The DOI matches its Crossref record; 151 of the 151 references it cites were found in a registry or an index.
A Receptor-Mediated Pathway for Cholesterol Homeostasis
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In the citing paper
“LDLR is a receptor that binds to apolipoprotein B and apoE in the periphery to facilitate the uptake of cholesterol-laden lipoproteins by cells [38].”
From Measurement of apolipoprotein E and amyloid β clearance rates in the mouse brain using bolus stable isotope labeling (2012) · cites this paper as [38]
In the citing paper
“Ldlr is normally localized to the plasma membrane where it binds extracellular ApoE lipoproteins followed by endocytosis and subsequent release of bound lipids in the lysosome (62).”
From Regulation of astrocyte lipid metabolism and ApoE secretion by the microglial oxysterol, 25-hydroxycholesterol (2023) · cites this paper as [62]
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 Brown and Goldstein, 1986
In the citing paper
“LDL is catabolized by the liver via the LDL receptor (LDLR), which binds APOB and removes LDL from circulation and traffics it to the endosomal system for degradation (15).”
From Hepatic sortilin regulates both apolipoprotein B secretion and LDL catabolism (2012) · cites this paper as [15]
In the citing paper
“internalized LDL is released from LDLR in acidic compartments (29, 30)”
From The small GTPase RAB10 regulates endosomal recycling of the LDL receptor and transferrin receptor in hepatocytes (2022) · cites this paper as [30]
In the citing paper
“Cholesterol derived from low-density lipoprotein (LDL) is taken into cells through endocytosis mediated by LDL receptors (LDLRs) (1).”
From Last step in the path of LDL cholesterol from lysosome to plasma membrane to ER is governed by phosphatidylserine (2020) · cites this paper as [1]
In the citing paper
“LDL-derived cholesterol is taken up by LDLRs and released in lysosomes (1).”
From Last step in the path of LDL cholesterol from lysosome to plasma membrane to ER is governed by phosphatidylserine (2020) · cites this paper as [1]
In the citing paper
“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 [18]
In the citing paper
“Upon binding of plasma LDLs, cell surface LDLRs are internalized and transported to endosomes, where low pH causes LDLR-LDL dissociation1.”
From Phosphatidylinositol-(4,5)-Bisphosphate Regulates Plasma Cholesterol Through LDL (Low-Density Lipoprotein) Receptor Lysosomal Degradation (2020) · cites this paper as [1]
In the citing paper
“As a transmembrane glycoprotein, low-density lipoprotein receptor (LDLR) is abundantly expressed on the surface of hepatocytes, where it facilitates the uptake of LDL cholesterol and maintains the homeostasis of lipid metabolism20,21.”
From ABCC4 impairs the clearance of plasma LDL cholesterol through suppressing LDLR expression in the liver (2025) · cites this paper as [21]
In the citing paper
“Low expression level of low-density lipoprotein receptor (LDLR) in hepatocytes leads to hypercholesterolemia and eventually contributes to atherosclerotic cardiovascular disease (ASCVD).”
From ABCC4 impairs the clearance of plasma LDL cholesterol through suppressing LDLR expression in the liver (2025) · cites this paper as [21]
In the citing paper
“Complete absence or defective LDLRs due to mutations in the LDLR gene cause FH, characterized by an autosomal dominant inheritance of hypercholesterolemia and premature ASCVD (a list of mutations can be found in Table 1)1–4.”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [2]
In the citing paper
“where it is concentrated into clathrin-coated pits to internalize bound LDL by receptor-mediated endocytosis (discussed separately below)2”
From Pathways and Molecular Mechanisms Governing LDL Receptor Regulation (2025) · cites this paper as [2]
In the citing paper
“Low-density lipoprotein receptor (LDLR) is an integral membrane protein that is most abundantly expressed in the liver, where it binds to and removes LDL-C from the circulation by endocytosis4,5.”
From Triciribine increases LDLR expression and LDL uptake through stabilization of LDLR mRNA (2018) · cites this paper as [4]
In the citing paper
“Feedback suppression of SREBP2 pathway by LDLR plays a pivotal role in maintaining the balance of cholesterol levels between liver and blood (Brown and Goldstein, 1986).”
