Evidence map›Paper›PMID 33315900›Full record

ArticlePloS one2020

Image-based screen capturing misfolding status of Niemann-Pick type C1 identifies potential candidates for chaperone drugs.

Ryuta Shioi, Fumika Karaki, Hiromasa Yoshioka, Tomomi Noguchi-Yachide, Minoru Ishikawa, Kosuke Dodo, Yuichi Hashimoto, Mikiko Sodeoka, Kenji Ohgane

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 26% 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

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. Alterations in Proteostasis Mechanisms in Niemann-Pick Type C Disease.International journal of molecular sciences · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. 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 at 3 institutions in 1 country.

Ryuta ShioiInstitute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Fumika KarakiInstitute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.ORCID 0000-0002-3815-713X
Hiromasa YoshiokaInstitute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.ORCID 0000-0002-9281-9982
Tomomi Noguchi-YachideInstitute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Minoru IshikawaGraduate School of Life Sciences, Tohoku University, Aoba-ku, Sendai, Japan.
Kosuke DodoSynthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama, Japan.ORCID 0000-0001-6008-2915
Yuichi HashimotoInstitute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Mikiko SodeokaSynthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama, Japan.
Kenji OhganeInstitute for Quantitative Biosciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.ORCID 0000-0003-0565-6503
The University of Tokyo · JPRIKEN · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Niemann-Pick disease type C is a rare, fatal neurodegenerative disorder characterized by massive intracellular accumulation of cholesterol. In most cases, loss-of-function mutations in the NPC1 gene that encodes lysosomal cholesterol transporter NPC1 are responsible for the disease, and more than half of the mutations are considered to interfere with the biogenesis or folding of the protein. We previously identified a series of oxysterol derivatives and phenanthridine-6-one derivatives as pharmacological chaperones, i.e., small molecules that can rescue folding-defective phenotypes of mutated NPC1, opening up an avenue to develop chaperone therapy for Niemann-Pick disease type C. Here, we present an improved image-based screen for NPC1 chaperones and we describe its application for drug-repurposing screening. We identified some azole antifungals, including itraconazole and posaconazole, and a kinase inhibitor, lapatinib, as probable pharmacological chaperones. A photo-crosslinking study confirmed direct binding of itraconazole to a representative folding-defective mutant protein, NPC1-I1061T. Competitive photo-crosslinking experiments suggested that oxysterol-based chaperones and itraconazole share the same or adjacent binding site(s), and the sensitivity of the crosslinking to P691S mutation in the sterol-sensing domain supports the hypothesis that their binding sites are located near this domain. Although the azoles were less effective in reducing cholesterol accumulation than the oxysterol-derived chaperones or an HDAC inhibitor, LBH-589, our findings should offer new starting points for medicinal chemistry efforts to develop better pharmacological chaperones for NPC1.

Indexed as

Drug DiscoveryDrug RepositioningHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsMutationNiemann-Pick C1 ProteinNiemann-Pick Disease, Type CProtein FoldingSmall Molecule LibrariesIntracellular Signaling Peptides and ProteinsNiemann-Pick C1 ProteinNPC1 protein, humanSmall Molecule Libraries

Identifiers

PMID33315900
PMCPMC7735562
OpenAlexW3113310116

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.