Evidence map›Paper›PMID 36657879›Full record

ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2023

A call to order: Examining structured domains in biomolecular condensates.

Ryan W Tibble, John D Gross

Open access · hybridAbstract read
In one paragraph

Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Allostery in Biomolecular Condensates.Journal of molecular biology · 2026
    Review
  5. Article
  6. Review
  7. High-qualitySolid state nuclear magnetic resonance · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Atomic resolution map of the solvent interactions driving SOD1 unfolding in CAPRIN1 condensates.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Review
  15. Review
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

2 authors at 1 institution in 1 country.

Ryan W TibbleProgram in Chemistry and Chemical Biology, University of California, San Francisco, United States; Department of Pharmaceutical Chemistry, University of California, San Francisco, United States.
John D GrossProgram in Chemistry and Chemical Biology, University of California, San Francisco, United States; Department of Pharmaceutical Chemistry, University of California, San Francisco, United States. Electronic address: jdgross@cgl.ucsf.edu.
University of California, San Francisco · US

Funding

Structure and Function of the Decapping Enzyme ComplexR01GM078360 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI GROSS, JOHN D · 2009 to 2018
$2.5M
Molecular Mechanisms that Control mRNA Decapping in Biological CondensatesR01GM148881 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI John D Gross · 2023 to 2026
$1.3M
NIGMS NIH HHS R01 GM078360NIGMS NIH HHS R01 GM148881
6 · The paper itself

Abstract

Diverse cellular processes have been observed or predicted to occur in biomolecular condensates, which are comprised of proteins and nucleic acids that undergo liquid-liquid phase separation (LLPS). Protein-driven LLPS often involves weak, multivalent interactions between intrinsically disordered regions (IDRs). Due to their inherent lack of defined tertiary structures, NMR has been a powerful resource for studying the behavior and interactions of IDRs in condensates. While IDRs in proteins are necessary for phase separation, core proteins enriched in condensates often contain structured domains that are essential for their function and contribute to phase separation. How phase separation can affect the structure and conformational dynamics of structured domains is critical for understanding how biochemical reactions can be effectively regulated in cellular condensates. In this perspective, we discuss the consequences phase separation can have on structured domains and outline NMR observables we believe are useful for assessing protein structure and dynamics in condensates.

Indexed as

Intrinsically Disordered ProteinsNucleic AcidsBiomolecular CondensatesMagnetic Resonance SpectroscopyMolecular ConformationIntrinsically Disordered ProteinsNucleic Acids

Identifiers

PMID36657879
PMCPMC10878105
OpenAlexW4317568034

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.