Evidence map›Paper›PMID 32683534›Full record

ReviewCellular and molecular life sciences : CMLS2021

Regulation of histone deacetylase activities and functions by phosphorylation and its physiological relevance.

Sonali Bahl, Edward Seto

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed, 1 pooled it
2.9field-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

54 citing papers in PubMed, 1 synthesis or guideline pooled it, 80 citations in OpenAlex.

  1. Pooled it
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  7. Harnessing Substituted 4-Chlorothieno[2,3-Pharmaceuticals (Basel, Switzerland) · 2026
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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.

Sonali BahlDepartment of Biochemistry & Molecular Medicine, School of Medicine & Health Sciences, George Washington Cancer Center, George Washington University, Washington, DC, 20037, USA.ORCID http://orcid.org/0000-0003-1035-1122
Edward SetoDepartment of Biochemistry & Molecular Medicine, School of Medicine & Health Sciences, George Washington Cancer Center, George Washington University, Washington, DC, 20037, USA. seto@gwu.edu.ORCID http://orcid.org/0000-0001-7562-7316
George Washington University · US

Funding

Targeting SIRT1 in Mantle Cell LymphomaR01CA187040 · NCI · H. LEE MOFFITT CANCER CTR & RES INST · PI SETO, EDWARD · 2014 to 2018
$1.6M
The Basic and Translational Implication of SIRT1 and DNMT1 in CancerR01CA169210 · NCI · H. LEE MOFFITT CANCER CTR & RES INST · PI SETO, EDWARD · 2012 to 2016
$1.6M
NCI NIH HHS R01 CA169210NCI NIH HHS R01CA169210NCI NIH HHS R01 CA187040NCI NIH HHS R01CA187040
6 · The paper itself

Abstract

Histone deacetylases (HDACs) are conserved enzymes that regulate many cellular processes by catalyzing the removal of acetyl groups from lysine residues on histones and non-histone proteins. As appropriate for proteins that occupy such an essential biological role, HDAC activities and functions are in turn highly regulated. Overwhelming evidence suggests that the dysregulation of HDACs plays a major role in many human diseases. The regulation of HDACs is achieved by multiple different mechanisms, including posttranslational modifications. One of the most common posttranslational modifications on HDACs is reversible phosphorylation. Many HDAC phosphorylations are context-dependent, occurring in specific tissues or as a consequence of certain stimuli. Additionally, whereas phosphorylation can regulate some HDACs in a non-specific manner, many HDAC phosphorylations result in specific consequences. Although some of these modifications support normal HDAC function, aberrations can contribute to disease development. Here we review and critically evaluate how reversible phosphorylation activates or deactivates HDACs and, thereby, regulates their many functions under various cellular and physiological contexts.

Indexed as

AnimalsEnzyme ActivationEnzyme StabilityHistone DeacetylasesHistonesHumansMitosisPhosphorylationProtein Processing, Post-TranslationalSubstrate SpecificityHistone DeacetylasesHistonesCell signalingEpigeneticsHistone deacetylasePhosphorylation

Identifiers

PMID32683534
PMCPMC7854769
OpenAlexW3042981957

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.