Evidence map›Paper›PMID 34346674›Full record

ArticleJournal of the American Chemical Society2021

Phosphorylation of a Human Microprotein Promotes Dissociation of Biomolecular Condensates.

Zhenkun Na, Yang Luo, Danica S Cui, Alexandra Khitun, Stephanie Smelyansky, J Patrick Loria, Sarah A Slavoff

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
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  5. bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Eukaryotic Microproteins.Annual review of biochemistry · 2025
    Review
  8. Review
  9. Article
  10. Noncanonical microprotein regulation of immunity.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Review
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
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  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Zhenkun NaDepartment of Chemistry, Yale University, New Haven, Connecticut 06520, United States.
Yang LuoDepartment of Chemistry, Yale University, New Haven, Connecticut 06520, United States.ORCID 0000-0002-8709-0103
Danica S CuiDepartment of Chemistry, Yale University, New Haven, Connecticut 06520, United States.
Alexandra KhitunDepartment of Chemistry, Yale University, New Haven, Connecticut 06520, United States.ORCID 0000-0003-4137-0035
Stephanie SmelyanskyDepartment of Chemistry, Yale University, New Haven, Connecticut 06520, United States.
J Patrick LoriaDepartment of Chemistry, Yale University, New Haven, Connecticut 06520, United States.ORCID 0000-0002-4824-9089
Sarah A SlavoffDepartment of Chemistry, Yale University, New Haven, Connecticut 06520, United States.ORCID 0000-0002-4443-2070
Yale University · US

Funding

Predoc Training at the Interface Chemistry and BiologyT32GM067543 · NIGMS · YALE UNIVERSITY · PI CRAWFORD, JASON MICHAEL · 2003 to 2022
$7.4M
Structural and functional roles of the microprotein NoBody in mRNA decapping and decayR01GM122984 · NIGMS · YALE UNIVERSITY · PI SLAVOFF, SARAH ANN · 2017 to 2021
$1.6M
NIGMS NIH HHS R01 GM122984NIGMS NIH HHS T32 GM067543
6 · The paper itself

Abstract

Proteogenomic identification of translated small open reading frames in humans has revealed thousands of microproteins, or polypeptides of fewer than 100 amino acids, that were previously invisible to geneticists. Hundreds of microproteins have been shown to be essential for cell growth and proliferation, and many regulate macromolecular complexes. However, the vast majority of microproteins remain functionally uncharacterized, and many lack secondary structure and exhibit limited evolutionary conservation. One such intrinsically disordered microprotein is NBDY, a 68-amino acid component of membraneless organelles known as P-bodies. In this work, we show that NBDY can undergo liquid-liquid phase separation, a biophysical process thought to underlie the formation of membraneless organelles, in the presence of RNA

Indexed as

Biomolecular CondensatesHumansIntrinsically Disordered ProteinsParticle SizePhosphorylationIntrinsically Disordered Proteins

Identifiers

PMID34346674
PMCPMC8564862
OpenAlexW3187350158

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.