Evidence map›Paper›PMID 25228883›Full record

ReviewFrontiers in physiology2014

Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondria.

Kyriakos N Papanicolaou, Brian O'Rourke, D Brian Foster

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.4field-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

45 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. The histone code of the fungal genusMicrobial genomics · 2022
    Article
  10. Article
  11. Review
  12. A New Target of the Four-Herb Chinese Medicine for Wound Repair Promoted by Mitochondrial Metabolism Using Protein Acetylation Analysis.Medical science monitor : international medical journal of experimental and clinical research · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Protein acetylation in cardiac aging.Journal of molecular and cellular cardiology · 2021
    Review
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Kyriakos N PapanicolaouDivision of Cardiology, Department of Medicine, The Johns Hopkins University School of Medicine Baltimore, MD, USA.
Brian O'RourkeDivision of Cardiology, Department of Medicine, The Johns Hopkins University School of Medicine Baltimore, MD, USA.
D Brian FosterDivision of Cardiology, Department of Medicine, The Johns Hopkins University School of Medicine Baltimore, MD, USA.
Johns Hopkins Medicine · US

Funding

JHU-UMD Diabetes Research CenterP30DK079637 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI AHIMA, REXFORD S. · 2013 to 2017
$9.7M
MItochondrial Dysfunction in Cardiac Hypertrophy and FailureR01HL101235 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI BERS, DONALD M, BLATTER, LOTHAR A · 2010 to 2013
$2.8M
A Systems Biology Approach To Cardiomyopathy in the D. Melanogaster Model SystemR21HL108052 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI FOSTER, D BRIAN, O'ROURKE, BRIAN · 2012 to 2013
$457k
NHLBI NIH HHS R01 HL101235NIDDK NIH HHS P30 DK079637
6 · The paper itself

Abstract

Lysine modifications have been studied extensively in the nucleus, where they play pivotal roles in gene regulation and constitute one of the pillars of epigenetics. In the cytoplasm, they are critical to proteostasis. However, in the last decade we have also witnessed the emergence of mitochondria as a prime locus for post-translational modification (PTM) of lysine thanks, in large measure, to evolving proteomic techniques. Here, we review recent work on evolving set of PTM that arise from the direct reaction of lysine residues with energized metabolic thioester-coenzyme A intermediates, including acetylation, succinylation, malonylation, and glutarylation. We highlight the evolutionary conservation, kinetics, stoichiometry, and cross-talk between members of this emerging family of PTMs. We examine the impact on target protein function and regulation by mitochondrial sirtuins. Finally, we spotlight work in the heart and cardiac mitochondria, and consider the roles acetylation and other newly-found modifications may play in heart disease.

Indexed as

acetylationglutarylationheartmalonylationSirt3Sirt5sirtuinsuccinylation

Identifiers

PMID25228883
PMCPMC4151196
OpenAlexW2121286598

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.