Evidence map›Paper›PMID 20553216›Full record

ReviewExpert review of anticancer therapy2010

Nonhistone protein acetylation as cancer therapy targets.

Brahma N Singh, Guanghua Zhang, Yi L Hwa, Jinping Li, Sean C Dowdy, Shi-Wen Jiang

Abstract readReview
In one paragraph

Review in Expert review of anticancer therapy, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 155 papers.

0numbers the graph read from it
0cells of the map it votes in
155citing papers in PubMed
–field-weighted citation impact
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

155 citing papers in PubMed.

  1. Article
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  9. Article
  10. Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
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  16. Activity-Based Acylome Profiling withJournal of the American Chemical Society · 2024
    Article
  17. Review
  18. Review
  19. Review
  20. Review

95 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

6 authors.

Brahma N SinghDepartment of Mycology & Plant Pathology, Institute of Agricultural Sciences, Banaras Hindu University, Varanasi, India.
Guanghua Zhang
Yi L Hwa
Jinping Li
Sean C Dowdy
Shi-Wen Jiang

Funding

Transcription Enhancer Factor Control of Placental GenesR01HD041577 · NICHD · MERCER UNIVERSITY MACON · PI JIANG, SHI-WEN · 2003 to 2007
$1.3M
NICHD NIH HHS R01 HD041577NICHD NIH HHS R01 HD 41577
6 · The paper itself

Abstract

Acetylation and deacetylation are counteracting, post-translational modifications that affect a large number of histone and nonhistone proteins. The significance of histone acetylation in the modification of chromatin structure and dynamics, and thereby gene transcription regulation, has been well recognized. A steadily growing number of nonhistone proteins have been identified as acetylation targets and reversible lysine acetylation in these proteins plays an important role(s) in the regulation of mRNA stability, protein localization and degradation, and protein-protein and protein-DNA interactions. The recruitment of histone acetyltransferases (HATs) and histone deacetylases (HDACs) to the transcriptional machinery is a key element in the dynamic regulation of genes controlling cellular proliferation, differentiation and apoptosis. Many nonhistone proteins targeted by acetylation are the products of oncogenes or tumor-suppressor genes and are directly involved in tumorigenesis, tumor progression and metastasis. Aberrant activity of HDACs has been documented in several types of cancers and HDAC inhibitors (HDACi) have been employed for therapeutic purposes. Here we review the published literature in this field and provide updated information on the regulation and function of nonhistone protein acetylation. While concentrating on the molecular mechanism and pathways involved in the addition and removal of the acetyl moiety, therapeutic modalities of HDACi are also discussed.

Indexed as

AcetylationChromosomal Proteins, Non-HistoneHistone Deacetylase InhibitorsHumansNeoplasmsChromosomal Proteins, Non-HistoneHistone Deacetylase Inhibitors

Identifiers

PMID20553216
PMCPMC3273412

What OpenQuestion holds

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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.