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.”
Citations
Cites
The Metabolic Basis of Inherited Disease.
(1988) · Annals of Internal Medicine · doi:10.7326/0003-4819-108-3-503_7 · Cited by 7,807
Sickle Cell Anemia, a Molecular Disease
Pauling, L., Itano, H. A., Singer, S. J., & Wells, I. C. (1949) · Science · doi:10.1126/science.110.2865.543 · Cited by 2,319
Gilbert, W. (1978) · Nature · doi:10.1038/271501a0 · Cited by 2,300
Serum cholesterol, lipoproteins, and the risk of coronary heart disease. The Framingham study.
Kannel, W., Castelli, W., Gordon, T., & McNamara, P. M. (2020) · Annals of Internal Medicine · doi:10.7326/0003-4819-74-1-1 · Cited by 2,160
Carbohydrate-Specific Receptors of the Liver
Ashwell, G., & Harford, J. (1982) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.51.070182.002531 · Cited by 1,914
The Low-Density Lipoprotein Pathway and its Relation to Atherosclerosis
Goldstein, L. J., & Brown, S. M. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.004341 · Cited by 1,906
De Duve, C., De Barsy, T., Poole, B., Trouet, A., Tulkens, P., & Van Hoof, F. (1974) · Biochemical Pharmacology · doi:10.1016/0006-2952(74)90174-9 · Cited by 1,901
Bilheimer, D. W., Eisenberg, S., & Levy, R. I. (1972) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(72)90034-3 · Cited by 1,815
Alberts, A. W., Chen, J., Kuron, G. W., Hunt, V. M., Huff, J. W., Hoffman, C., Rothrock, J. W., López, M., Joshua, H., Harris, E., et al. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.7.3957 · Cited by 1,630
Flagged first, then by citations
Research works printed but not linked: 13
- BAILEY, J.M., CIBA FOUNDATION SYMPOSIUM 12: 63 (1973).
- BROWN, M.S., RECENT PROGRESS IN HORMONE RESEARCH 35: 215 (1979).
- Calvert, G. D. F., Low Density Liproteins: 281 (1976).
- FREDRICKSON, D.S., HARVEY LECTURE SERIES 68: 185 (1974).
- Fredrickson, D. S., The Metabolic Basis of Inherited Disease: 545 (1972).
- GOFMAN, J.W., PLASMA 2: 413 (1954).
- GOLDSTEIN, J.L., LIPOPROTEIN RECEPTORS - GENETIC DEFENSE AGAINST ATHEROSCLEROSIS, CLINICAL RESEARCH 30: 417 (1982).
- KOVANEN, P.T., INCREASED BINDING OF LOW-DENSITY LIPOPROTEIN TO LIVER MEMBRANES FROM RATS TREATED WITH 17-ALPHA-ETHYNYL ESTRADIOL, JOURNAL OF BIOLOGICAL CHEMISTRY 254: 1367 (1979).
- Lehrman, M. A., Proceedings of the National Academy of Sciences of the United States of America 83: 3679 (1986).
- MULLER, C, ACTA MEDICA SCANDINAVICA 89: 75 (1938).
- ONCLEY, J.L., HARVEY LECTURES 50: 71 (1956).
- PALADE, G. E., JOURNAL OF APPLIED PHYSICS 24: 1424 (1953).
- SCHNEIDER, W.J., MOL BIOL MED 1: 353 (1983).
