Evidence map›Paper›PMID 39760245›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2025

Hsf1 is essential for proteotoxic stress response in smyd1b-deficient embryos and fish survival under heat shock.

Huanhuan Xiao, Mofei Li, Yongwang Zhong, Avani Patel, Rui Xu, Chenyu Zhang, Thomas W Athey, Shengyun Fang, Tianjun Xu, Shaojun Du

Abstract read
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In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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

10 authors.

Huanhuan XiaoDepartment of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, Maryland, USA.ORCID 0009-0003-9114-1561
Mofei LiDepartment of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, Maryland, USA.ORCID 0000-0001-5029-1502
Yongwang ZhongDepartment of Physiology, Center for Biomedical Engineering, University of Maryland School of Medicine, Baltimore, Maryland, USA.ORCID 0009-0009-0994-4730
Avani PatelDepartment of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, Maryland, USA.ORCID 0009-0000-3258-0319
Rui XuDepartment of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, Maryland, USA.ORCID 0009-0009-2777-0391
Chenyu ZhangDepartment of Pathology, University of Maryland School of Medicine, Baltimore, Maryland, USA.ORCID 0009-0003-3030-3328
Thomas W AtheyDepartment of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, Maryland, USA.ORCID 0000-0002-2514-7389
Shengyun FangDepartment of Physiology, Center for Biomedical Engineering, University of Maryland School of Medicine, Baltimore, Maryland, USA.ORCID 0000-0001-7280-5463
Tianjun XuDepartment of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, Maryland, USA.ORCID 0000-0003-3606-8069
Shaojun DuDepartment of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, Maryland, USA.ORCID 0000-0001-9227-4153

Funding

Molecular regulation of muscle development by Smyd1R01AR072703 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI DU, SHAOJUN · 2018 to 2023
$1.7M
China Scholarship Council (CSC)HHS | NIH | National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS) R01AR072703NIAMS NIH HHS R01 AR072703
6 · The paper itself

Abstract

Molecular chaperones play critical roles in post-translational maintenance in protein homeostasis. Previous studies have shown that loss of Smyd1b function results in defective myofibril organization and dramatic upregulation of heat shock protein gene (hsp) expression in muscle cells of zebrafish embryos. To investigate the molecular mechanisms and functional importance of this stress response, we characterized changes of gene expression in smyd1b knockdown and knockout embryos using RNA-seq. The results showed that the top upregulated genes encode mostly cytosolic heat shock proteins. Co-IP assay revealed that the upregulated cytosolic Hsp70s associate with myosin chaperone UNC45b which is critical for myosin protein folding and sarcomere assembly. Strikingly, several hsp70 genes also display muscle-specific upregulation in response to heat shock-induced stress in zebrafish embryos. To investigate the regulation of hsp gene upregulation and its functional significance in muscle cells, we generated heat shock factor 1 (hsf

Indexed as

Heat-Shock ResponseZebrafishZebrafish ProteinsAnimalsEmbryo, NonmammalianGene Expression Regulation, DevelopmentalHeat Shock Transcription FactorsHSP70 Heat-Shock ProteinsMuscle ProteinsProteotoxic StressHeat Shock Transcription FactorsHSP70 Heat-Shock ProteinsMuscle ProteinsUnc45b protein, zebrafishZebrafish Proteinsheat shock factor 1heat shock proteinmyofibrilSmyd1bstress response

Identifiers

PMID39760245
PMCPMC11740226

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Registered trials

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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.