Evidence map›Paper›PMID 27233499›Full record

ReviewCellular and molecular life sciences : CMLS2016

Post-translational modifications in mitochondria: protein signaling in the powerhouse.

Amanda R Stram, R Mark Payne

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

90 citing papers in PubMed, 148 citations in OpenAlex.

  1. Review
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  7. Review
  8. NADH dehydrogenase reverses dietary and clock metabolic syndrome.bioRxiv : the preprint server for biology · 2025
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  11. Review
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  14. Rapid modulation of interscapular brown adipose tissue mitochondrial activity by ketosis induced by 1,3-butanediol administration to rats.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  15. Article
  16. Article
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  18. Review
  19. Article
  20. Article

30 more citing papers are in PubMed but not listed here.

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.

Amanda R StramDepartment of Surgery, Indiana University School of Medicine, Indianapolis, IN, USA.ORCID 0000-0002-3046-3749
R Mark PayneDepartment of Pediatrics, Indiana University School of Medicine, Indianapolis, IN, USA. rpayne@iu.edu.
Indiana University School of Medicine

Funding

The Role of Mitochondrial Protein Acetylation in Left Ventricular FunctionF31HL126489 · NHLBI · INDIANA UNIVERSITY INDIANAPOLIS · PI STRAM, AMANDA · 2015 to 2016
$62k
NHLBI NIH HHS F31 HL126489NHLBI NIH HHS L40 HL129417
6 · The paper itself

Abstract

There is an intimate interplay between cellular metabolism and the pathophysiology of disease. Mitochondria are essential to maintaining and regulating metabolic function of cells and organs. Mitochondrial dysfunction is implicated in diverse diseases, such as cardiovascular disease, diabetes and metabolic syndrome, neurodegeneration, cancer, and aging. Multiple reversible post-translational protein modifications are located in the mitochondria that are responsive to nutrient availability and redox conditions, and which can act in protein-protein interactions to modify diverse mitochondrial functions. Included in this are physiologic redox signaling via reactive oxygen and nitrogen species, phosphorylation, O-GlcNAcylation, acetylation, and succinylation, among others. With the advent of mass proteomic screening techniques, there has been a vast increase in the array of known mitochondrial post-translational modifications and their protein targets. The functional significance of these processes in disease etiology, and the pathologic response to their disruption, are still under investigation. However, many of these reversible modifications act as regulatory mechanisms in mitochondria and show promise for mitochondrial-targeted therapeutic strategies. This review addresses the current knowledge of post-translational processing and signaling mechanisms in mitochondria, and their implications in health and disease.

Indexed as

Protein Processing, Post-TranslationalSignal TransductionAnimalsHumansLysineMitochondriaMitochondrial ProteinsOxidation-ReductionLysineMitochondrial ProteinsAcetylationMetabolismMitochondriaPost-translational modification

Identifiers

PMID27233499
PMCPMC5045789
OpenAlexW2404128784

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.