Evidence map›Paper›PMID 34767801›Full record

ReviewJournal of molecular biology2022

Conformational Freedom and Topological Confinement of Proteins in Biomolecular Condensates.

Daniel Scholl, Ashok A Deniz

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

6 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Neurological Diseases can be Regulated by Phase Separation.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  6. RNA encodes physical information.bioRxiv : the preprint server for biology · 2024
    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

2 authors at 1 institution in 1 country.

Daniel SchollDepartment of Integrative and Computational Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, United States. Electronic address: https://twitter.com/@DanielScholl_be.
Ashok A DenizDepartment of Integrative and Computational Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, United States. Electronic address: deniz@scripps.edu.
Scripps Research Institute · US

Funding

Biophysics of Protein Disorder and Complexity, Single Molecules to MesoscalesR35GM130375 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A · 2019 to 2023
$2.4M
NIGMS NIH HHS R35 GM130375
6 · The paper itself

Abstract

The emergence of biomolecular condensation and liquid-liquid phase separation (LLPS) introduces a new layer of complexity into our understanding of cell and molecular biology. Evidence steadily grows indicating that condensates are not only implicated in physiology but also human disease. Macro- and mesoscale characterization of condensates as a whole have been instrumental in understanding their biological functions and dysfunctions. By contrast, the molecular level characterization of condensates and how condensates modify the properties of the molecules that constitute them thus far remain comparably scarce. In this minireview we summarize and discuss the findings of several recent studies that have focused on structure, dynamics, and interactions of proteins undergoing condensation. The mechanistic insights they provide help us identify the relevant properties nature and scientists can leverage to modulate the behavior of condensate systems. We also discuss the unique environment of the droplet surface and speculate on effects of topological constraints and physical exclusion on condensate properties.

Indexed as

Biomolecular CondensatesBiophysical PhenomenaCaenorhabditis elegans ProteinsNucleophosminProtein ConformationProteinsRNA-Binding Protein FUSRNA-Binding ProteinsCaenorhabditis elegans ProteinsMEG-3 protein, C elegansNPM1 protein, humanNucleophosminPGL-3 protein, C elegansProteinsRNA-Binding Protein FUSRNA-Binding Proteinsbiomolecular condensatesdisordered proteinsphase separationprotein dynamicstopology

Identifiers

PMID34767801
PMCPMC8748313
OpenAlexW3213583078

What Socratic 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 Socratic graph.