Evidence map›Paper›PMID 38918466›Full record

ArticleScientific reports2024

A novel insight into neurological disorders through HDAC6 protein-protein interactions.

Nasim Bahram Sangani, Jarno Koetsier, Jonathan Mélius, Martina Kutmon, Friederike Ehrhart, Chris T Evelo, Leopold M G Curfs, Chris P Reutelingsperger, Lars M T Eijssen

Abstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Review
  3. Molecular and cellular mechanisms of pentadecanoic acid.World journal of biological chemistry · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. 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

9 authors.

Nasim Bahram SanganiDepartment of Biochemistry, Cardiovascular Research Institute Maastricht (CARIM), Maastricht University, 6200 MD, Maastricht, The Netherlands. nasim.sangani@maastrichtuniversity.nl.
Jarno KoetsierDepartment of Biochemistry, Cardiovascular Research Institute Maastricht (CARIM), Maastricht University, 6200 MD, Maastricht, The Netherlands.
Jonathan MéliusDataHub, Maastricht University & Maastricht UMC+, P. Debyelaan 15, 6229 HX, Maastricht, The Netherlands.
Martina KutmonMaastricht Centre for Systems Biology (MaCSBio), Maastricht University, 6200 MD, Maastricht, The Netherlands.
Friederike EhrhartDepartment of Bioinformatics - BiGCaT, Research Institute of Nutrition and Translational Research in Metabolism (NUTRIM), Maastricht University, 6200 MD, Maastricht, The Netherlands.
Chris T EveloMaastricht Centre for Systems Biology (MaCSBio), Maastricht University, 6200 MD, Maastricht, The Netherlands.
Leopold M G CurfsGKC, Maastricht University Medical Centre, 6229 ER, Maastricht, The Netherlands.
Chris P ReutelingspergerDepartment of Biochemistry, Cardiovascular Research Institute Maastricht (CARIM), Maastricht University, 6200 MD, Maastricht, The Netherlands.
Lars M T EijssenDepartment of Bioinformatics - BiGCaT, Research Institute of Nutrition and Translational Research in Metabolism (NUTRIM), Maastricht University, 6200 MD, Maastricht, The Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Due to its involvement in physiological and pathological processes, histone deacetylase 6 (HDAC6) is considered a promising pharmaceutical target for several neurological manifestations. However, the exact regulatory role of HDAC6 in the central nervous system (CNS) is still not fully understood. Hence, using a semi-automated literature screening technique, we systematically collected HDAC6-protein interactions that are experimentally validated and reported in the CNS. The resulting HDAC6 network encompassed 115 HDAC6-protein interactions divided over five subnetworks: (de)acetylation, phosphorylation, protein complexes, regulatory, and aggresome-autophagy subnetworks. In addition, 132 indirect interactions identified through HDAC6 inhibition were collected and categorized. Finally, to display the application of our HDAC6 network, we mapped transcriptomics data of Alzheimer's disease, Parkinson's disease, and Amyotrophic Lateral Sclerosis on the network and highlighted that in the case of Alzheimer's disease, alterations predominantly affect the HDAC6 phosphorylation subnetwork, whereas differential expression within the deacetylation subnetwork is observed across all three neurological disorders. In conclusion, the HDAC6 network created in the present study is a novel and valuable resource for the understanding of the HDAC6 regulatory mechanisms, thereby providing a framework for the integration and interpretation of omics data from neurological disorders and pharmacodynamic assessments.

Indexed as

Histone Deacetylase 6Protein Interaction MapsAcetylationAlzheimer DiseaseHumansNervous System DiseasesParkinson DiseasePhosphorylationHDAC6 protein, humanHistone Deacetylase 6Alzheimer’s diseaseAmyotrophic lateral sclerosisCentral nervous systemHistone deacetylase 6 (HDAC6)Parkinson’s diseaseProtein–protein interactions

Identifiers

PMID38918466
PMCPMC11199618

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.