Cited by 4

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

PCSK9-promoted LDLR degradation: Recruitment or prevention of essential cofactors?

Li, Rong, Zhang, Cindy Xinyi, Liu, Junli, Zhang, Da-wei·2025·Metabolism Open

Overview

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Integrity signals

Registry

Crossref · 10.1016/j.metop.2025.100362

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

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Claims other papers make about this one

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  • PCSK9 prevents LDLR recycling and reduces ApoE uptake.

    “The activity of LDLR is tightly regulated by PCSK9, as it prevents its recycling to the surface and subsequently reduces ApoE uptake [31][32][33] .”

    From ApoE4 impairs astrocyte lipid droplet formation via endolysosomal dysfunction (2026) · cites this paper as [33]

    In the paper’s main text (page unavailable), PCSK9 is described as blocking LDLR recycling and reducing the number of LDL receptors at the cell surface for LDL clearance. The paper discusses LDL uptake, but it does not say that PCSK9 reduces ApoE uptake. (LLM, conf=0.88)

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Citations

Cites

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Research works printed but not linked: 4

  1. Zhang, 2007, Binding of proprotein convertase subtilisin/kexin type 9 to epidermal growth factor-like repeat A of low density lipoprotein receptor decreases receptor recycling and increases degradation, J Biol Chem, 282, 18602, 10.1074/jbc.M702027200 · DOI · Paper page
  2. Nguyen, 2014, Internalized PCSK9 dissociates from recycling LDL receptors in PCSK9-resistant SV-589 fibroblasts, J Lipid Res, 55, 266, 10.1194/jlr.M044156 · DOI
  3. Grefhorst, 2008, Plasma PCSK9 preferentially reduces liver LDL receptors in mice, J Lipid Res, 49, 1303, 10.1194/jlr.M800027-JLR200 · DOI · Paper page
  4. Wang, 2012, Molecular characterization of proprotein convertase subtilisin/kexin type 9-mediated degradation of the LDLR, J Lipid Res, 53, 1932, 10.1194/jlr.M028563 · DOI · Paper page

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Metadata

Authors
Li, R., Zhang, C. X., Liu, J., & Zhang, D.-W.
Venue
Metabolism Open
Publisher
Elsevier BV
Published
2025-06
Volume
26
Pages
100362
ISSN
2589-9368
Cited by
4
References
2
Language
en
Funders
Natural Sciences and Engineering Research Council of Canada (RGPIN-2024-06088)

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