Evidence map›Paper›PMID 32302874›Full record

ReviewCurrent opinion in structural biology2020

Recent advances suggest increased influence of selective pressure in allostery.

Archana S Bhat, Richard Dustin Schaeffer, Lisa Kinch, Kirill E Medvedev, Nick V Grishin

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Investigating Plasma-Activated Water (PAW) onFood science & nutrition · 2025
    Article
  4. Global hinge sites of proteins as target sites for drug binding.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021
    Review
  12. Article
  13. 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

5 authors.

Archana S BhatDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390-9050, United States.
Richard Dustin SchaefferDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390-9050, United States.
Lisa KinchHoward Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390-9050, United States.
Kirill E MedvedevDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390-9050, United States.
Nick V GrishinDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390-9050, United States; Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390-9050, United States. Electronic address: grishin@chop.swmed.edu.

Funding

Computational analysis of proteinsR35GM127390 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GRISHIN, NICK V. · 2018 to 2022
$1.5M
NIGMS NIH HHS R35 GM127390
6 · The paper itself

Abstract

Allosteric regulation of protein functions is ubiquitous in organismal biology, but the principles governing its evolution are not well understood. Here we discuss recent studies supporting the large-scale existence of latent allostery in ancestor proteins of superfamilies. As suggested, the evolution of allostery could be driven by the need for specificity in paralogs of slow evolving protein complexes with conserved active sites. The same slow evolution is displayed by purifying selection exhibited in allosteric proteins with somatic mutations involved in cancer, where disease-associated mutations are enriched in both orthosteric and allosteric sites. Consequently, disease-associated variants can be used to identify druggable allosteric sites that are specific for paralogs in protein superfamilies with otherwise similar functions.

Indexed as

Models, MolecularProteinsAllosteric RegulationAllosteric SiteAnimalsCatalytic DomainHumansProtein BindingProteins

Identifiers

PMID32302874
PMCPMC8011830

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Registered trials

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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.