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The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

The Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol

Barrett, Paul J., Song, Yuanli, Van Horn, Wade D., Hustedt, Eric J., Schafer, Johanna M., Hadziselimovic, Arina, Beel, Andrew J., Sanders, Charles R.·2012·Science
DOI 10.1126/science.1219988PMC PMC3528355
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Abstract

Insights into Amyloidogenesis: The amyloid-β (Aβ) peptides associated with Alzheimer's disease are generated by cleavage of the transmembrane C-terminal domain (C99) of the amyloid precursor protein by the enzyme γ-secretase. Barrett et al. (p. 1168 ) used nuclear magnetic resonance (NMR) and electron paramagnetic resonance spectroscopy to show that C99 contains surface-associated N- and C-terminal helices and a flexibly curved transmembrane helix that is well suited to processive cleavage by γ-secretase. Elevated cholesterol levels have been found to increase Aβ generation. NMR titration together with mutagenesis revealed a binding site for cholesterol within C99 that included a motif previously implicated in protein oligomerization.

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Crossref · 10.1126/science.1219988

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

  • The APP protein has a cholesterol binding site.

    “The conclusion is further supported by the existence of a cholesterol binding site in the APP protein (61).”

    From Regulation of beta-amyloid production in neurons by astrocyte-derived cholesterol (2021) · cites this paper as [61]

    The paper identifies a cholesterol-binding site in C99, a fragment of APP, and reports cholesterol binding by that fragment. It says full-length APP is *likely* to bind cholesterol with similar avidity; the unqualified claim about the full-length protein goes beyond what was directly shown. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

  • The effect of CE on Aβ is mediated by a domain in APP that has previously been shown to bind cholesterol.

    “We show that the effect of CE on Aβ is mediated by a domain in APP that has previously been shown to bind cholesterol (Barrett et al., 2012), possibly suggesting that this cholesterol-binding domain can also sense CE.”

    From Cholesterol Metabolism Is a Druggable Axis that Independently Regulates Tau and Amyloid-β in iPSC-Derived Alzheimer’s Disease Neurons (2019) · cites this paper as Barrett et al., 2012

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Citations

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Research works printed but not linked: 42

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Metadata

Authors
Barrett, P. J., Song, Y., Van Horn, W. D., Hustedt, E. J., Schafer, J. M., Hadziselimovic, A., Beel, A. J., & Sanders, C. R.
Affiliations
  • Department of Biochemistry, Center for Structural Biology and Institute of Chemical Biology, Vanderbilt University School of Medicine, Nashville, TN 37232 USA.
  • Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN 37232 USA.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2012-06
Volume
336
Issue
6085
Pages
1168-1171
ISSN
  • 0036-8075
  • 1095-9203
DOI
10.1126/science.1219988
PMC
PMC3528355
Cited by
467
References
1
Language
en

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