Evidence map›Paper›PMID 24449617›Full record

ReviewChemMedChem2014

Lysine deacetylase (KDAC) regulatory pathways: an alternative approach to selective modulation.

Michael W Van Dyke

Abstract readReview
In one paragraph

Review in ChemMedChem, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

20 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
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  9. Article
  10. A bismuth diethyldithiocarbamate compound induced apoptosis via mitochondria-dependent pathway and suppressed invasion in MCF-7 breast cancer cells.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021
    Article
  11. Review
  12. Article
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  14. Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020
    Review
  15. Article
  16. Review
  17. Article
  18. Sirt7 promotes adipogenesis in the mouse by inhibiting autocatalytic activation of Sirt1.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Article
  20. Review
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.

Michael W Van DykeDepartment of Chemistry & Biochemistry, Kennesaw State University, 1000 Chastain Road, MD# 1203, Kennesaw, GA 30144 (USA). mvandyk2@kennesaw.edu.
Kennesaw State University · US

Funding

DNA-Binding Protein Discovery by the Combinatorial Method REPSAR15GM104833 · NIGMS · KENNESAW STATE UNIVERSITY · PI VAN DYKE, MICHAEL W · 2013 to 2013
$270k
NIGMS NIH HHS GM 104833NIGMS NIH HHS R15 GM104833
6 · The paper itself

Abstract

Protein lysine deacetylases (KDACs), including the classic Zn(2+) -dependent histone deacetylases (HDACs) and the nicotinamide adenine dinucleotide (NAD(+) )-requiring sirtuins, are enzymes that play critical roles in numerous biological processes, particularly the epigenetic regulation of global gene expression programs in response to internal and external cues. Dysregulation of KDACs is characteristic of several human diseases, including chronic metabolic, neurodegenerative, and cardiovascular diseases and many cancers. This has led to the development of KDAC modulators, two of which (HDAC inhibitors vorinostat and romidepsin) have been approved for the treatment of cutaneous T cell lymphoma. By their nature, existing KDAC modulators are relatively nonspecific, leading to pan-KDAC changes and undesired side effects. Given that KDACs are regulated at many levels, including transcriptional, post-translational, subcellular localization, and through their complexation with other proteins, it should be possible to affect specific KDAC activity through manipulation of endogenous signaling pathways. In this Minireview, we discuss our present knowledge of the cellular controls of KDAC activity and examples of their pharmacologic regulation.

Indexed as

Histone Deacetylase InhibitorsHistone DeacetylasesHumansLysineMolecular StructureSirtuinsStructure-Activity RelationshipHistone Deacetylase InhibitorsHistone DeacetylasesLysineSirtuinsepigeneticshistone deacetylases (HDACs)homeostasislysine deacetylases (KDACs)multiprotein complexespharmacologic regulationsirtuins

Identifiers

PMID24449617
PMCPMC4105970
OpenAlexW2131105039

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.