Evidence map›Paper›PMID 32697684›Full record

ArticleeLife2020

Controlling protein function by fine-tuning conformational flexibility.

Sonja Schmid, Thorsten Hugel

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Ligand-driven modulation of chaperone-cochaperone networks shapes proteostasis outcomes.Protein science : a publication of the Protein Society · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
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  13. Review
  14. Structural transitions modulate the chaperone activities of Grp94.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. The role of Aha1 in cancer and neurodegeneration.Frontiers in molecular neuroscience · 2024
    Review
  17. The Onset of Molecule-Spanning Dynamics in Heat Shock Protein Hsp90.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  18. Review
  19. Article
  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

2 authors at 1 institution in 1 country.

Sonja SchmidInstitute of Physical Chemistry, University of Freiburg, Freiburg, Germany.ORCID 0000-0002-3710-5602
Thorsten HugelInstitute of Physical Chemistry, University of Freiburg, Freiburg, Germany.ORCID 0000-0003-3292-4569
University of Freiburg · DE

Funding

Deutsche Forschungsgemeinschaft SFB 1381European Commission 681891Swiss National Science Foundation ​Postdoc.Mobility fellowships
6 · The paper itself

Abstract

In a living cell, protein function is regulated in several ways, including post-translational modifications (PTMs), protein-protein interaction, or by the global environment (e.g. crowding or phase separation). While site-specific PTMs act very locally on the protein, specific protein interactions typically affect larger (sub-)domains, and global changes affect the whole protein non-specifically. Herein, we directly observe protein regulation under three different degrees of localization, and present the effects on the Hsp90 chaperone system at the levels of conformational steady states, kinetics and protein function. Interestingly using single-molecule FRET, we find that similar functional and conformational steady states are caused by completely different underlying kinetics. We disentangle specific and non-specific effects that control Hsp90's ATPase function, which has remained a puzzle up to now. Lastly, we introduce a new mechanistic concept: functional stimulation through conformational confinement. Our results demonstrate how cellular protein regulation works by fine-tuning the conformational state space of proteins.

Indexed as

HSP90 Heat-Shock ProteinsMolecular ChaperonesProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHSP82 protein, S cerevisiaeHSP90 Heat-Shock ProteinsMolecular ChaperonesSaccharomyces cerevisiae ProteinsAha1biochemistrychaperonechemical biologycrowdingFRETHsp90S. cerevisiaeSMACKS

Identifiers

PMID32697684
PMCPMC7375816
OpenAlexW3044557441

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.