Evidence map›Paper›PMID 35119946›Full record

ReviewAnnual review of biophysics2022

Rules of Physical Mathematics Govern Intrinsically Disordered Proteins.

Kingshuk Ghosh, Jonathan Huihui, Michael Phillips, Austin Haider

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biophysics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

35 citing papers in PubMed, 59 citations in OpenAlex.

  1. Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026
    Article
  2. A Sequence-Specific Theory for Charge-Regulating IDPs.The journal of physical chemistry. B · 2026
    Article
  3. Dilute but Dense - Reversible Crosslinking Enables Water-Rich (Bio)polymer Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Mapping Charge Interactions in Intrinsically Disordered Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. bioRxiv : the preprint server for biology · 2026
    Article
  6. Sticky interactions govern sequence-dependent dynamics in biomolecular condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
  8. Article
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  11. Article
  12. A genetically encoded anomalous SAXS ruler to probe the dimensions of intrinsically disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. HYPK: A marginally disordered protein sensitive to charge decoration.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Review
  20. 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

4 authors at 1 institution in 1 country.

Kingshuk GhoshDepartment of Physics and Astronomy, University of Denver, Denver, Colorado, USA; email: kghosh@du.edu.
Jonathan HuihuiDepartment of Physics and Astronomy, University of Denver, Denver, Colorado, USA; email: kghosh@du.edu.
Michael PhillipsDepartment of Physics and Astronomy, University of Denver, Denver, Colorado, USA; email: kghosh@du.edu.
Austin HaiderMolecular and Cellular Biophysics Program, University of Denver, Denver, Colorado, USA.
University of Denver · US

Funding

Modeling Conformational Ensembles of the Disordered ProteinsR01GM138901 · NIGMS · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI GHOSH, KINGSHUK · 2020 to 2024
$1.3M
NIGMS NIH HHS R01 GM138901
6 · The paper itself

Abstract

In stark contrast to foldable proteins with a unique folded state, intrinsically disordered proteins and regions (IDPs) persist in perpetually disordered ensembles. Yet an IDP ensemble has conformational features-even when averaged-that are specific to its sequence. In fact, subtle changes in an IDP sequence can modulate its conformational features and its function. Recent advances in theoretical physics reveal a set of elegant mathematical expressions that describe the intricate relationships among IDP sequences, their ensemble conformations, and the regulation of their biological functions. These equations also describe the molecular properties of IDP sequences that predict similarities and dissimilarities in their functions and facilitate classification of sequences by function, an unmet challenge to traditional bioinformatics. These physical sequence-patterning metrics offer a promising new avenue for advancing synthetic biology at a time when multiple novel functional modes mediated by IDPs are emerging.

Indexed as

Intrinsically Disordered ProteinsMathematicsProtein ConformationIntrinsically Disordered Proteinsdisorderfunctionheteropolymerliquid–liquid phase separationpolyampholyteproteome

Identifiers

PMID35119946
PMCPMC9190209
OpenAlexW4210539583

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.