Cited by
Sorted by citations
Items 501–600 of 1,059
1H NMR spectroscopy of human blood plasma
Ala‐Korpela, M. (1995) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/0079-6565(95)01013-0 · Cited by 168
Simons, M., Krämer, E.-M., Macchi, P., Rathke-Hartlieb, S., Trotter, J., Nave, K.-A., & Schulz, J. B. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200110138 · Cited by 168
Regulation of Monocyte CD36 and Thrombospondin-1 Expression by Soluble Mediators
Yesner, L. M., Huh, H., Pearce, S. F. A., & Silverstein, R. L. (1996) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.16.8.1019 · Cited by 167
Membrane Receptors for Endocytosis in the Renal Proximal Tubule
Christensen, E. L., Birn, H., Verroust, P. J., & Moestrup, S. K. (1998) · International review of cytology · doi:10.1016/s0074-7696(08)61772-6 · Cited by 165
Roles of AP-2 in Clathrin-Mediated Endocytosis
Boucrot, E., Saffarian, S., Zhang, R., & Kirchhausen, T. L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010597 · Cited by 173
Tybjærg‐Hansen, A., Gallagher, J. J., Vincent, J., Houlston, R. S., Talmud, P. J., Dunning, A. M., Seed, M., Hamsten, A., Humphries, S. E., & Myant, N. B. (1990) · Atherosclerosis · doi:10.1016/0021-9150(90)90031-d · Cited by 166
Pal, S., Ho, N., Santos, C., Dubois, P., Mamo, J. C. L., Allister, E. M., & Croft, K. D. (2003) · Journal of Nutrition · doi:10.1093/jn/133.3.700 · Cited by 165
Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase
Jo, Y., & DeBose‐Boyd, R. A. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.485605 · Cited by 170
Regulation of hepatic LDL receptors by mTORC1 and PCSK9 in mice
Ai, D., Chen, C., Han, S., Ganda, A., Murphy, A. J., Haeusler, R. A., Thorp, E. B., Accili, D., Horton, J. D., & Tall, A. R. (2012) · Journal of Clinical Investigation · doi:10.1172/jci61919 · Cited by 169
Dyslipoproteinemia in pediatric systemic lupus erythematosus
Ilowite, N. T., Samuel, P., Ginzler, E. M., & Jacobson, M. S. (1988) · Arthritis & Rheumatism · doi:10.1002/art.1780310706 · Cited by 165
Influence of age on the metabolism of plasma low density lipoproteins in healthy males.
Ericsson, S., Eriksson, M., Vitols, S., Einarsson, K., Berglund, L., & Angelin, B. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115034 · Cited by 165
Prattes, S., Hörl, G., Hammer, A., Blaschitz, A., Graier, W. F., Sattler, W., Zechner, R., & Steyrer, E. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.17.2977 · Cited by 165
Human cholesterol metabolism and therapeutic molecules
Charlton-Menys, V., & Durrington, P. N. (2007) · Experimental Physiology · doi:10.1113/expphysiol.2007.035147 · Cited by 167
Asparaginase-Associated Lipid Abnormalities in Children With Acute Lymphoblastic Leukemia
Parsons, S. K., Skapek, S. X., Neufeld, E. J., Kuhlman, C., Young, M. L., Donnelly, M., Brunzell, J. D., Otvos, J. D., Sallan, S. E., & Rifai, N. (1997) · Blood · doi:10.1182/blood.v89.6.1886 · Cited by 164
Gleason, M. M., Medow, M. S., & Tulenko, T. N. (1991) · Circulation Research · doi:10.1161/01.res.69.1.216 · Cited by 164
The low-density lipoprotein receptor gene family: multiple roles in lipid metabolism
Willnow, T. E. (1999) · Journal of Molecular Medicine · doi:10.1007/s001090050356 · Cited by 165
Lellek, H., Kirsten, R., Diehl, I., Apostel, F., Buck, F., & Greeve, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001786200 · Cited by 150
LaFerla, F. M., Troncoso, J. C., Strickland, D. K., Kawas, C. H., & Jay, G. D. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119536 · Cited by 165
Clinical Pharmacokinetics of Fluvastatin
Scripture, C. D., & Pieper, J. A. (2001) · Clinical Pharmacokinetics · doi:10.2165/00003088-200140040-00003 · Cited by 165
Arca, M., Zuliani, G., Wilund, K., Campagna, F., Fellin, R., Bertolini, S., Calandra, S., Ricci, G., Glorioso, N., Maioli, M., et al. (2002) · The Lancet · doi:10.1016/s0140-6736(02)07955-2 · Cited by 136
Bolotina, V. M., Omelyanenko, V. G., Heyes, B., Ryan, U. S., & Bregestovski, P. D. (1989) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/bf00370875 · Cited by 163
Deep-etch visualization of proteins involved in clathrin assembly.
