Evidence map›Paper›PMID 34780988›Full record

ReviewFree radical biology & medicine2022

Mitochondrial chaperones in human health and disease.

Tyler Bahr, Joshua Katuri, Ting Liang, Yidong Bai

Open access · greenAbstract readReview
In one paragraph

Review in Free radical biology & medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

30 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. The role of impaired mitochondrial function in neurological manifestations of mitochondrial diseases.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Review
  3. Review
  4. Review
  5. Article
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  9. Article
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  11. Article
  12. Mitochondrial dysfunction in Alzheimer's disease: Guiding the path to targeted therapies.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  13. Review
  14. Review
  15. HADHA Regulates Respiratory Complex Assembly and Couples FAO and OXPHOS.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  16. Review
  17. Article
  18. Article
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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 1 institution in 1 country.

Tyler BahrDepartment of Cell Systems & Anatomy University of Texas Health San Antonio, 7703 Floyd Curl Dr, San Antonio, TX, 78229, USA.
Joshua KaturiDepartment of Cell Systems & Anatomy University of Texas Health San Antonio, 7703 Floyd Curl Dr, San Antonio, TX, 78229, USA.
Ting LiangDepartment of Cell Systems & Anatomy University of Texas Health San Antonio, 7703 Floyd Curl Dr, San Antonio, TX, 78229, USA.
Yidong BaiDepartment of Cell Systems & Anatomy University of Texas Health San Antonio, 7703 Floyd Curl Dr, San Antonio, TX, 78229, USA. Electronic address: baiy@uthscsa.edu.
The University of Texas Health Science Center at San Antonio · US

Funding

Regulation of mitochondrial respiratory complex I dynamicsR01GM109434 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI BAI, YIDONG · 2014 to 2017
$1.3M
The role of Grp75 in supercomplex assembly and neurodegenerationR01GM130129 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI BAI, YIDONG · 2018 to 2019
$580k
NIGMS NIH HHS R01 GM109434NIGMS NIH HHS R01 GM130129
6 · The paper itself

Abstract

Molecular chaperones are a family of proteins that maintain cellular protein homeostasis through non-covalent peptide folding and quality control mechanisms. The chaperone proteins found within mitochondria play significant protective roles in mitochondrial biogenesis, quality control, and stress response mechanisms. Defective mitochondrial chaperones have been implicated in aging, neurodegeneration, and cancer. In this review, we focus on the two most prominent mitochondrial chaperones: mtHsp60 and mtHsp70. These proteins demonstrate different cellular localization patterns, interact with different targets, and have different functional activities. We discuss the structure and function of these prominent mitochondrial chaperone proteins and give an update on newly discovered regulatory mechanisms and disease implications.

Indexed as

HSP70 Heat-Shock ProteinsMolecular ChaperonesHumansMitochondriaMitochondrial ProteinsProtein FoldingHSP70 Heat-Shock ProteinsMitochondrial ProteinsMolecular ChaperonesMitochondrial chaperoneMitochondrial homeostasismtHsp60mtHsp70Stressresponse

Identifiers

PMID34780988
PMCPMC8893670
OpenAlexW3211622484

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.