From GPR146 Deficiency Protects against Hypercholesterolemia and Atherosclerosis (2019) · cites this paper as Brown and Goldstein, 1986
In the citing paper
“hepatic cells also play major roles in removing LDL from the circulation”
From Endocytic adaptors Arh and Dab2 control homeostasis of circulatory cholesterol (2016) · cites this paper as [7]
In the citing paper
“The main carriers of atherogenic circulating cholesterol in humans are the LDL particles, which are produced mainly by the liver to deliver cholesterol to peripheral tissues”
From Endocytic adaptors Arh and Dab2 control homeostasis of circulatory cholesterol (2016) · cites this paper as [7]
In the citing paper
“The balance of serum cholesterol level is determined by dietary intake, synthesis, and catabolism”
From Endocytic adaptors Arh and Dab2 control homeostasis of circulatory cholesterol (2016) · cites this paper as [7]
In the citing paper
“LDL clearance from the circulation by LDL receptor (LDLR)-mediated endocytosis by hepatic and peripheral tissues and subsequent feedback regulation of endogenous synthesis of cholesterol is a key determinant of serum LDL level”
From Endocytic adaptors Arh and Dab2 control homeostasis of circulatory cholesterol (2016) · cites this paper as [7]
In the citing paper
“Excessive cholesterol in the circulation, upon uptake by the liver via LDL receptor (LDLR)-mediated endocytosis, suppresses endogenous synthesis of cholesterol in the liver”
From Endocytic adaptors Arh and Dab2 control homeostasis of circulatory cholesterol (2016) · cites this paper as [7]
In the citing paper
“The expression of liver LDL receptor (LDLR) regulates human plasma LDL-cholesterol (LDL-C) homeostasis”
From A novel posttranscriptional mechanism for dietary cholesterol-mediated suppression of liver LDL receptor expression (2014) · cites this paper as [2]
In the citing paper
“Following dissociation of the LDLR-LDL complex, LDL is directed to lysosomes whereas the LDLR recycles to the plasma membrane.”
From The LXR-IDOL axis defines a clathrin-, caveolae-, and dynamin-independent endocytic route for LDLR internalization and lysosomal degradation (2013) · cites this paper as [2]
In the citing paper
“Low density lipoprotein (LDL) cholesterol is taken up into cells via clathrin-mediated endocytosis of the LDL receptor (LDLR).”
From The LXR-IDOL axis defines a clathrin-, caveolae-, and dynamin-independent endocytic route for LDLR internalization and lysosomal degradation (2013) · cites this paper as [2]
In the citing paper
“LDL, which is derived by peripheral lipolysis of VLDL (very-low-density lipoprotein), is primarily cleared from the circulation in the liver via the LDLR (LDL receptor) pathway.1,2”
From (Pro)renin Receptor Inhibition Reprograms Hepatic Lipid Metabolism and Protects Mice From Diet-Induced Obesity and Hepatosteatosis (2018) · cites this paper as [1]
In the citing paper
“This results in induction of the full set of genes required for de novo biosynthesis of cholesterol via the mevalonate pathway and of the low-density lipoprotein receptor (LDLR) that is required for uptake of LDL-derived cholesterol (7,8).”
From A MARCH6 and IDOL E3 Ubiquitin Ligase Circuit Uncouples Cholesterol Synthesis from Lipoprotein Uptake in Hepatocytes (2016) · cites this paper as [8]
In the citing paper
“The LDLR structure from the N-terminus to the C-terminus includes seven ligand-binding domain repeats, an epidermal growth factor (EGF) precursor homology domain, an O-linked sugar domain, a transmembrane domain, and a cytoplasmic domain”
From ENO1–BACE2-mediated LDLR cleavage promotes liver cancer progression by remodelling cholesterol metabolism (2025) · cites this paper as Brown and Goldstein, 1986
In the citing paper
“Early studies on normal and FH fibroblasts demonstrated that LDLRs, shortly after being synthesized, appear on the cell surface where they gather in coated pits (1).”
In the citing paper
“The low density lipoprotein receptor (LDLR) 2 plays a pivotal role in the regulation of cholesterol metabolism (1).”
In the citing paper
“As noted in the Introduction, LDLR tends to cluster in clathrincoated pits on the cell surface under defined conditions.”
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Spady, D. K., Bilheimer, D. W., & Dietschy, J. M. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.11.3499 · Cited by 228
Regulation of Cholesterol Biosynthesis in Normal and Malignant Tissues
(1970) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152802-7.50009-8 · Cited by 227
Brown, M. D. (1976) · Cell · doi:10.1016/0092-8674(76)90130-6 · Cited by 222
Self-citationReceptor-mediated endocytosis: coated pits, receptosomes and the Golgi
Pastan, I. H., & Willingham, M. C. (1983) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(83)90351-1 · Cited by 222
Metabolic Studies in Familial Hypercholesterolemia
Bilheimer, D. W., Stone, N. J., & Grundy, S. M. (1979) · Journal of Clinical Investigation · doi:10.1172/jci109490 · Cited by 218
Neufeld, E. F., & Fratantoni, J. C. (1970) · Science · doi:10.1126/science.169.3941.141 · Cited by 215
The transport of lysosomal enzymes
Neufeld, E. F., Sando, G. N., Garvin, A. J., & Rome, L. H. (1977) · Journal of Supramolecular Structure · doi:10.1002/jss.400060108 · Cited by 211
Computer-based characterization of epidermal growth factor precursor
Doolittle, R. F., Feng, D. F., & Johnson, M. S. (1984) · Nature · doi:10.1038/307558a0 · Cited by 210
Basu, S., Goldstein, J. L., & Brown, M. S. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34768-3 · Cited by 210
Self-citationKita, T., Brown, M. S., Bilheimer, D. W., & Goldstein, J. L. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.18.5693 · Cited by 208
Self-citationSpady, D. K., Turley, S. D., & Dietschy, J. (1985) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)34361-3 · Cited by 206
Xanthomata, Hypercholesterolemia, Angina Pectoris.
