The DOI matches its Crossref record; 202 of the 202 references it cites were found in a registry or an index.
Lipoprotein Receptors in the Nervous System
Abstract
The low-density-lipoprotein (LDL) receptor family is an evolutionarily ancient gene family of structurally closely related cell-surface receptors. Members of the family are involved in the cellular uptake of extracellular ligands and regulate diverse biological processes including lipid and vitamin metabolism and cell-surface protease activity. Some members of the family also participate in cellular signaling and regulate the development and functional maintenance of the nervous system. Here we review the roles of this family of multifunctional receptors in the nervous system and focus on recent advances toward the understanding of the mechanisms by which lipoprotein receptors and their ligands transmit and modulate signals in the brain.
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In the citing paper
“ApoE binds to a group of structurally related proteins known as the low density lipoprotein receptor (LDLR) family.”
From Overexpression of Low-Density Lipoprotein Receptor in the Brain Markedly Inhibits Amyloid Deposition and Increases Extracellular Aβ Clearance (2009) · cites this paper as Herz and Bock, 2002
In the citing paper
“Among the LDLR family of proteins, the VLDLR (very low density lipoprotein receptor) and ApoER2 (also known as LRP8) share the highest overall sequence homology with the LDLR (14).”
From The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2 (2010) · cites this paper as [14]
In the citing paper
“Our investigation of the substrate specificity of IDOL was largely prompted by the high degree of evolutionary conservation within the LDLR family of receptors (14).”
From The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2 (2010) · cites this paper as [14]
In the citing paper
“ApoE receptors are members of the low-density lipoprotein receptor gene family that play important roles in maintaining the proper function of neurons (Herz and Bock, 2002).”
From The E3 ubiquitin ligase IDOL regulates synaptic ApoER2 levels and is important for plasticity and learning (2017) · cites this paper as Herz and Bock, 2002
In the citing paper
“The ligands for LRP1 include several proteins already implicated in AD pathogenesis, such as apoE, APP, Aβ, α2-macroglobulin, matrix metallopeptidase 9, and tissue-type plasminogen activator (Herz and Bock, 2002).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Herz and Bock, 2002
In the citing paper
“LRP1 functions as an endocytic and signaling receptor with a wide expression pattern in a variety of tissues.”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Herz and Bock, 2002
In the citing paper
“LDLR is a cell surface glycoprotein that plays an important role in mediating the removal of cholesterol and cholesteryl ester-containing low-density lipoprotein (LDL) particles from the circulation (Brown and Goldstein, 1986; Herz and Bock, 2002).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Herz and Bock, 2002
In the citing paper
“The LDL receptor-related protein (LRP) is a multiligand endocytic receptor that belongs to the LDL receptor family (Herz and Bock, 2002).”
From Sorting nexin 17 facilitates LRP recycling in the early endosome (2005) · cites this paper as Herz and Bock, 2002
In the citing paper
“The low-density lipoprotein receptor (LDLR)-related protein 1 (LRP1) is a transmembrane receptor that belongs to the LDLR family [20].”
From LRP1 is a neuronal receptor for α-synuclein uptake and spread (2022) · cites this paper as [20]
Citations
Cites
Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429
Neurogenesis in the adult human hippocampus
Eriksson, P. S., Perfilieva, E., Björk-Eriksson, T., Alborn, A.-M., Nordborg, C., Peterson, D. A., & Gage, F. H. (1998) · Nature Medicine · doi:10.1038/3305 · Cited by 6,369
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
The Genome Sequence of Drosophila melanogaster
Adams, M. D., Celniker, S., Holt, R. A., Evans, C. A., Gocayne, J. D., Amanatides, P. G., Scherer, S. E., Li, P. W., Hoskins, R. A., Galle, R. F., et al. (2000) · Science · doi:10.1126/science.287.5461.2185 · Cited by 5,902
A Receptor-Mediated Pathway for Cholesterol Homeostasis
Brown, M. S., & Goldstein, J. L. (1986) · Science · doi:10.1126/science.3513311 · Cited by 5,703
Polakis, P. (2000) · Genes & Development · doi:10.1101/gad.14.15.1837 · Cited by 3,183
Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
Anderson, R. G. W. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.199 · Cited by 1,941
Statins and the risk of dementia
Jick, H., Zornberg, G. L., Jick, S. S., Seshadri, S. S., & Drachman, D. (2000) · The Lancet · doi:10.1016/s0140-6736(00)03155-x · Cited by 1,764
A protein related to extracellular matrix proteins deleted in the mouse mutant reeler
D'Arcangelo, G., G. Miao, G., Chen, S.-C., Scares, H. D., Morgan, J. I., & Curran, T. (1995) · Nature · doi:10.1038/374719a0 · Cited by 1,748
Research works printed but not linked: 12
- Goldstein JL, Hobbs HH, Brown MS. 2001.Familial Hypercholesterolemiaed. CR Scriver, AL Beaudet, WS Sly, D Valle, B Childs, et al. pp. 2863–913. New York: McGraw-Hill
- 10.1172/JCI200113992 · DOI · Paper page
- 10.1146/annurev.bi.63.070194.003125 · DOI
- Liu CX, 2000, Cancer Res., 60, 1961
- Bachinsky DR, 1993, Am. J. Pathol., 143, 598
- Abbate M, 1993, Eur. J. Cell Biol., 61, 139
- Boyles JK, 1986, Circulation, 74, II
- Wolf BB, 1992, Am. J. Pathol., 141, 37
- Mahley RW, Rall SC. 1995.Type III Hyperlipoproteinemia (Dysbetalipoproteinemia): The Role of Apolipoprotein E in Normal and Abnormal Lipoprotein Metabolismed. CR Scriver, AL Beaudet, WS Sly, D Valle, pp. 1953–80. New York: McGraw-Hill
- 10.1074/jbc.270.16.9543 · DOI
- 10.1034/j.1600-0854.2001.020206.x · DOI · Paper page
- 10.1042/0264-6021:3470613 · DOI
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Metadata
- Authors
- Herz, J., & Bock, H. H.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2002-06
- Volume
- 71
- Issue
- 1
- Pages
- 405-434
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2149816215
- Cited by
- 457
- References
- 202
- Citations by year
- 2026: 6 · 2025: 12 · 2024: 14 · 2023: 18 · 2022: 19 · 2021: 11 · 2020: 16 · 2019: 13 · 2018: 10 · 2017: 8 · 2016: 11 · 2015: 8 · 2014: 21 · 2013: 12 · 2012: 20
- FWCI
- 6.54
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (R37HL063762)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- low-density lipoprotein receptor family, lipoprotein receptors, nervous system, brain, receptor signaling, lipid metabolism, vitamin metabolism, proteolytic activity, cell surface receptors, brain development, neuroprotection
- MeSH terms
- Reelin Protein, Animals, Apolipoproteins E, Brain, Central Nervous System, Cholesterol, Multigene Family, Learning, Ligands, Nerve Tissue Proteins, Proto-Oncogene Proteins, Receptors, LDL, Serine Endopeptidases, Signal Transduction, Trans-Activators, Cell Adhesion Molecules, Neuronal, Receptors, N-Methyl-D-Aspartate, Extracellular Matrix Proteins, Protein Transport, Caveolae, Membrane Microdomains, Zebrafish Proteins, Wnt Proteins, Hedgehog Proteins
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