Evidence map›Paper›PMID 23277556›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Histone deacetylase inhibitors increase glucocerebrosidase activity in Gaucher disease by modulation of molecular chaperones.

Chunzhang Yang, Shervin Rahimpour, Jie Lu, Karel Pacak, Barbara Ikejiri, Roscoe O Brady, Zhengping Zhuang

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.4field-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

57 citing papers in PubMed, 78 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Unifying biology of neurodegeneration in lysosomal storage diseases.Journal of inherited metabolic disease · 2025
    Review
  7. Article
  8. International journal of molecular sciences · 2024
    Review
  9. Lysosomal storage, impaired autophagy and innate immunity in Gaucher and Parkinson's diseases: insights for drug discovery.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  10. Article
  11. Autophagy: Regulator of cell death.Cell death & disease · 2023
    Review
  12. Proteostasis Modulation in Germline Missense von Hippel Lindau Disease.Clinical cancer research : an official journal of the American Association for Cancer Research · 2023
    Article
  13. Review
  14. Cells · 2022
    Review
  15. Genetic variations inFrontiers in neurology · 2022
    Review
  16. Review
  17. Article
  18. Article
  19. TheAnnals of translational medicine · 2020
    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

7 authors at 2 institutions in 1 country.

Chunzhang YangSurgical Neurology Branch, National Institute of Neurological Disorders and Stroke, and Program in Reproductive and Adult Endocrinology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Shervin Rahimpour
Jie Lu
Karel Pacak
Barbara Ikejiri
Roscoe O Brady
Zhengping Zhuang
National Institute of Neurological Disorders and Stroke · USNational Institutes of Health · US

Funding

Molecular Pathogenesis of NeoplasiaZIANS003052 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI HEISS, JOHN · 2009 to 2025
$20.7M
Intramural NIH HHS
6 · The paper itself

Abstract

Gaucher disease is caused by mutations of the GBA gene that encodes the lysosomal enzyme glucocerebrosidase (GCase). GBA mutations often result in protein misfolding and premature degradation, but usually exert less effect on catalytic activity. In this study, we identified the molecular mechanism by which histone deacetylase inhibitors increase the quantity and activity of GCase. Specifically, these inhibitors limit the deacetylation of heat shock protein 90, resulting in less recognition of the mutant peptide and GCase degradation. These findings provide insight into a possible therapeutic strategy for Gaucher disease and other genetic disorders by modifying molecular chaperone and protein degradation pathways.

Indexed as

AcetylationEndoplasmic Reticulum-Associated DegradationGaucher DiseaseGlucosylceramidaseHistone Deacetylase InhibitorsHSP90 Heat-Shock ProteinsHumansModels, BiologicalMolecular ChaperonesMutagenesis, Site-DirectedMutant ProteinsMutationProtein FoldingRecombinant ProteinsGlucosylceramidaseHistone Deacetylase InhibitorsHSP90AB1 protein, humanHSP90 Heat-Shock ProteinsMolecular ChaperonesMutant ProteinsRecombinant Proteins

Identifiers

PMID23277556
PMCPMC3549125
OpenAlexW2033125252

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.