Müller, C. (1938) · Acta Medica Scandinavica · doi:10.1111/j.0954-6820.1938.tb19279.x · Cited by 203
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Pittman, R. C., Carew, T. E., Attie, A., Witztum, J. L., Watanabe, Y., & Steinberg, D. H. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34287-x · Cited by 199
Reduction of Serum Cholesterol in Heterozygous Patients with Familial Hypercholesterolemia
Mabuchi, H., Sakai, T., Sakai, Y., Yoshimura, A., Watanabe, A., WAKASUGI, T., Koizumi, J., & Takeda, R. (1983) · New England Journal of Medicine · doi:10.1056/nejm198303173081101 · Cited by 198
Sherrill, B. C., & Dietschy, J. M. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62331-8 · Cited by 197
Luskey, K. L., Faust, J. R., Chin, D. J., Brown, M. S., & Goldstein, J. L. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)82087-0 · Cited by 195
Self-citationDavis, C. G., Elhammer, Å. P., Russell, D. W., Schneider, W. J., Kornfeld, S. A., Brown, M. S., & Goldstein, J. L. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35862-3 · Cited by 194
Self-citationAnderson, R. G., Goldstein, J. L., & Brown, M. S. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.7.2434 · Cited by 186
Self-citationTolleshaug, H., Goldstein, J. L., Schneider, W. J., & Brown, M. S. (1982) · Cell · doi:10.1016/0092-8674(82)90276-8 · Cited by 186
Self-citationCassette of Eight Exons Shared by Genes for LDL Receptor and EGF Precursor
Südhof, T. C., Russell, D. W., Goldstein, J. L., Brown, M. S., Sánchez-Pescador, R., & Bell, G. I. (1985) · Science · doi:10.1126/science.3873704 · Cited by 183
Self-citationReceptor-mediated low density lipoprotein catabolism in man.
Shepherd, J., Bicker, S., Lorimer, A. R., & Packard, C. J. (1979) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)40002-1 · Cited by 182
Innerarity, T. L., Weisgraber, K. H., Arnold, K. S., Rall, S. C., & Mahley, R. W. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39866-6 · Cited by 179
The genealogy of some recently evolved vertebrate proteins
Doolittle, R. F. (1985) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(85)90140-9 · Cited by 178
The sequence and topology of human complement component C9.
Stanley, K. K., Kocher, H. P., Luzio, J. P., Jackson, P., & Tschopp, J. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03639.x · Cited by 178
Kita, T., Goldstein, J. L., Brown, M. S., Watanabe, Y., Hornick, C. A., & Havel, R. J. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.11.3623 · Cited by 167
Self-citationCarpentier, J. L., Görden, P., Anderson, R. G. W., Goldstein, J. L., Brown, M. S., Cohen, S., & Orci, L. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.95.1.73 · Cited by 167
Self-citationcDNA cloning of the bovine low density lipoprotein receptor: feedback regulation of a receptor mRNA.
Russell, D. W., Yamamoto, T., Schneider, W. J., Slaughter, C. A., Brown, M. S., & Goldstein, J. L. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.24.7501 · Cited by 164
Self-citationThe distribution and composition of serum lipoproteins in eighteen animals
MILLS, G. L., & Taylaur, C. E. (1971) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/0305-0491(71)90234-3 · Cited by 163
Lehrman, M. A., Russell, D. W., Goldstein, J. L., & Brown, M. S. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.3679 · Cited by 161
Self-citationAssessment of long-term plasma exchange for familial hypercholesterolaemia.
