Evidence map›Paper›PMID 29791979›Full record

ArticleThe FEBS journal2018

Functional and structural characterization of zebrafish ASC.

Yajuan Li, Yi Huang, Xiaocong Cao, Xueying Yin, Xiangyu Jin, Sheng Liu, Jiansheng Jiang, Wei Jiang, Tsan Sam Xiao, Rongbin Zhou and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

12 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  3. Is Zebrafish a Good Model for the Alpha-Gal Syndrome?FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
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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

13 authors at 3 institutions in 2 countries.

Yajuan LiLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, China.
Yi HuangLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, China.
Xiaocong CaoLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, China.
Xueying YinLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, China.
Xiangyu JinLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, China.
Sheng LiuLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, China.
Jiansheng JiangLaboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.
Wei JiangLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, China.
Tsan Sam XiaoDepartment of Pathology, Case Western Reserve University, Cleveland, OH, USA.
Rongbin ZhouLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, China.
Gang CaiLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, China.
Bing HuLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, China.
Tengchuan JinLaboratory of Structural Immunology, CAS Key Laboratory of Innate Immunity and Chronic Disease, School of Life Sciences and Medical Center, University of Science and Technology of China, Hefei, China.ORCID 0000-0002-1395-188X
University of Science and Technology of China · CNCase Western Reserve University · USNational Institutes of Health · US

Funding

Molecular mechanisms of gasdermins and pyroptosisR01GM127609 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI XIAO, TSAN SAM · 2018 to 2021
$1.4M
Developing chemical probes that target specific inflammasomesR21AR069908 · NIAMS · CASE WESTERN RESERVE UNIVERSITY · PI XIAO, TSAN SAM · 2016 to 2017
$384k
NIAMS NIH HHS R21 AR069908NIGMS NIH HHS R01 GM127609
6 · The paper itself

Abstract

The zebrafish genome encodes homologs for most of the proteins involved in inflammatory pathways; however, the molecular components and activation mechanisms of fish inflammasomes are largely unknown. ASC [apoptosis-associated speck-like protein containing a caspase-recruitment domain (CARD)] is the only adaptor involved in the formation of multiple types of inflammasomes. Here, we demonstrate that zASC is also involved in inflammasome activation in zebrafish. When overexpressed in vitro and in vivo in zebrafish, both the zASC and zASC pyrin domain (PYD) proteins form speck and filament structures. Importantly, the crystal structures of the N-terminal PYD and C-terminal CARD of zebrafish ASC were determined independently as two separate entities fused to maltose-binding protein. Structure-guided mutagenesis revealed the functional relevance of the PYD hydrophilic surface found in the crystal lattice. Finally, the fish caspase-1 homolog Caspy, but not the caspase-4/11 homolog Caspy2, interacts with zASC through homotypic PYD-PYD interactions, which differ from those in mammals. These observations establish the conserved and unique structural/functional features of the zASC-dependent inflammasome pathway. DATABASE: Structural data are available in the PDB under accession numbers 5GPP and 5GPQ.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCaspasesCloning, MolecularCrystallography, X-RayCytoskeletal ProteinsEscherichia coliGene ExpressionGenetic VectorsGillsHydrophobic and Hydrophilic InteractionsInflammasomesIntestinesMaltose-Binding ProteinsModels, Molecularcaspa protein, zebrafishCaspasesCytoskeletal ProteinsInflammasomesMaltose-Binding Proteinspycard protein, zebrafishRecombinant Fusion ProteinsZebrafish ProteinsASCcaspase-1inflammasomePYDzebrafish

Identifiers

PMID29791979
PMCPMC6105367
OpenAlexW2803817356

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.