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The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Structures of dimeric human NPC1L1 provide insight into mechanisms for cholesterol absorption

Long, Tao, Liu, Yang, Qin, Yu, DeBose-Boyd, Russell A., Li, Xiaochun·2021·Science Advances
DOI 10.1126/sciadv.abh3997PMC PMC8373123
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Abstract

The cryo-EM structures of human NPC1L1 reveal a dimeric state mediating cholesterol and vitamin E uptake.

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Crossref · 10.1126/sciadv.abh3997

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  • Structural analyses have revealed that the N-terminal domain of NPC1L1 possesses a cavity that accommodates cholesterol.

    “Structural analyses have revealed that the N-terminal domain of NPC1L1 possesses a cavity that accommodates cholesterol (14–16).”

    From Aster-dependent nonvesicular transport facilitates dietary cholesterol uptake (2023) · cites this paper as [16]

    The Introduction says that a mutation in NPC1L1’s N-terminal domain abolishes cholesterol binding. But the Results (Structures of hNPC1L1 with distinct lipid cargoes) say the N-terminal domain was not built into the structural models; the observed cholesterol-binding pocket is in the intramolecular channel, not a demonstrated N-terminal cavity. The paper therefore supports N-terminal involvement in binding, but not the claimed structural observation of a cavity there. (LLM, conf=0.88)

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Metadata

Authors
Long, T., Liu, Y., Qin, Y., DeBose-Boyd, R. A., & Li, X.
Affiliations
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
ORCID
Venue
Science Advances
Publisher
American Association for the Advancement of Science (AAAS)
Published
2021-08-20
Volume
7
Issue
34
ISSN
2375-2548
DOI
10.1126/sciadv.abh3997
PMC
PMC8373123
Cited by
36
References
2
Language
en
Licence
creativecommons.org/licenses/by-nc/4.0/ (vor)
Funders
National Institutes of Health (P01 HL020948, R01 GM134700, R01 GM135343)

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