Thompson, G. R., Myant, N. B., Kilpatrick, D., Oakley, C. M., Raphael, M. J., & Steiner, R. E. (1980) · Heart · doi:10.1136/hrt.43.6.680 · Cited by 155
NEONATAL DIAGNOSIS OF FAMILIAL TYPE-II HYPERLIPOPROTEINÆMIA
Kwiterovich, P., Levy, R., & Fredrickson, D. (1973) · The Lancet · doi:10.1016/s0140-6736(73)90194-3 · Cited by 154
Goldstein, J. L., Brown, M. S., & Stone, N. J. (1977) · Cell · doi:10.1016/0092-8674(77)90263-x · Cited by 151
Self-citationInteraction of swine lipoproteins with the low density lipoprotein receptor in human fibroblasts
Bersot, T. P., Mahley, R. W., Brown, M. S., & Goldstein, J. L. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33600-1 · Cited by 150
Self-citationRegulation of Cholesterol Metabolism
Dietschy, J. M., & Wilson, J. D. (1970) · New England Journal of Medicine · doi:10.1056/nejm197005282822206 · Cited by 148
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Bilheimer, D. W., Ho, Y. K., Brown, M. S., Anderson, R. G. W., & Goldstein, J. L. (1978) · Journal of Clinical Investigation · doi:10.1172/jci108980 · Cited by 142
Self-citationLowering Plasma Cholesterol by Raising LDL Receptors
Brown, M. S., & Goldstein, J. L. (1981) · New England Journal of Medicine · doi:10.1056/nejm198108273050909 · Cited by 142
Self-citationFrancke, U., Brown, M. S., & Goldstein, J. L. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.9.2826 · Cited by 137
Self-citationPatterson, D., & Slack, J. (1972) · The Lancet · doi:10.1016/s0140-6736(72)90853-7 · Cited by 133
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Self-citationMevinolin Plus Colestipol in Therapy for Severe Heterozygous Familial Hypercholesterolemia
Illingworth, D. R. (1984) · Annals of Internal Medicine · doi:10.7326/0003-4819-101-5-598 · Cited by 129
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Regulation of Cholesterol Biosynthesis
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Down-regulation of the low-density lipoprotein receptor by dietary cholesterol
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Recycling of Cell-surface Receptors: Observations from the LDL Receptor SystemPreprint
Brown, M. S., Anderson, R. G. W., Basu, S., & Goldstein, J. L. (1982) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1982.046.01.068 · Cited by 82
Self-citationSoutar, A. K., Myant, N. B., & Thompson, G. R. (1982) · Atherosclerosis · doi:10.1016/0021-9150(82)90024-7 · Cited by 79
Schneider, W. J., Slaughter, C. A., Goldstein, J. L., Anderson, R. G. W., Capra, J. D., & Brown, M. S. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.5.1635 · Cited by 76
Self-citationGenes and Chemical Reactions in Neurospora
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Functional segregation of hepatic receptors for asialoglycoproteins during endocytosis.
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A Case History in Biological Research
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Biologically active low density lipoprotein in human peripheral lymph.
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Sorted by citations
Regulation of the mevalonate pathway
Goldstein, J. L., & Brown, M. S. (1990) · Nature · doi:10.1038/343425a0 · Cited by 5,394
Self-citationApolipoprotein E: Cholesterol Transport Protein with Expanding Role in Cell Biology
Mahley, R. W. (1988) · Science · doi:10.1126/science.3283935 · Cited by 4,028
Brown, M. S., & Goldstein, J. L. (1997) · Cell · doi:10.1016/s0092-8674(00)80213-5 · Cited by 3,834
Self-citationGoodman, D. S. (1988) · Archives of Internal Medicine · doi:10.1001/archinte.1988.00380010040006 · Cited by 2,458
LDL Receptor-Related Protein 5 (LRP5) Affects Bone Accrual and Eye Development
Gong, Y., Slee, R. B., Fukai, N., Rawadi, G., Roman-Roman, S., Reginato, A. M., Wang, H., Cundy, T., Glorieux, F. H., Lev, D., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00571-2 · Cited by 2,235
Metadata
- Authors
- Brown, M. S., & Goldstein, J. L.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Venue
- Science
- Published
- 1986-04-04
- Volume
- 232
- Issue
- 4746
- Pages
- 34-47
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2084744450
- Semantic Scholar
- 272a968782c9511ffde67976c781969ead33e19e
- Cited by
- 5,703
- References
- 151
- Citations by year
- 2026: 64 · 2025: 78 · 2024: 61 · 2023: 105 · 2022: 107 · 2021: 125 · 2020: 118 · 2019: 108 · 2018: 131 · 2017: 140 · 2016: 130 · 2015: 145 · 2014: 139 · 2013: 134 · 2012: 139
- FWCI
- 30.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- cholesterol homeostasis, cholesterol metabolism, lipid transport
- MeSH terms
- Biological Transport, Cholesterol, Endocytosis, Homeostasis, Humans, Hyperlipoproteinemia Type II, Kinetics, Lipid Metabolism, Inborn Errors, Lipoproteins, HDL, Lipoproteins, LDL, Models, Biological, Mutation, Receptors, LDL
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