Evidence map›Paper›PMID 26822488›Full record

ReviewTrends in biochemical sciences2016

Mechanisms and Dynamics of Protein Acetylation in Mitochondria.

Josue Baeza, Michael J Smallegan, John M Denu

Open access · bronzeAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers.

0numbers the graph read from it
0cells of the map it votes in
190citing papers in PubMed
16.0field-weighted citation impact, top 1% 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

190 citing papers in PubMed, 314 citations in OpenAlex.

  1. Trial
  2. Review
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  7. Review
  8. BLOC1S1 depletion via splice-switching oligonucleotides improves mitochondrial respiration and rescues ALS phenotypes.Molecular therapy : the journal of the American Society of Gene Therapy · 2026
    Article
  9. Article
  10. Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026
    Review
  11. Article
  12. Atlas of lysine acetylation in the mouse.bioRxiv : the preprint server for biology · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

130 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

3 authors at 2 institutions in 1 country.

Josue BaezaDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI 53715, USA; Wisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI 53715, USA.
Michael J SmalleganWisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI 53715, USA.
John M DenuDepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI 53715, USA; Wisconsin Institute for Discovery, University of Wisconsin-Madison, Madison, WI 53715, USA. Electronic address: john.denu@wisc.edu.
Wisconsin Institutes for Discovery · USUniversity of Wisconsin–Madison · US

Funding

GRADUATE TRAINING IN MOLECULAR BIOSCIENCEST32GM007215 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HULL, CHRISTINA M · 1985 to 2018
$22.5M
Reversible protein acetylation and sirtuin functionR01GM065386 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 2003 to 2022
$7.3M
NIGMS NIH HHS GM065386NIGMS NIH HHS R01 GM065386NIGMS NIH HHS T32 GM007215
6 · The paper itself

Abstract

Reversible protein acetylation is a major regulatory mechanism for controlling protein function. Through genetic manipulations, dietary perturbations, and new proteomic technologies, the diverse functions of protein acetylation are coming into focus. Protein acetylation in mitochondria has taken center stage, revealing that 63% of mitochondrially localized proteins contain lysine acetylation sites. We summarize the field and discuss salient topics that cover spurious versus targeted acetylation, the role of SIRT3 deacetylation, nonenzymatic acetylation, and molecular models for regulatory acetylations that display high and low stoichiometry.

Indexed as

AcetylationMitochondriaProteinsProteinsacetylationacylationmetabolic regulationmitochondrianonenzymaticstoichiometry

Identifiers

PMID26822488
PMCPMC4783225
OpenAlexW2250423544

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.