Evidence map›Paper›PMID 7720410›Full record

ReviewChromosoma1994

Histone acetylation: facts and questions.

P Loidl

Abstract readReview
PubMed Publisher
In one paragraph

Review in Chromosoma, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 169 citations in OpenAlex.

  1. Article
  2. Protein acetylation in cardiac aging.Journal of molecular and cellular cardiology · 2021
    Review
  3. Heparanase: A Dynamic Promoter of Myeloma Progression.Advances in experimental medicine and biology · 2020
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Altered histone modifications in gliomas.Brain tumor research and treatment · 2014
    Review
  11. Histone-mediated epigenetics in addiction.Progress in molecular biology and translational science · 2014
    Review
  12. Review
  13. Article
  14. Article
  15. Pathways for ischemic cytoprotection: role of sirtuins in caloric restriction, resveratrol, and ischemic preconditioning.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2011
    Review
  16. Article
  17. Article
  18. Review
  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

1 author at 1 institution in 1 country.

P LoidlDepartment of Microbiology, University of Innsbruck-Medical School, Austria.
Innsbruck Medical University · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The DNA of eukaryotic cells is organized in a complex with proteins, either as interphase chromatin or mitotic chromosomes. Nucleosomes, the structural subunits of chromatin, have long been considered as static structures, incompatible with processes occurring in chromatin. During the past few years it has become evident that the histone part of the nucleosome has important regulatory functions. Some of these functions are mediated by the N-terminal core histone domains which contain sites for posttranslational modifications, among them lysine residues for reversible acetylation. Recent results indicate that acetylation and deacetylation of N-terminal lysines of nucleosomal core histones represent a means of molecular communication between chromatin and the cellular signal transduction network, resulting in heritable epigenetic information. Data on enzymes involved in acetylation and the pattern of acetylated lysine sites on chromosomes, as well as genetic data on yeast transcriptional repression, suggest that acetylation may lead to structural transitions as well as specific signalling within distinct chromatin domains.

Indexed as

Protein Processing, Post-TranslationalSaccharomyces cerevisiae ProteinsSignal TransductionAcetylationAcetyltransferasesAnimalsChromatinChromosomal Proteins, Non-HistoneDrosophilaFungal ProteinsGene Expression Regulation, FungalHistone AcetyltransferasesHistone DeacetylasesHistonesLysineMaleAcetyltransferasesChromatinChromosomal Proteins, Non-HistoneFungal ProteinsHistone AcetyltransferasesHistone DeacetylasesHistonesLysineNucleosomesSaccharomyces cerevisiae Proteins

Identifiers

PMID7720410
OpenAlexW2033607377

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.