microscopy are compared in the context of a directional model for inflammasome assembly.

Indexed as

AnimalsCARD Signaling Adaptor ProteinsHumansInflammasomesProtein AggregatesProtein DomainsCARD Signaling Adaptor ProteinsInflammasomesProtein AggregatesASCDeath domainInflammasomeInflammasome adapterInflammationInnate immunityNLRP3NMRProtein assemblyPYD CARDTEM

Identifiers

PMID31152698
PMCPMC8455077
OpenAlexW2947234709

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.