Evidence map›Paper›PMID 39825060›Full record

ReviewCell biochemistry and biophysics2025

Histone Deacetylation in Alzheimer's Diseases (AD); Hope or Hype.

Nabaa Hisham Ateya, Sarah F Al-Taie, Saade Abdalkareem Jasim, Subasini Uthirapathy, Kamlesh Chaudhary, Pooja Rani, Mayank Kundlas, K Satyam Naidu, Nevin Adel Amer, Jawad Kadhim Ahmed

Abstract readReview
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In one paragraph

Review in Cell biochemistry and biophysics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

10 authors.

Nabaa Hisham AteyaBiotechnology Department, College of Applied Science, Fallujah University, Al-Fallujah, Iraq.
Sarah F Al-TaieUniversity of Baghdad, College of Science, Department of Biotechnology, Baghdad, Iraq.
Saade Abdalkareem JasimMedical Laboratory Techniques department, College of Health and Medical Technology, University of Al-maarif, Anbar, Ramadi, Iraq. saade.a.j@uoa.edu.iq.
Subasini UthirapathyPharmacy Department, Tishk International University Erbil, Kurdistan Region, Erbil, Iraq.
Kamlesh ChaudharyDepartment of Neurology, National Institute of Medical Sciences, NIMS University Rajasthan, Jaipur, India.
Pooja RaniDepartment of Pharmacy, Chandigarh Pharmacy College, Chandigarh Group of Colleges-Jhanjeri, Mohali, 140307, Punjab, India.
Mayank KundlasCentre for Research Impact & Outcome, Chitkara University Institute of Engineering and Technology, Chitkara University, Rajpura, 140401, Punjab, India.
K Satyam NaiduDepartment of Chemistry, Raghu Engineering College, Visakhapatnam, Andhra Pradesh, 531162, India.
Nevin Adel AmerNursing Department, College of Applied Medical Sciences, Jouf University, Sakakah, Saudi Arabia.
Jawad Kadhim AhmedDepartment of Medical Laboratories Technology, AL-Nisour University College, Baghdad, Iraq.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone acetylation is the process by which histone acetyltransferases (HATs) add an acetyl group to the N-terminal lysine residues of histones, resulting in a more open chromatin structure. Histone acetylation tends to increase gene expression more than methylation does. In the central nervous system (CNS), histone acetylation is essential for controlling the expression of genes linked to cognition and learning. Histone deacetylases (HDACs), "writing" enzymes (HATs), and "reading" enzymes with bromodomains that identify and localize to acetylated lysine residues are responsible for maintaining histone acetylation. By giving animals HDAC inhibitors (HDACis), it is possible to intentionally control the ratios of "writer" and "eraser" activity, which will change the acetylation of histones. In addition to making the chromatin more accessible, these histone acetylation alterations re-allocate the targeting of "readers," including the transcriptional co-activators, cAMP response element-binding protein (CBP), and bromodomain-containing protein 4 (Brd4) in the CNS. Conclusive evidence has shown that HDACs slow down the progression of Alzheimer's disease (AD) by reducing the amount of histone acetylation, decreasing the activity of genes linked to memory, supporting cognitive decline and Amyloid beta (Aβ) protein accumulation, influencing aberrant tau phosphorylation, and promoting the emergence of neurofibrillary tangles (NFTs). In this review, we have covered the therapeutic targets and functions of HDACs that might be useful in treating AD.

Indexed as

Alzheimer DiseaseHistonesAcetylationAnimalsHistone Deacetylase InhibitorsHistone DeacetylasesHumansHistone Deacetylase InhibitorsHistone DeacetylasesHistonesAlzheimer’s disease (AD)Amyloid beta (Aβ)Histone deacetylase (HDAC)Histone deacetylase inhibitor (HDACi)Neurofibrillary tangles (NFTs)

Identifiers

PMID39825060

What OpenQuestion holds

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Registered trials

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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.