OSCR

YTHDC1 functions as a molecular chaperone to suppress ALS-linked hnRNPA1 mutants from aggregation.

Overview

Authors: Kang Ren1, Mingjie Cheng2, Qiudan Luo1, Boxin Zhang3, Haosheng Zhang2, Zhe Li1, Yuxin Liu1, Yujie Wang1, Ting Kang1, Xiaoming Dai1,4, Jiong Chen3, Yuanming Cheng2,4, Liangqian Huang1,4
ORCID iDs: Kang Ren, Xiaoming Dai, Jiong Chen, Liangqian Huang
  1. Institute of Modern Biology, Department of Neurosurgery, Affiliated Nanjing Drum Tower Hospital, Nanjing University, Nanjing, Jiangsu China
  2. Institute of Modern Biology, Department of Hematology, Affiliated Nanjing Drum Tower Hospital, Nanjing University, Nanjing, Jiangsu China
  3. MOE Key Laboratory of Model Animals for Disease Study, Jiangsu Key Laboratory of Molecular Medicine, Model Animal Research Center, Medical School of Nanjing University, Nanjing, Jiangsu China
  4. State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing, Jiangsu China
Institutions: Nanjing Drum Tower Hospital (China); Nanjing University (China); Model Animal Research Center (China); State Key Laboratory of Pharmaceutical Biotechnology
Journal: Nature communications, volume 17, issue 1, article 9357
Dates: received 18 January 2026; accepted 7 August 2026; published online 21 August 2026
Type: Research article · Language: English
License: CC BY-NC-ND
Identifiers: DOI 10.1038/s41467-026-77016-y · PMID 42680774 · PMCID PMC13534550 · OpenAlex W7203903238
Open access: gold, a free copy (OpenAlex)
Status: data only
Categories: human (organism), other condition (population), cellular / molecular (subfield)
Methods: Statistics, Evoked potentials, Graphs
Keywords: Chaperones, Protein aggregation, Amyotrophic lateral sclerosis
MeSH: Amyotrophic Lateral Sclerosis*, Heterogeneous Nuclear Ribonucleoprotein A1*, Molecular Chaperones*, Nerve Tissue Proteins*, Animals, Humans, Mutation, Neurons, Protein Aggregates, Protein Aggregation, Pathological, Protein Folding (* major topic)
Topic: RNA modifications and cancer (Molecular Biology, Biochemistry, Genetics and Molecular Biology), according to OpenAlex
Funding: National Natural Science Foundation of China (32300651, 82370182)
Citations: not cited yet (Europe PMC); 51 references in the paper

Abstract

The abstract is not reproduced here: the paper's license (CC BY-NC-ND) does not allow it. Read it in the paper, at the publisher or on Europe PMC.

Code

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Data

Datasets cited

Data availability statement

The paper has a data availability statement. Its license (CC BY-NC-ND) does not allow reproducing it here; in short, from what the harvester recognized in it:

Read it in the paper: doi.org/10.1038/s41467-026-77016-y.

Versions

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Version 1, 27 September 2026: the first record

Recorded: type, language, journal, volume, issue, pages, dates, 13 authors, 3 keywords, 11 MeSH terms, 1 funder, 51 references.

Cite

This paper

Ren, K., Cheng, M., Luo, Q., Zhang, B., Zhang, H., Li, Z., Liu, Y., Wang, Y., Kang, T., Dai, X., Chen, J., Cheng, Y., & Huang, L. (2026). YTHDC1 functions as a molecular chaperone to suppress ALS-linked hnRNPA1 mutants from aggregation. Nature communications, 17(1), 9357. https://doi.org/10.1038/s41467-026-77016-y

BibTeX

@article{ren2026ythdc1,
author = {Ren, Kang and Cheng, Mingjie and Luo, Qiudan and Zhang, Boxin and Zhang, Haosheng and Li, Zhe and Liu, Yuxin and Wang, Yujie and Kang, Ting and Dai, Xiaoming and Chen, Jiong and Cheng, Yuanming and Huang, Liangqian},
title = {{YTHDC1 functions as a molecular chaperone to suppress ALS-linked hnRNPA1 mutants from aggregation}},
journal = {Nature communications},
year = {2026},
month = aug,
volume = {17},
number = {1},
pages = {9357},
publisher = {Nature Publishing Group},
issn = {2041-1723},
doi = {10.1038/s41467-026-77016-y},
url = {https://doi.org/10.1038/s41467-026-77016-y},
pmid = {42680774},
pmcid = {PMC13534550}
}

RIS

TY - JOUR
AU - Ren, Kang
AU - Cheng, Mingjie
AU - Luo, Qiudan
AU - Zhang, Boxin
AU - Zhang, Haosheng
AU - Li, Zhe
AU - Liu, Yuxin
AU - Wang, Yujie
AU - Kang, Ting
AU - Dai, Xiaoming
AU - Chen, Jiong
AU - Cheng, Yuanming
AU - Huang, Liangqian
TI - YTHDC1 functions as a molecular chaperone to suppress ALS-linked hnRNPA1 mutants from aggregation
T2 - Nature communications
J2 - Nat Commun
PY - 2026
DA - 2026/08/21
VL - 17
IS - 1
SP - 9357
SN - 2041-1723
PB - Nature Publishing Group
DO - 10.1038/s41467-026-77016-y
UR - https://doi.org/10.1038/s41467-026-77016-y
LA - en
ER -

CSL-JSON

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"container-title-short": "Nat Commun",
"volume": "17",
"issue": "1",
"page": "9357",
"DOI": "10.1038/s41467-026-77016-y",
"PMID": "42680774",
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"language": "en",
"issued": {
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