Evidence map›Paper›PMID 27098312›Full record

ReviewExpert review of proteomics2016

Progress and potential of non-inhibitory small molecule chaperones for the treatment of Gaucher disease and its implications for Parkinson disease.

Olive Jung, Samarjit Patnaik, Juan Marugan, Ellen Sidransky, Wendy Westbroek

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Expert review of proteomics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

37 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. International journal of molecular sciences · 2024
    Review
  3. Review
  4. Glucocerebrosidase mutations and Parkinson disease.Journal of neural transmission (Vienna, Austria : 1996) · 2022
    Review
  5. Review
  6. Cells · 2022
    Review
  7. Genetic variations inFrontiers in neurology · 2022
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. A Pharmacological Chaperone Therapy for Acute Intermittent Porphyria.Molecular therapy : the journal of the American Society of Gene Therapy · 2020
    Article
  17. Review
  18. Small Molecule Chaperones for the Treatment of Gaucher Disease andFrontiers in cell and developmental biology · 2020
    Review
  19. Review
  20. Article
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

5 authors at 2 institutions in 1 country.

Olive Junga Section on Molecular Neurogenetics, Medical Genetics Branch , National Human Genome Research Institute, NIH , Bethesda , MD , USA.
Samarjit Patnaikb National Center for Advancing Translational Sciences , National Institutes of Health , Bethesda , MD , USA.
Juan Maruganb National Center for Advancing Translational Sciences , National Institutes of Health , Bethesda , MD , USA.
Ellen Sidranskya Section on Molecular Neurogenetics, Medical Genetics Branch , National Human Genome Research Institute, NIH , Bethesda , MD , USA.
Wendy Westbroeka Section on Molecular Neurogenetics, Medical Genetics Branch , National Human Genome Research Institute, NIH , Bethesda , MD , USA.
National Human Genome Research Institute · USNational Center for Advancing Translational Sciences · US

Funding

Genetic and clinical studies of Gaucher disease and other lysosomal disordersZIAHG200336 · NHGRI · NATIONAL HUMAN GENOME RESEARCH INSTITUTE · PI SIDRANSKY, ELLEN · 2009 to 2025
$45.2M
Small molecule screening programZ01HG200319 · NHGRI · NATIONAL HUMAN GENOME RESEARCH INSTITUTE · PI AUSTIN, CHRISTOPHER P · 2004 to 2008
$32.3M
Intramural NIH HHS Z01 HG200319
6 · The paper itself

Abstract

Gaucher disease, caused by pathological mutations GBA1, encodes the lysosome-resident enzyme glucocerebrosidase, which cleaves glucosylceramide into glucose and ceramide. In Gaucher disease, glucocerebrosidase deficiency leads to lysosomal accumulation of substrate, primarily in cells of the reticulo-endothelial system. Gaucher disease has broad clinical heterogeneity, and mutations in GBA1 are a risk factor for the development of different synucleinopathies. Insights into the cell biology and biochemistry of glucocerebrosidase have led to new therapeutic approaches for Gaucher disease including small chemical chaperones. Such chaperones facilitate proper enzyme folding and translocation to lysosomes, thereby preventing premature breakdown of the enzyme in the proteasome. This review discusses recent progress in developing chemical chaperones as a therapy for Gaucher disease, with implications for the treatment of synucleinopathies. It focuses on the development of non-inhibitory glucocerebrosidase chaperones and their therapeutic advantages over inhibitory chaperones, as well as the challenges involved in identifying and validating chemical chaperones.

Indexed as

Gaucher DiseaseGlucosylceramidaseHumansMutationParkinson DiseaseProtein FoldingSynucleinsGlucosylceramidaseSynucleinschemical chaperoneGaucher diseaseglucocerebrosidasehigh throughput screeningLysosomal storage diseasesParkinson diseasesynculeinopathies

Identifiers

PMID27098312
PMCPMC5381920
OpenAlexW2340165674

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.