Heuser, J. E., & Keen, J. H. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.3.877 · Cited by 163
Connelly, M. A., & Williams, D. L. (2004) · Current Opinion in Lipidology · doi:10.1097/00041433-200406000-00008 · Cited by 162
Coordinated Nonvectorial Folding in a Newly Synthesized Multidomain Protein
Jansens, A., van Duijn, E., & Braakman, I. (2002) · Science · doi:10.1126/science.1078376 · Cited by 162
Gene targeting approaches to complex genetic diseases: atherosclerosis and essential hypertension.
Smithies, O., & Maeda, N. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5266 · Cited by 162
Willnow, T. E., & Herz, J. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.3.719 · Cited by 162
Host but Not Parasite Cholesterol Controls Toxoplasma Cell Entry by Modulating Organelle Discharge
Coppens, I., & Joiner, K. A. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0830 · Cited by 161
Emerging roles of the intestine in control of cholesterol metabolism
Kruit, J. K. (2006) · World Journal of Gastroenterology · doi:10.3748/wjg.v12.i40.6429 · Cited by 165
Cyclosporine, Low-Density Lipoprotein, and Cholesterol
de Groen, P. C. (1988) · Mayo Clinic Proceedings · doi:10.1016/s0025-6196(12)64916-7 · Cited by 160
Chinese green tea lowers cholesterol level through an increase in fecal lipid excretion
Yang, T. T. C., & Koo, M. W. L. (1999) · Life Sciences · doi:10.1016/s0024-3205(99)00607-4 · Cited by 161
Wang, H. H., Liu, M., Clegg, D. J., Portincasa, P., & Wang, D. Q. ‐. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.06.006 · Cited by 160
Effect of Lycopene and Tomato Products on Cholesterol Metabolism
Palozza, P., Catalano, A., Simone, R. E., Mele, M. C., & Cittadini, A. R. M. (2012) · Annals of Nutrition and Metabolism · doi:10.1159/000342077 · Cited by 161
Contribution of monocyte-derived macrophages and smooth muscle cells to arterial foam cell formation
Allahverdian, S., Pannu, P. S., & Francis, G. A. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs094 · Cited by 166
Infante, R. E., & Radhakrishnan, A. (2017) · eLife · doi:10.7554/elife.25466 · Cited by 163
Underwood, K. W., Jacobs, N. L., Howley, A., & Liscum, L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.7.4266 · Cited by 159
Cholesterol in islet dysfunction and type 2 diabetes
Brunham, L. R., Kruit, J. K., Verchere, C. B., & Hayden, M. R. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33296 · Cited by 158
Role of Cholesterol and Lipid Rafts in Cancer Signaling: A Promising Therapeutic Opportunity?
