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PARylation regulates stress granule dynamics, phase separation, and neurotoxicity of disease-related RNA-binding proteins
Duan Y, Du A, Gu J, Duan G, Wang C, Gui X, Ma Z, Qian B et al.. Cell research, 2019-02-06
Topic: Brain proteins, microglia and lab models
Mutations in RNA-binding proteins (RBPs) localized in ribonucleoprotein (RNP) granules, such as hnRNP A1 and TDP-43, promote aberrant protein aggregation, which is a pathological hallmark of various neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Protein posttranslational modifications (PTMs) are known to regulate RNP granules. In this study, we investigate the function of poly(ADP-ribosyl)ation (PARylation), an important PTM involved in DNA damage repair and cell death, in RNP granule-related neurodegeneration.
Key findings
- Protein posttranslational modifications (PTMs) are known to regulate RNP granules.
- In this study, we investigate the function of poly(ADP-ribosyl)ation (PARylation), an important PTM involved in DNA damage repair and cell death, in RNP granule-related neurodegeneration.
- We reveal that PARylation levels are a major regulator of the assembly-disassembly dynamics of RNP granules containing disease-related RBPs, hnRNP A1 and TDP-43.
- We find that hnRNP A1 can both be PARylated and bind to PARylated proteins or poly(ADP-ribose) (PAR).
Why it matters
This laboratory study investigated how PARylation regulates the assembly and disassembly of RNP granules containing disease-related RNA-binding proteins such as hnRNP A1 and TDP-43. It is mechanistic cell work related to ALS and frontotemporal dementia and does not test a treatment in patients.
Study details
- Evidence strengthLow
How this study scored 49/100
Published in a peer-reviewed journal. Scored zero for study design, sample size, effect reported, studied in people and randomised / blinded because the record does not state it.
| Component | Points | Why |
|---|---|---|
| Journal tier | 7 / 10 | Tier 3 — peer-reviewed journal (Cell research) |
| Journal's citation record | 3 / 4 | Cell Research: journal h-index 271 (OpenAlex, 2026-10-29) |
| Study design | 0 / 12 | No study design recorded — scores zero, not guessed (not stated in the record — scored 0) |
| Strength of evidence | 1 / 5 | Rated “low” in our summary |
| Peer-review validation | 10 / 10 | Peer-reviewed. Published as an article in a named peer-reviewed journal. |
| How recent | 2 / 5 | 2019 — within 10 year(s) of the newest study here |
| Sample size | 0 / 4 | Participant count not stated — scores zero (not stated in the record — scored 0) |
| Effect reported | 0 / 3 | No effect size reported — scores zero (not stated in the record — scored 0) |
| Studied in people | 0 / 3 | Not stated whether this was studied in people — scores zero (not stated in the record — scored 0) |
| Randomised / blinded | 0 / 2 | No randomisation or blinding stated — scores zero (not stated in the record — scored 0) |
| Times cited | 5 / 7 | Cited 279 times (OpenAlex, 2026-10-10) |
| Citations per year | 4 / 5 | 31.0 citations a year over 9 year(s) since 2019 |
| Impact for its field and year | 5 / 6 | Cited 20.3× the average for papers of its field and year (OpenAlex FWCI) |
| Cited by studies here | 1 / 6 | Cited by 1 other studies in this library |
| Still being cited | 3 / 4 | Cited 103 times in 2024–2026 (2026 still in progress; OpenAlex) |
| Senior author's track record | 2 / 4 | Last-listed author Yanshan Fang: h-index 26 (OpenAlex, whole career) |
| Institution's track record | 2 / 3 | Chinese Academy of Sciences: institution h-index 1,801 (OpenAlex) |
| Multi-centre collaboration | 2 / 3 | OpenAlex lists 4 institution(s) in 1 country |
| Indexed in PubMed | 2 / 2 | Indexed in PubMed (PMID 30728452) |
| Free to read | 0 / 2 | Behind a paywall — scores zero |
| Total | 49 / 100 | — |
What each of these 20 components measures, and what this score is not →
Read the original
- DOI: 10.1038/s41422-019-0141-z
- PubMed: 30728452
- Original source →
- Free full text: bioRxiv (Cold Spring Harbor Laboratory) →
Full text: free to read — OpenAlex lists this copy as free to read: the link above (checked 6 Feb 1020).
Cite this study APA, Vancouver, BibTeX · download .bib or .ris
Built from the record alzhub holds for this paper, not looked up. Volume, issue and page numbers are not held in the record. The record's author list ends in “et al.”, so not every author is named. Check the citation against the original before you use it.
APA 7th
Duan, Y., Du, A., Gu, J., Duan, G., Wang, C., Gui, X., et al. (2019). PARylation regulates stress granule dynamics, phase separation, and neurotoxicity of disease-related RNA-binding proteins. Cell research. https://doi.org/10.1038/s41422-019-0141-z
Vancouver
Duan Y, Du A, Gu J, Duan G, Wang C, Gui X, et al. PARylation regulates stress granule dynamics, phase separation, and neurotoxicity of disease-related RNA-binding proteins. Cell research. 2019. doi:10.1038/s41422-019-0141-z. PMID: 30728452.
BibTeX
@article{duan2019-30728452,
author = {Duan, Y. and Du, A. and Gu, J. and Duan, G. and Wang, C. and Gui, X. and Ma, Z. and Qian, B. and others},
title = {{PARylation regulates stress granule dynamics, phase separation, and neurotoxicity of disease-related RNA-binding proteins}},
journal = {Cell research},
year = {2019},
doi = {10.1038/s41422-019-0141-z},
pmid = {30728452},
url = {https://doi.org/10.1038/s41422-019-0141-z}
}
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