Evidence map›Paper›PMID 34453889›Full record

ArticleMolecular cell2021

Conformational equilibria in allosteric control of Hsp70 chaperones.

Wei Wang, Qinglian Liu, Qun Liu, Wayne A Hendrickson

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Cholesterol-dependent enzyme activity of human TSPO1.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. AlphaFold-guided molecular replacement for solving challenging crystal structures.Acta crystallographica. Section D, Structural biology · 2025
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Effect of evolution of the C-terminal region on chaperone activity of Hsp70.Protein science : a publication of the Protein Society · 2023
    Article
  13. Ssa1-targeted antibody prevents host invasion byFrontiers in microbiology · 2023
    Article
  14. Article
  15. Conformational dynamics of the Hsp70 chaperone throughout key steps of its ATPase cycle.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Review
  17. Review
  18. 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 2 institutions in 1 country.

Wei WangDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
Qinglian LiuDepartment of Physiology and Biophysics, Virginia Commonwealth University, Richmond, VA 23298, USA.
Qun LiuBiology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
Wayne A HendricksonDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA; Department of Physiology and Cellular Biophysics, Columbia University, New York, NY 10032, USA. Electronic address: wah2@cumc.columbia.edu.
Columbia University · USVirginia Commonwealth University · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Structural and Functional Studies of Hsp70 Molecular ChaperonesR01GM098592 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI Qinglian Liu · 2013 to 2026
$4.3M
Proposal for an Administrative Supplement for Equipment Purchases for NIGMS Awardees NOT-GM-18-022R01GM107462 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI HENDRICKSON, WAYNE A. · 2014 to 2021
$3.6M
Targeting a novel Hsp70 substrate binding mode for potential treatment of gonorrhea infectionR21AI140006 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI CORNELISSEN, CYNTHIA N, HARTMAN, MATTHEW C · 2018 to 2019
$423k
NIAID NIH HHS R21 AI140006NIGMS NIH HHS P30 GM124165NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM098592NIGMS NIH HHS R01 GM107462
6 · The paper itself

Abstract

Heat-shock proteins of 70 kDa (Hsp70s) are vital for all life and are notably important in protein folding. Hsp70s use ATP binding and hydrolysis at a nucleotide-binding domain (NBD) to control the binding and release of client polypeptides at a substrate-binding domain (SBD); however, the mechanistic basis for this allostery has been elusive. Here, we first characterize biochemical properties of selected domain-interface mutants in bacterial Hsp70 DnaK. We then develop a theoretical model for allosteric equilibria among Hsp70 conformational states to explain the observations: a restraining state, Hsp70

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAllosteric RegulationBinding SitesEscherichia coli ProteinsHSP70 Heat-Shock ProteinsHydrolysisKineticsModels, MolecularMutationProtein BindingProtein ConformationSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipAdenosine TriphosphatasesAdenosine TriphosphatednaK protein, E coliEscherichia coli ProteinsHSP70 Heat-Shock ProteinsSaccharomyces cerevisiae ProteinsSSA1 protein, S cerevisiaeallosteric regulationcrystal structureDnaKHsp70molecular chaperoneprotein folding

Identifiers

PMID34453889
PMCPMC8500941
OpenAlexW3196833843

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.