Vona, R., Iessi, E., & Matarrese, P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.622908 · Cited by 169
Bile acid sequestrants: Mechanisms of action on bile acid and cholesterol metabolism
Einarsson, K., Ericsson, S., Ewerth, S., Reihnér, E., Rudling, M. J., Ståhlberg, D., & Angelin, B. (1991) · European Journal of Clinical Pharmacology · doi:10.1007/bf03216291 · Cited by 158
Konikoff, F. M., Chung, D. S., Donovan, J., SMALL, D. M., & Carey, M. C. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115935 · Cited by 158
Potential role of the low-density lipoprotein receptor family as mediators of cellular drug uptake
Chung, N., & Wasan, K. M. (2004) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2003.12.003 · Cited by 165
Auwerx, J. H., Schoonjans, K., Fruchart, J., & Staels, B. (1996) · Atherosclerosis · doi:10.1016/0021-9150(96)05854-6 · Cited by 158
SREBP transcriptional activity is mediated through an interaction with the CREB-binding protein.Preprint
Oliner, J., Andresen, J. M., Hansen, S. K., Zhou, S., & Tjian, R. (1996) · Genes & Development · doi:10.1101/gad.10.22.2903 · Cited by 159
TMEM41B acts as an ER scramblase required for lipoprotein biogenesis and lipid homeostasis
Huang, D., Xu, B., Liu, L., Wu, L., Zhu, Y., Ghanbarpour, A., Wang, Y., Chen, F., Lyu, J., Hu, Y., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.05.006 · Cited by 157
Ilnytska, O., Santiana, M., Hsu, N.-Y., Du, W., Chen, Y.-H., Viktorova, E. G., Belov, G. A., Brinker, A., Storch, J., Moore, C., et al. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.08.002 · Cited by 156
Power of deep, all-exon resequencing for discovery of human trait genes
Kryukov, G. V., Shpunt, A., Stamatoyannopoulos, J. A., & Sunyaev, S. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812824106 · Cited by 157
Structure of human Niemann–Pick C1 protein
Li, X., Wang, J., Coutavas, E. E., Shi, H., Hao, Q., & Blobel, G. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1607795113 · Cited by 162
Germi, R., Crance, J., Garín, D., Guimet, J., Lortat‐Jacob, H., Ruigrok, R. W. H., Zarski, J., & Drouet, E. (2002) · Journal of Medical Virology · doi:10.1002/jmv.10196 · Cited by 155
Liu, C.-X., Li, Y., Obermoeller, L. M., Schwartz, A. L., & Bu, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102727200 · Cited by 155
The genetics and screening of familial hypercholesterolaemia
Henderson, R., O’Kane, M., McGilligan, V., & Watterson, S. (2016) · Journal of Biomedical Science · doi:10.1186/s12929-016-0256-1 · Cited by 166
Targeting PCSK9 to tackle cardiovascular disease
Hummelgaard, S., Vilstrup, J. P., Gustafsen, C., Glerup, S., & Weyer, K. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108480 · Cited by 150
Qureshi, A., Qureshi, N., Hasler-Rapacz, J., Weber, F., Chaudhary, V., Crenshaw, T. D., GAPOR, A., Ong, A. S. H., Chong, Y. H., Peterson, D. M., et al. (1991) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/53.4.1042s · Cited by 152
Hiltunen, T. P., Luoma, J. S., Nikkari, T., & Ylä‐Herttuala, S. (1998) · Circulation · doi:10.1161/01.cir.97.11.1079 · Cited by 155
Effects of polyphenolic natural products on the lipid profiles of rats fed high fat diets
Yugarani, T., Tan, B. K. H., Teh, M., & Das, N. P. (1992) · Lipids · doi:10.1007/bf02536175 · Cited by 155
Cardiovascular disease and nutrient antioxidants: Role of low‐density lipoprotein oxidation
Frei, B. B. (1995) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408399509527689 · Cited by 157
Modulation of Luteal Activity in Postpartum Beef Cows through Changes in Dietary Lipid
Williams, G. L. (1989) · Journal of Animal Science · doi:10.2527/jas1989.673785x · Cited by 155
Castellano, J. M., Deane, R., Gottesdiener, A. J., Verghese, P. B., Stewart, F. R., West, T., Paoletti, A. C., Kasper, T. R., DeMattos, R. B., Zlokovic, B. V., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206446109 · Cited by 154
