Evidence map›Paper›PMID 25326522›Full record

ReviewEukaryotic cell2014

Protein acetylation and acetyl coenzyme a metabolism in budding yeast.

Luciano Galdieri, Tiantian Zhang, Daniella Rogerson, Rron Lleshi, Ales Vancura

Open access · diamondAbstract readReview
In one paragraph

Review in Eukaryotic cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed, 1 pooled it
3.1field-weighted citation impact, top 8% 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

67 citing papers in PubMed, 1 synthesis or guideline pooled it, 127 citations in OpenAlex.

  1. Guideline
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. NADCells · 2025
    Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Metabolic transitions regulate global protein fatty acylation.The Journal of biological chemistry · 2024
    Article
  18. Article
  19. Article
  20. Article

7 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

5 authors at 1 institution in 1 country.

Luciano GaldieriDepartment of Biological Sciences, St. John's University, Queens, New York, USA.
Tiantian ZhangDepartment of Biological Sciences, St. John's University, Queens, New York, USA.
Daniella RogersonDepartment of Biological Sciences, St. John's University, Queens, New York, USA.
Rron LleshiDepartment of Biological Sciences, St. John's University, Queens, New York, USA.
Ales VancuraDepartment of Biological Sciences, St. John's University, Queens, New York, USA vancuraa@stjohns.edu.
St. John's University · US

Funding

Intermediary Metabolism, Histone Acetylation, and Transcriptional RegulationR15GM106324 · NIGMS · ST. JOHN'S UNIVERSITY · PI VANCURA, ALES · 2013 to 2013
$377k
NIGMS NIH HHS GM106324NIGMS NIH HHS R15 GM106324
6 · The paper itself

Abstract

Cells sense and appropriately respond to the physical conditions and availability of nutrients in their environment. This sensing of the environment and consequent cellular responses are orchestrated by a multitude of signaling pathways and typically involve changes in transcription and metabolism. Recent discoveries suggest that the signaling and transcription machineries are regulated by signals which are derived from metabolism and reflect the metabolic state of the cell. Acetyl coenzyme A (CoA) is a key metabolite that links metabolism with signaling, chromatin structure, and transcription. Acetyl-CoA is produced by glycolysis as well as other catabolic pathways and used as a substrate for the citric acid cycle and as a precursor in synthesis of fatty acids and steroids and in other anabolic pathways. This central position in metabolism endows acetyl-CoA with an important regulatory role. Acetyl-CoA serves as a substrate for lysine acetyltransferases (KATs), which catalyze the transfer of acetyl groups to the epsilon-amino groups of lysines in histones and many other proteins. Fluctuations in the concentration of acetyl-CoA, reflecting the metabolic state of the cell, are translated into dynamic protein acetylations that regulate a variety of cell functions, including transcription, replication, DNA repair, cell cycle progression, and aging. This review highlights the synthesis and homeostasis of acetyl-CoA and the regulation of transcriptional and signaling machineries in yeast by acetylation.

Indexed as

AcetylationAcetyl Coenzyme AAnimalsHomeostasisHumansProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAcetyl Coenzyme ASaccharomyces cerevisiae Proteins

Identifiers

PMID25326522
PMCPMC4248685
OpenAlexW1996782134

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.