Evidence map›Paper›PMID 20544878›Full record

ReviewEnvironmental and molecular mutagenesis2010

The mitochondrial proteome: a dynamic functional program in tissues and disease states.

Robert S Balaban

Open access · greenAbstract readReview
In one paragraph

Review in Environmental and molecular mutagenesis, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Fyn kinase regulates translation in mammalian mitochondria.Biochimica et biophysica acta. General subjects · 2017
    Article
  5. Review
  6. Review
  7. Role of soluble adenylyl cyclase in mitochondria.Biochimica et biophysica acta · 2014
    Review
  8. Review
  9. Article
  10. The role of mitochondria from mature oocyte to viable blastocyst.Obstetrics and gynecology international · 2013
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Computational modeling of mitochondrial energy transduction.Critical reviews in biomedical engineering · 2011
    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

1 author at 1 institution in 1 country.

Robert S BalabanLaboratory of Cardiac Energetics, National Heart Lung and Blood Institute, Department of Health and Human Services, Bethesda, Maryland, USA. rsb@nih.gov
National Heart Lung and Blood Institute · US

Funding

Control Of Cellular Energy MetabolismZIAHL004601 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BALABAN, ROBERT · 2009 to 2023
$24.4M
Macromolecular Structure of Arterial WallsZIAHL006027 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI BALABAN, ROBERT · 2009 to 2018
$2.4M
Intramural NIH HHS ZIA HL004601Intramural NIH HHS ZIA HL006027
6 · The paper itself

Abstract

The nuclear DNA transcriptional programming of the mitochondria proteome varies dramatically between tissues depending on its functional requirements. This programming generally regulates all of the proteins associated with a metabolic or biosynthetic pathway associated with a given function, essentially regulating the maximum rate of the pathway while keeping the enzymes at the same molar ratio. This may permit the same regulatory mechanisms to function at low- and high-flux capacity situations. This alteration in total protein content results in rather dramatic changes in the mitochondria proteome between tissues. A tissues mitochondria proteome also changes with disease state, in Type 1 diabetes the liver mitochondrial proteome shifts to support ATP production, urea synthesis, and fatty acid oxidation. Acute flux regulation is modulated by numerous posttranslational events that also are highly variable between tissues. The most studied posttranslational modification is protein phosphorylation, which is found all of the complexes of oxidative phosphorylation and most of the major metabolic pathways. The functional significance of these modifications is currently a major area of research along with the kinase and phosphatase regulatory network. This near ubiquitous presence of protein phosphorylations, and other posttranslational events, in the matrix suggest that not all posttranslational events have functional significance. Screening methods are being introduced to detect the active or dynamic posttranslational sites to focus attention on sites that might provide insight into regulatory mechanisms.

Indexed as

Diabetes Mellitus, Type 1HumansMitochondriaMitochondrial ProteinsProtein Processing, Post-TranslationalProteomeTranscription, GeneticMitochondrial ProteinsProteome

Identifiers

PMID20544878
PMCPMC3209511
OpenAlexW2026762998

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.