Evidence map›Paper›PMID 37287189›Full record

ReviewFEBS letters2023

The roles of molecular chaperones in regulating cell metabolism.

Matthew J Binder, Anthony M Pedley

Open access · hybridAbstract readReview
In one paragraph

Review in FEBS letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 1 synthesis or guideline pooled it, 22 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Identification of novel small molecule chaperone activators for neurodegenerative disease treatment.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2025
    Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Review
  16. A journey into the regulatory secrets of theFrontiers in pharmacology · 2024
    Review
  17. 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.

Matthew J BinderDepartment of Chemistry, The Pennsylvania State University, University Park, PA, USA.ORCID 0009-0006-6715-4073
Anthony M PedleyDepartment of Chemistry, The Pennsylvania State University, University Park, PA, USA.ORCID 0000-0003-1034-5072
Pennsylvania State University · US

Funding

Molecular Chaperone-mediated Regulation of Cell MetabolismR35GM150481 · NIGMS · UNIVERSITY OF IOWA · PI Anthony M Pedley · 2023 to 2026
$1.8M
NIGMS NIH HHS R35 GM150481
6 · The paper itself

Abstract

Fluctuations in nutrient and biomass availability, often as a result of disease, impart metabolic challenges that must be overcome in order to sustain cell survival and promote proliferation. Cells adapt to these environmental changes and stresses by adjusting their metabolic networks through a series of regulatory mechanisms. Our understanding of these rewiring events has largely been focused on those genetic transformations that alter protein expression and the biochemical mechanisms that change protein behavior, such as post-translational modifications and metabolite-based allosteric modulators. Mounting evidence suggests that a class of proteome surveillance proteins called molecular chaperones also can influence metabolic processes. Here, we summarize several ways the Hsp90 and Hsp70 chaperone families act on human metabolic enzymes and their supramolecular assemblies to change enzymatic activities and metabolite flux. We further highlight how these chaperones can assist in the translocation and degradation of metabolic enzymes. Collectively, these studies provide a new view for how metabolic processes are regulated to meet cellular demand and inspire new avenues for therapeutic intervention.

Indexed as

Molecular ChaperonesProtein FoldingHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansProtein Processing, Post-TranslationalHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular Chaperonescellular metabolismmetabolonsmolecular chaperonesprotein degradationprotein foldingsupramolecular complexes

Identifiers

PMID37287189
PMCPMC10984649
OpenAlexW4379769521

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.