Evidence map›Paper›PMID 37818566›Full record

ReviewMini reviews in medicinal chemistry2024

HDAC9 as a Privileged Target: Reviewing its Role in Different Diseases and Structure-activity Relationships (SARs) of its Inhibitors.

Totan Das, Samima Khatun, Tarun Jha, Shovanlal Gayen

Abstract readReview
PubMed Publisher
In one paragraph

Review in Mini reviews in medicinal chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Exploring Neutrophil Extracellular Traps in Cardiovascular Pathologies: The Impact of Lipid Profiles, PAD4, and Radiation.Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al · 2025
    Article
  3. 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

4 authors at 1 institution in 1 country.

Totan DasDepartment of Pharmaceutical Technology, Laboratory of Drug Design and Discovery, Jadavpur University, Kolkata, 700032, India.
Samima KhatunDepartment of Pharmaceutical Technology, Laboratory of Drug Design and Discovery, Jadavpur University, Kolkata, 700032, India.ORCID 0000-0002-3322-9915
Tarun JhaDepartment of Pharmaceutical Technology, Natural Science Laboratory, Division of Medicinal and Pharmaceutical Chemistry, Jadavpur University, Kolkata, 700032, India.ORCID 0000-0002-9996-738X
Shovanlal GayenDepartment of Pharmaceutical Technology, Laboratory of Drug Design and Discovery, Jadavpur University, Kolkata, 700032, India.ORCID 0000-0002-3367-578X
Jadavpur University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

HDAC9 is a histone deacetylase enzyme belonging to the class IIa of HDACs which catalyses histone deacetylation. HDAC9 inhibit cell proliferation by repairing DNA, arresting the cell cycle, inducing apoptosis, and altering genetic expression. HDAC9 plays a significant part in human physiological system and are involved in various type of diseases like cancer, diabetes, atherosclerosis and CVD, autoimmune response, inflammatory disease, osteoporosis and liver fibrosis. This review discusses the role of HDAC9 in different diseases and structure-activity relationships (SARs) of various hydroxamate and non-hydroxamate-based inhibitors. SAR of compounds containing several scaffolds have been discussed in detail. Moreover, structural requirements regarding the various components of HDAC9 inhibitor (cap group, linker and zinc-binding group) has been highlighted in this review. Though, HDAC9 is a promising target for the treatment of a number of diseases including cancer, a very few research are available. Thus, this review may provide useful information for designing novel HDAC9 inhibitors to fight against different diseases in the future.

Indexed as

Histone Deacetylase InhibitorsHistone DeacetylasesNeoplasmsRepressor ProteinsAnimalsAtherosclerosisDiabetes MellitusHumansOsteoporosisStructure-Activity RelationshipHDAC9 protein, humanHistone Deacetylase InhibitorsHistone DeacetylasesRepressor ProteinscancerEpigeneticHDAC9 inhibitorSARs.selectivitystructure-activity relationships

Identifiers

PMID37818566
OpenAlexW4387515812

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.