Cited by 908

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LRP: a multifunctional scavenger and signaling receptor

Herz, Joachim, Strickland, Dudley K.·2001·Journal of Clinical Investigation

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Crossref · 10.1172/jci200113992

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  • Multiple intracellular adaptor and scaffolding proteins bind the LRP 100 amino acid cytoplasmic tail.

    “Multiple intracellular adaptor and scaffolding proteins bind the LRP 100 amino acid cytoplasmic tail (16,17);”

    From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [16]

    The sections “Interactions with intracellular adapter and scaffold proteins” and “Structural organization of LRP” state that multiple cytoplasmic adaptor and scaffold proteins interact with the LRP tail. Our copy does not specify that the tail is 100 amino acids long, so that numerical detail is unsupported. (LLM, conf=0.85)

    Experimental — accuracy not yet measured
  • LRP1 belongs to the same family as LRP5 and is known to regulate crucial processes that help maintain synaptic integrity and cholesterol homeostasis in the brain.

    “LRP1 belongs to the same family as LRP5 and is known to regulate crucial processes that help maintain synaptic integrity and cholesterol homeostasis in the brain.[44][45][46]”

    From Canonical Wnt pathway and the LDL receptor superfamily in neuronal cholesterol homeostasis and function (2024) · cites this paper as [45]

    The Introduction places LRP in the LDL receptor gene family, and “Emerging functions in neurotransmission” describes its possible role in synaptic plasticity. But the paper does not identify LRP5 as a family member, and “Lipoprotein metabolism” presents LRP-mediated uptake of cholesterol in the brain as a possibility, not an established role in cholesterol homeostasis. (LLM, conf=0.88)

    Experimental — accuracy not yet measured
  • LRP's four extracellular binding domains mediate endocytosis of a wide array of ligands, including APP, apolipoprotein E and α2-macroglobulin.

    “its four extracellular binding domains mediate endocytosis of a wide array of ligands, including several of potential importance for Alzheimer disease pathophysiology: APP, apolipoprotein E and ␣ 2 -macroglobulin (16 -18).”
  • LRP functions in the catabolism of Aβ peptides.

    “LRP also functions in the catabolism of Aβ peptides”

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Metadata

Authors
Herz, J., & Strickland, D. K.
Venue
Journal of Clinical Investigation
Published
2001-09-15
Volume
108
Issue
6
Pages
779-784
ISSN
0021-9738
Cited by
908
References
0
Language
en

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