Cited by 40

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Selective Aster inhibitors distinguish vesicular and nonvesicular sterol transport mechanisms

Xiao, Xu, Kim, Youngjae, Romartinez-Alonso, Beatriz, Sirvydis, Kristupas, Ory, Daniel S., Schwabe, John W. R., Jung, Michael E., Tontonoz, Peter·2021·Proceedings of the National Academy of Sciences

Abstract

Significance: The Aster proteins are transporters that move cholesterol between the plasma membrane and the ER. Here, we develop and characterize small molecules that selectively inhibit one or more Aster proteins. Importantly, we identify compounds that block Aster-mediated cholesterol transport without interfering with other sterol regulatory proteins, including NPC1 and SREBP2. Cell studies reveal that inhibition of Aster function by small molecules blocks the movement of LDL-derived cholesterol from the plasma membrane to the ER, thus positioning the nonvesicular Aster pathway downstream of the NPC1 vesicular pathway in the movement of LDL-derived cholesterol.

Overview

Integrity signals

Registry

Crossref · 10.1073/pnas.2024149118

Cites

5 of 5 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • AI-3d potently inhibits Aster-A, -B, and -C.

    “Previous work from our laboratory identified a small molecule, AI-3d, that potently inhibits Aster-A, -B, and -C (36).”
  • AI-3d reduced cholesterol transport to the ER and expanded the pool of accessible cholesterol at PM of intestinal enteroids.

    “The inhibitor AI-3d, which had been shown previously (36) to inhibit Aster-mediated non-vesicular transport in vitro, reduced cholesterol transport to the ER and expanded the pool of accessible cholesterol at PM of intestinal enteroids.”
  • One limitation is that the AI-3d inhibitor targets all Aster proteins, including GRAMD1B, GRAMD1A, and GRAMD1C.

    “However, one limitation is that the AI-3d inhibitor targets all Aster proteins, including GRAMD1B, GRAMD1A, and GRAMD1C85.”

Citations

Cites

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Research works printed but not linked: 32

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Metadata

Authors
Xiao, X., Kim, Y., Romartinez-Alonso, B., Sirvydis, K., Ory, D. S., Schwabe, J. W. R., Jung, M. E., & Tontonoz, P.
Affiliations
  • Department of Pathology and Laboratory Medicine, University of California, Los Angeles, CA 90095;
  • Department of Chemistry, University of California, Los Angeles, CA 90095;
  • Institute of Structural and Chemical Biology, Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, United Kingdom;
  • Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110
Venue
Proceedings of the National Academy of Sciences
Published
2020-12-29
Volume
118
Issue
2
ISSN
  • 0027-8424
  • 1091-6490
Cited by
40
References
5
Language
en
Funders
  • HHS | NIH | National Heart, Lung, and Blood Institute (146358)
  • Fondation Leducq (19CVD04)

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

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