Oil-in-water lipid emulsions: implications for parenteral and ocular delivering systems
Tamilvanan, S. (2004) · Progress in Lipid Research · doi:10.1016/j.plipres.2004.09.001 · Cited by 156
Membrane trafficking in health and disease
Yarwood, R., Hellicar, J., Woodman, P. G., & Lowe, M. (2020) · Disease Models & Mechanisms · doi:10.1242/dmm.043448 · Cited by 161
Shimomura, I., Bashmakov, Y., Shimano, H., Horton, J. D., Goldstein, J. L., & Brown, M. S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12354 · Cited by 132
Self-citationGoulbourne, C. N., Gin, P., Tatar, A., Nobumori, C., Hoenger, A., Jiang, H., Grovenor, C. R. M., Adeyo, O., Esko, J. D., Goldberg, I. J., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.01.017 · Cited by 149
Deffieu, M. S., & Pfeffer, S. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110439108 · Cited by 165
Zhao, K., & Ridgway, N. D. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.028 · Cited by 155
Influence of cholesterol on cancer progression and therapy
Mayengbam, S. S., Singh, A., Pillai, A. D., & Bhat, M. K. (2021) · Translational Oncology · doi:10.1016/j.tranon.2021.101043 · Cited by 155
Carleton, R. A., Dwyer, J. T., Finberg, L., Flora, J. D., Goodman, D. S., Grundy, S. M., Havas, S., Hunter, G., Kritchevsky, D., & Lauer, R. M. (1991) · Circulation · doi:10.1161/01.cir.83.6.2154 · Cited by 155
Argraves, K. M., Battey, F. D., MacCalman, C. D., McCrae, K. R., Gåfvels, M. E., Kozarsky, K., Chappell, D. A., Strauss, J. F., & Strickland, D. K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.44.26550 · Cited by 153
Universal Screening for Familial Hypercholesterolemia in Children
Klančar, G., Grošelj, U., Kovač, J., Bratanič, N., Bratina, N., Podkrajšek, K. T., & Battelino, T. (2015) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2015.07.017 · Cited by 152
Nammi, S., Satyanarayana, S., & Roufogalis, B. D. (2009) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/j.1742-7843.2008.00362.x · Cited by 152
Premature Atherosclerosis Associated With Monogenic Insulin Resistance
Hegele, R. A. (2001) · Circulation · doi:10.1161/01.cir.103.18.2225 · Cited by 151
Kadowaki, T., Kadowaki, H., & Taylor, S. I. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.2.658 · Cited by 149
microRNAs and cholesterol metabolism
Moore, K. J., Rayner, K. J., Suárez, Y., & Fernandez-Hernando, C. F. (2010) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2010.08.008 · Cited by 149
Brodsky, J. L. (2007) · Biochemical Journal · doi:10.1042/bj20061890 · Cited by 149
Accili, D., Frapier, C., Mosthaf, L., McKeon, C., Elbein, S. C., Permutt, M. A., Ramos, E., Lander, E. S., Ullrich, A., & Taylor, S. I. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08388.x · Cited by 150
Cellular cholesterol homeostasis and Alzheimer’s disease
Chang, T.-Y., Yamauchi, Y., Hasan, M. T., & Chang, C. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075630 · Cited by 155
Simvastatin enhances learning and memory independent of amyloid load in mice
Li, L., Cao, D., Kim, H., Lester, R. A. J., & Fukuchi, K. (2006) · Annals of Neurology · doi:10.1002/ana.21053 · Cited by 156
Lipoprotein Mutations in Pigs Are Associated with Elevated Plasma Cholesterol and Atherosclerosis
Rapacz, J., Hasler‐Rapacz, J., Taylor, K. M., Checovich, W. J., & Attie, A. (1986) · Science · doi:10.1126/science.3787263 · Cited by 150
Bursill, C. A., Abbey, M., & Roach, P. D. (2006) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2006.08.033 · Cited by 149
Soluble fiber and nondigestible carbohydrate effects on plasma lipids and cardiovascular risk
Fernández, M. L. (2001) · Current Opinion in Lipidology · doi:10.1097/00041433-200102000-00007 · Cited by 149
Mutations in the RB1 Gene and Their Effects on Transcription
Dunn, J. M., Phillips, R. A., Zhu, X., Becker, A., & Gallie, B. L. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.11.4596 · Cited by 150
