Evidence map›Paper›PMID 31083504›Full record

ReviewInternational journal of molecular sciences2019

The Physics of Entropic Pulling: A Novel Model for the Hsp70 Motor Mechanism.

Rui Sousa, Eileen M Lafer

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Article
  4. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
    Review
  5. Article
  6. Article
  7. Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ.Protein science : a publication of the Protein Society · 2024
    Article
  8. Domperidone InhibitsToxins · 2023
    Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Mechanistic basis for ubiquitin modulation of a protein energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches.Computational and structural biotechnology journal · 2021
    Review
  17. Article
  18. Article
  19. Review
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.

Rui SousaDepartment of Biochemistry and Structural Biology, University of Texas Health Science Center, San Antonio, TX 78229-3900, USA. sousa@uthscsa.edu.
Eileen M LaferDepartment of Biochemistry and Structural Biology, University of Texas Health Science Center, San Antonio, TX 78229-3900, USA. lafer@uthscsa.edu.
The University of Texas Health Science Center at San Antonio · US

Funding

Chaperone Mechanisms in Clathrin Mediated Neuronal Vesicle TraffickingR01GM118933 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI LAFER, EILEEN M., SOUSA, RUI J. · 2016 to 2019
$1.7M
National Institutes of Health NIH GM118933NIGMS NIH HHS R01 GM118933
6 · The paper itself

Abstract

Hsp70s use ATP to generate forces that disassemble protein complexes and aggregates, and that translocate proteins into organelles. Entropic pulling has been proposed as a novel mechanism, distinct from the more familiar power-stroke and Brownian ratchet models, for how Hsp70s generate these forces. Experimental evidence supports entropic pulling, but this model may not be well understood among scientists studying these systems. In this review we address persistent misconceptions regarding the dynamics of proteins in solution that contribute to this lack of understanding, and we clarify the basic physics of entropic pulling with some simple analogies. We hope that increased understanding of the entropic pulling mechanism will inform future efforts to characterize how Hsp70s function as motors, and how they coordinate with their regulatory cochaperones in mechanochemical cycles that transduce the energy of ATP hydrolysis into physical changes in their protein substrates.

Indexed as

EntropyModels, BiologicalAdenosine TriphosphateHSP70 Heat-Shock ProteinsMolecular Motor ProteinsAdenosine TriphosphateHSP70 Heat-Shock ProteinsMolecular Motor Proteinsbrownian ratchetchaperonesDISAGGREGATIONentropic pullingHsp110Hsp70J cochaperonesmotor proteinspower-strokeprotein translocation

Identifiers

PMID31083504
PMCPMC6539501
OpenAlexW2944386600

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.