Evidence map›Paper›PMID 25746103›Full record

ReviewCritical reviews in oncogenesis2015

Histone deacetylases and mechanisms of regulation of gene expression.

Hong Ping Chen, Yu Tina Zhao, Ting C Zhao

Abstract readReview
In one paragraph

Review in Critical reviews in oncogenesis, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 171 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
171citing papers in PubMed, 1 pooled it
10.4field-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

171 citing papers in PubMed, 1 synthesis or guideline pooled it, 285 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Advances in applications of siRNA in cancer therapy: challenges and opportunities.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026
    Review
  6. Review
  7. Article
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  9. Review
  10. Article
  11. Article
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  13. Synthesis and crystal structure of HDAC6 selective inhibitor ofActa crystallographica. Section E, Crystallographic communications · 2026
    Article
  14. Article
  15. Review
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111 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 2 countries.

Hong Ping ChenDepartment of Surgery, Boston University Medical School, Boston University, Roger Williams Medical Center, Providence, RI; Department of Histology and Embryology, Medical College, Nanchang University, Nanchang, China.
Yu Tina ZhaoDepartment of Surgery, Boston University Medical School, Boston University, Roger Williams Medical Center, Providence, RI.
Ting C ZhaoDepartment of Surgery, Boston University Medical School, Boston University, Roger Williams Medical Center, Providence, RI.
Boston University · USNanchang University · CN

Funding

Histone Deacetylase Inhibition: A Novel Approach to CardioprotectionR01HL089405 · NHLBI · ROGER WILLIAMS MEDICAL CENTER · PI ZHAO, TING C · 2009 to 2020
$3.4M
p38 acetylation: Novel signaling mechanisms and myocardial protectionR01HL115265 · NHLBI · ROGER WILLIAMS MEDICAL CENTER · PI ZHAO, TING C · 2013 to 2016
$1.6M
NHLBI NIH HHS R01 HL089405NHLBI NIH HHS R01 HL115265
6 · The paper itself

Abstract

In recent years it has become widely recognized that histone modification plays a pivotal role in controlling gene expression and is involved in a wide spectrum of disease regulation. Histone acetylation is a major modification that affects gene transcription and is controlled by histone acetyltransferases (HATs) and histone deacetylases (HDACs). HATs acetylate lysines of histone proteins, resulting in the relaxation of chromatin structure, and they also facilitate gene activation. Conversely, HDACs remove acetyl groups from hyperacetylated histones and suppress general gene transcription. In addition to histones, numerous nonhistone proteins can be acetylated and deacetylated, and they also are involved in the regulation of a wide range of diseases. To date there are 18 HDACs in mammals classified into 4 classes based on homology to yeast HDACs. Accumulating evidence has revealed that HDACs play crucial roles in a variety of biological processes including inflammation, cell proliferation, apoptosis, and carcinogenesis. In this review we summarize the current state of knowledge of HDACs in carcinogenesis and describe the involvement of HDACs in cancer-associated molecular processes. It is hoped than an understanding of the role of HDACs in cancer will lead to the design of more potent and specific drugs targeting selective HDAC proteins for the treatment of the disease.

Indexed as

Gene Expression RegulationAnimalsCarcinoma, HepatocellularColonic NeoplasmsFemaleHematologic NeoplasmsHistone Deacetylase InhibitorsHistone DeacetylasesHumansInflammationLiver NeoplasmsMaleUrogenital NeoplasmsHistone Deacetylase InhibitorsHistone Deacetylases

Identifiers

PMID25746103
PMCPMC4809735
OpenAlexW2028391746

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.