Evidence map›Paper›PMID 10839822›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2000

Acetylation of histones and transcription-related factors.

D E Sterner, S L Berger

Abstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 720 papers.

0numbers the graph read from it
0cells of the map it votes in
720citing papers in PubMed
34.2field-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

720 citing papers in PubMed, 1,751 citations in OpenAlex.

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660 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

2 authors at 1 institution in 1 country.

D E SternerThe Wistar Institute, Philadelphia, Pennsylvania 19104, USA.
S L Berger
The Wistar Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The state of chromatin (the packaging of DNA in eukaryotes) has long been recognized to have major effects on levels of gene expression, and numerous chromatin-altering strategies-including ATP-dependent remodeling and histone modification-are employed in the cell to bring about transcriptional regulation. Of these, histone acetylation is one of the best characterized, as recent years have seen the identification and further study of many histone acetyltransferase (HAT) proteins and their associated complexes. Interestingly, most of these proteins were previously shown to have coactivator or other transcription-related functions. Confirmed and putative HAT proteins have been identified from various organisms from yeast to humans, and they include Gcn5-related N-acetyltransferase (GNAT) superfamily members Gcn5, PCAF, Elp3, Hpa2, and Hat1: MYST proteins Sas2, Sas3, Esa1, MOF, Tip60, MOZ, MORF, and HBO1; global coactivators p300 and CREB-binding protein; nuclear receptor coactivators SRC-1, ACTR, and TIF2; TATA-binding protein-associated factor TAF(II)250 and its homologs; and subunits of RNA polymerase III general factor TFIIIC. The acetylation and transcriptional functions of these HATs and the native complexes containing them (such as yeast SAGA, NuA4, and possibly analogous human complexes) are discussed. In addition, some of these HATs are also known to modify certain nonhistone transcription-related proteins, including high-mobility-group chromatin proteins, activators such as p53, coactivators, and general factors. Thus, we also detail these known factor acetyltransferase (FAT) substrates and the demonstrated or potential roles of their acetylation in transcriptional processes.

Indexed as

Saccharomyces cerevisiae ProteinsAcetylationAcetyltransferasesAnimalsGene Products, tatHigh Mobility Group ProteinsHistone AcetyltransferasesHistonesHumansNucleosomesTranscription FactorsAcetyltransferasesGene Products, tatHigh Mobility Group ProteinsHistone AcetyltransferasesHistonesKAT7 protein, humanKAT8 protein, humanNucleosomesSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID10839822
PMCPMC98999
OpenAlexW2096501714

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.