Evidence map›Paper›PMID 40560612›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

PLAA/UFD-3 regulates P-bodies through its intrinsic disordered domain.

Alakananda Das, Yanping Qiu, Trevor J Wolf, Ella Brissett, Jaehyoung Cho, Heenam Park, Eugene C Chen, Tsui-Fen Chou, Paul W Sternberg

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. PLAA/UFD-3 regulates P-bodies through its intrinsic disordered domain.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

9 authors.

Alakananda Das *Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.
Yanping Qiu *Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.
Trevor J WolfDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.
Ella BrissettDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.
Jaehyoung ChoDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.
Heenam ParkDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.ORCID 0000-0001-7911-5828
Eugene C ChenDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.
Tsui-Fen ChouDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.ORCID 0000-0003-2410-2186
Paul W SternbergDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.ORCID 0000-0002-7699-0173

Funding

WormBase: a core data resource for C. elegans and other nematodesU24HG002223 · NHGRI · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI TIM SCHEDL, PAUL Warren STERNBERG · 2018 to 2026
$18.9M
Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Aric L Daul, Ann E. Rougvie · 2012 to 2026
$7.5M
Enhancing the C. elegans animal resource through genome editingR24OD023041 · OD · UNIVERSITY OF MINNESOTA · PI ROUGVIE, ANN E., STERNBERG, PAUL WARREN · 2017 to 2024
$5.1M
HHS | NIH | National Human Genome Research Institute (NHGRI) U24HG002223HHS | NIH (NIH) R24OD023041NHGRI NIH HHS U24 HG002223NIH HHS P40 OD010440NIH HHS R24 OD023041
6 · The paper itself

Abstract

Regulation of proteome homeostasis is crucial for the survival and adaptation to changing environments for all species. In eukaryotes, this process is finely tuned through regulation at the level of transcription, translation, protein modification, and protein degradation. The phospholipase A2 activating protein (PLAA) is present in all eukaryotes and believed to be a key player in ubiquitin-dependent protein sorting and degradation via its interactions with ubiquitin and/or the AAA+ ATPase, valosin-containing protein (VCP/p97). PLAA's molecular targets and interaction network remain unclear. We used

Indexed as

Caenorhabditis elegansCaenorhabditis elegans ProteinsIntrinsically Disordered ProteinsAnimalsProtein DomainsUbiquitinUbiquitinationValosin Containing ProteinCaenorhabditis elegans ProteinsIntrinsically Disordered ProteinsUbiquitinValosin Containing Proteinintrinsically disordered regmating behaviorprotein localizationproteomicsproximity labeling

Identifiers

PMID40560612
PMCPMC12232612

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.