Evidence map›Paper›PMID 36404287›Full record

ArticleProteins2023

In silico modeling human VPS13 proteins associated with donor and target membranes suggests lipid transfer mechanisms.

Filippo Dall'Armellina, Massimiliano Stagi, Laura E Swan

Open access · hybridAbstract read
In one paragraph

Article in Proteins, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.2field-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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The molecular mechanism of lipid uptake by membrane-anchored bridge-like lipid transfer proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. ATG2 is a triglyceride transfer protein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. An Autopsy Series of Seven Cases of VPS13A Disease (Chorea-Acanthocytosis).Movement disorders : official journal of the Movement Disorder Society · 2023
    Article
  14. Article
  15. Article
  16. Neuroacanthocytosis Syndromes: The Clinical Perspective.Contact (Thousand Oaks (Ventura County, Calif.))
    Review
  17. 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

3 authors at 1 institution in 1 country.

Filippo Dall'ArmellinaDepartment of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.ORCID 0000-0002-6790-6312
Massimiliano StagiDepartment of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.ORCID 0000-0002-5827-902X
Laura E SwanDepartment of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.ORCID 0000-0002-6312-6263
University of Liverpool · GB

Funding

Medical Research Council MR/N010035/1Wellcome TrustWellcome Trust 204822/Z/16/Z
6 · The paper itself

Abstract

The VPS13 protein family constitutes a novel class of bridge-like lipid transferases. Autosomal recessive inheritance of mutations in VPS13 genes is associated with the development of neurodegenerative diseases in humans. Bioinformatic approaches previously recognized the domain architecture of these proteins. In this study, we model the first ever full-length structures of the four human homologs VPS13A, VPS13B, VPS13C, and VPS13D in association with model membranes, to investigate their lipid transfer ability and potential structural association with membrane leaflets. We analyze the evolutionary conservation and physicochemical properties of these proteins, focusing on conserved C-terminal amphipathic helices that disturb organelle surfaces and that, adjoined, resemble a traditional Venetian gondola. The gondola domains share significant structural homology with lipid droplet surface-binding proteins. We introduce in silico protein-membrane models displaying the mode of association of VPS13A, VPS13B, VPS13C, and VPS13D to donor and target membranes, and present potential models of action for protein-mediated lipid transfer.

Indexed as

LipidsVesicular Transport ProteinsHumansMembranesMutationProteinsProtein Structure, SecondaryLipidsProteinsVesicular Transport ProteinsVPS13D protein, humaninterorganelle contactsjunctionslipid transfermembrane interactionperilipinprotein modelingVPS13

Identifiers

PMID36404287
PMCPMC10953354
OpenAlexW4309443626

What OpenQuestion holds

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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.