Evidence map›Paper›PMID 29895621›Full record

ArticleThe Journal of biological chemistry2018

Analysis of heat-induced protein aggregation in human mitochondria.

Anne Wilkening, Cornelia Rüb, Marc Sylvester, Wolfgang Voos

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

32 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  6. Review
  7. Around theMethodsX · 2025
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  8. Review
  9. Genesis and regulation of C-terminal cyclic imides from protein damage.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Bioenergetic myths of energy transduction in eukaryotic cells.Frontiers in molecular biosciences · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Intracellular Aβ42 Aggregation Leads to Cellular Thermogenesis.Journal of the American Chemical Society · 2022
    Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Anne WilkeningInstitute for Biochemistry and Molecular Biology, Friedrich Wilhelm University, 53115 Bonn, Germany.
Cornelia RübInstitute for Biochemistry and Molecular Biology, Friedrich Wilhelm University, 53115 Bonn, Germany.
Marc SylvesterInstitute for Biochemistry and Molecular Biology, Friedrich Wilhelm University, 53115 Bonn, Germany.
Wolfgang VoosInstitute for Biochemistry and Molecular Biology, Friedrich Wilhelm University, 53115 Bonn, Germany. Electronic address: wolfgang.voos@uni-bonn.de.
University of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins in mammalian cells exhibit optimal stability at physiological temperatures, and even small temperature variations may cause unfolding and nonspecific aggregation. Because this process leads to a loss of function of the affected polypeptides and to cytotoxic stress, formation of protein aggregates has been recognized as a major pathogenic factor in human diseases. In this study, we determined the impact of physiological heat stress on mitochondria isolated from HeLa cells. We found that the heat-stressed mitochondria had lower membrane potential and ATP level and exhibited a decreased production of reactive oxygen species. An analysis of the mitochondrial proteome by 2D PAGE showed that the overall solubility of endogenous proteins was only marginally affected by elevated temperatures. However, a small subset of polypeptides exhibited an high sensitivity to heat stress. The mitochondrial translation elongation factor Tu (Tufm), a protein essential for organellar protein biosynthesis, was highly aggregation-prone and lost its solubility already under mild heat-stress conditions. Moreover, mitochondrial translation and the import of cytosolic proteins were defective in the heat-stressed mitochondria. Both types of nascent polypeptides, produced by translation or imported into the mitochondria, exhibited a strong tendency to aggregate in the heat-exposed mitochondria. We propose that a fast and specific inactivation of elongation factors may prevent the accumulation of misfolded nascent polypeptides and may thereby attenuate proteotoxicity under heat stress.

Indexed as

Heat-Shock ResponseProtein AggregatesAdenosine TriphosphateHeLa CellsHot TemperatureHumansMembrane Potential, MitochondrialMitochondriaMitochondrial ProteinsPeptide Elongation Factor TuAdenosine TriphosphateMitochondrial ProteinsPeptide Elongation Factor TuProtein AggregatesTUFM protein, humanheat stressmitochondriamitochondrial elongation factor Tuprotein aggregationprotein importproteomicstranslationTufm

Identifiers

PMID29895621
PMCPMC6065183
OpenAlexW2808583562

What OpenQuestion holds

Textmetadata
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.