FUKI, I. V., MEYER, M. E., & WILLIAMS, K. J. (2000) · Biochemical Journal · doi:10.1042/bj3510607 · Cited by 151
Cayo, M. A., Cai, J., DeLaForest, A., Noto, F. K., Nagaoka, M., Clark, B. S., Collery, R. F., Si‐Tayeb, K., & Duncan, S. A. (2012) · Hepatology · doi:10.1002/hep.25871 · Cited by 153
Shen, W.-J., Asthana, S., Kraemer, F. B., & Azhar, S. (2018) · Journal of Lipid Research · doi:10.1194/jlr.r083121 · Cited by 148
Autoregulatory control of mitochondrial glutathione homeostasis
Liu, Y., Liu, S., Tomar, A., Yen, F. S., Ünlü, G., Ropek, N., Weber, R. A., Wang, Y., Khan, A., Gad, M., et al. (2023) · Science · doi:10.1126/science.adf4154 · Cited by 149
ACAT inhibitors as antiatherosclerotic agents: Compounds and mechanisms
Matsuda, K. (1994) · Medicinal Research Reviews · doi:10.1002/med.2610140302 · Cited by 148
Daumerie, C. M., Woollett, L. A., & Dietschy, J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.10797 · Cited by 147
Prevalence of lipoprotein (a) [Lp(a)] excess in coronary artery disease
Genest, J. J., Jenner, J. L., McNamara, J. R., Ordovás, J. M., Silberman, S. R., Wilson, P. W. F., & Schaefer, E. J. (1991) · The American Journal of Cardiology · doi:10.1016/0002-9149(91)90862-f · Cited by 148
Free radical modification of low-density lipoprotein: Mechanisms and biological consequences
Heinecke, J. W. (1987) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(87)90040-2 · Cited by 148
Polygenic Scores to Assess Atherosclerotic Cardiovascular Disease Risk
Aragam, K. G., & Natarajan, P. (2020) · Circulation Research · doi:10.1161/circresaha.120.315928 · Cited by 148
Jeong, A., Suazo, K. F., Wood, W. G., Distefano, M. D., & Li, L. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1458070 · Cited by 152
Oka, K., Pastore, L., Kim, I.-H., Merched, A. J., Nomura, S., Lee, H., Merched-Sauvage, M., Arden-Riley, C., Lee, B., Finegold, M. J., et al. (2001) · Circulation · doi:10.1161/01.cir.103.9.1274 · Cited by 146
Physiological and pathological implications of cholesterol
Cortés, V. (2014) · Frontiers in bioscience · doi:10.2741/4216 · Cited by 153
Postprandial lipoproteins and atherosclerosis
Kenneth, C.-W. Y. (2001) · Frontiers in bioscience · doi:10.2741/yu · Cited by 145
REVIEW: Efficacy and Mechanisms of Action of Statins in the Treatment of Diabetic Dyslipidemia
Ginsberg, H. N. (2006) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2005-2084 · Cited by 146
The pathogenesis and clinical significance of xanthelasma palpebrarum
Bergman, R. (1994) · Journal of the American Academy of Dermatology · doi:10.1016/s0190-9622(94)70023-0 · Cited by 145
Oxidized LDL, a critical factor in atherogenesis☆
Li, D., & Mehta, J. L. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.09.009 · Cited by 145
Parra-Peralbo, E., & Culí, J. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1001297 · Cited by 145
Understanding the molecular mechanisms of statin pleiotropic effects
German, C. A., & Liao, J. K. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03492-6 · Cited by 160
Hewat, E. A., Neumann, E., Conway, J. F., Moser, R., Ronacher, B., Marlovits, T. C., & Blaas, D. (2000) · The EMBO Journal · doi:10.1093/emboj/19.23.6317 · Cited by 144
Transport of Lipids from High and Low Density Lipoproteins via Scavenger Receptor-BI
Stangl, H., Hyatt, M., & Hobbs, H. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.32692 · Cited by 144
Genetic factors controlling structure and expression of apolipoproteins B and E in mice.
Lusis, A. J., Taylor, B. A., Quon, D., Zollman, S., & LeBoeuf, R. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47607-7 · Cited by 144
Pedersen, T. R., & Tobert, J. A. (2004) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.5.12.2583 · Cited by 147
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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