The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Low-Density Lipoprotein Receptor Family
Abstract
The low-density lipoprotein receptor (LDLR) family is composed of a class of single transmembrane glycoproteins, generally recognized as cell surface endocytic receptors, which bind and internalize extracellular ligands for degradation by lysosomes. Structurally, members of the LDLR family share homology within their extracellular domains, which are highlighted by the presence of clusters of ligand-binding repeats. Recently, information regarding the structural and functional elements within their cytoplasmic tails has begun to emerge, which suggests that members of the LDLR family function not only in receptor-mediated endocytosis, but also in transducing signals that are important during embryonic development and the pathogenesis of Alzheimer's disease. This review focuses on recent knowledge of the structural and functional aspects of LDLR family members in endocytosis and signal transduction. The relationship of these functions to the development of the neuronal system and in the pathogenesis of Alzheimer's disease is specifically discussed.
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LDLR is a major determinant of circulating levels of LDL.
“A number of scholars reported that LDLR is a major determinant of circulating levels of LDL.[16][17][18]”
From USP16 Regulates the Stability and Function of LDL receptor by Deubiquitination (2020) · cites this paper as [17]
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).”
From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [17]
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 [17]
Citations
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A protein related to extracellular matrix proteins deleted in the mouse mutant reeler
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“Reelin, the product of the reeler gene (40), is synthesized and secreted in the cerebral cortex, predominantly by the Cajal-Retzius cell of the marginal zone, the outermost layer of the developing cortex (40,41).”
BackgroundReelin Is a Ligand for Lipoprotein Receptors
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“Subsequently, Reelin was demonstrated to be a ligand for both VLDLR and apoER2 (47,48).”
BackgroundScrambler and yotari disrupt the disabled gene and produce a reeler -like phenotype in mice
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Proteins of the CNR Family Are Multiple Receptors for Reelin
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The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and -2
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“The interaction with JIPs is specific for apoER2, since neither the LDLR nor the VLDLR bind to these adaptor proteins (34).”
BackgroundEvidence for a second alpha 2-macroglobulin receptor.
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Zhuang, L., Kim, J., Adam, R. M., Solomon, K. R., & Freeman, M. R. (2005) · Journal of Clinical Investigation · doi:10.1172/jci200519935 · Cited by 567
The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate
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Fuentealba, R. A., Liu, Q., Zhang, J., Kanekiyo, T., Hu, X., Lee, J.-M., LaDu, M. J., & Bu, G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011884 · Cited by 116
Self-citationFunctional Roles of the Interaction of APP and Lipoprotein Receptors
Pohlkamp, T., Wasser, C. R., & Herz, J. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00054 · Cited by 92
Cholesterol uptake in adrenal and gonadal tissues: the SR-BI and “selective” pathway connection
Azhar, S. (2003) · Frontiers in bioscience · doi:10.2741/1165 · Cited by 109
Cenarro, A., Etxebarria, A., de Castro-Orós, I., Stef, M., Bea, A. M., Palacios, L., Mateo-Gallego, R., Benito-Vicente, A., Ostolaza, H., Tejedor, T., et al. (2016) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2015-3874 · Cited by 100
Wnt/β-Catenin Signaling in Alzheimer’s Disease
Ferrari, G., Avila, M., Medina, M., Perez-Palma, E., Bustos, B., & Alarcon, M. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527312666131223113900 · Cited by 95
The generation and function of soluble apoE receptors in the CNS
Rebeck, G. W., LaDu, M. J., Estus, S., Bu, G., & Weeber, E. J. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-15 · Cited by 66
Self-citationUSP16 Regulates the Stability and Function of LDL receptor by Deubiquitination
Li, Y., Rao, Y., Zhu, H., Jiang, B., & Zhu, M. (2020) · International Heart Journal · doi:10.1536/ihj.20-043 · Cited by 8
Self-citation
Metadata
- Authors
- Bu, G., Li, Y., & Cam, J.
- Venue
- Molecular Neurobiology
- Published
- 2001
- Volume
- 23
- Issue
- 1
- Pages
- 53-68
- ISSN
- 0893-7648
- Cited by
- 137
- References
- 17
- Language
- en
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