Receptor-Mediated Endocytosis: Concepts Emerging from the LDL Receptor System

Goldstein, Joseph L.; Brown, Michael S.; Anderson, Richard G. W.; Russell, David W.; Schneider, Wolfgang J.

doi:10.1146/annurev.cb.01.110185.000245

Cited by 1,541 publications

(691 citation statements)

References 118 publications

(140 reference statements)

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“…Nicotinic acid also has a synergistic effect with bile acid sequestrant resins in hypercholesterolaemic patients with reductions of up to 50% in LDL-cholesterol observed. Data from the CholesterolLowering Atherosclerosis Study (CLAS) of 162 patients with previous coronary artery by-pass surgery showed a significant reduction in angiographic deterioration over 2 years in subjects receiving combined colestipol (30 g daily) and niacin (3)(4)(5)(6)(7)(8)(9)(10)(11)(12) g daily) (33).…”

Section: Nicotinic Acid a N D Derivativesmentioning

confidence: 99%

Approaches to the management of hypercholesterolemia

Florkowski

Cramb

1992

Journal of Clinical Pharmacy and Therapeutics

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Section: Nicotinic Acid a N D Derivativesmentioning

confidence: 99%

Approaches to the management of hypercholesterolemia

Florkowski

Cramb

1992

Journal of Clinical Pharmacy and Therapeutics

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“…These receptors share a group of common structural elements, which include cysteine-rich ligand-binding (LB) or complement repeats [I]. The LDLR has a binding domain which consists of seven contiguous LB repeats, each -40 amino acids long [2]. with a repeating pattern of six cysteine residues and a highly conserved series of negatively charged amino acids near the COOH-terminus.…”

Section: Introductionmentioning

confidence: 99%

“…The LDLR utilizes these repeats to bind plasma lipoproteins that contain apolipoprotein (apo) B-IOO [3] and apoE [4]. Binding is believed to involve iOlliC interactions between acidic residues in the repeats and clusters of basic ammo acids in apoB-IOO and apoE [2]. LB repeats are not restncted to the LDL receptor family of cell surface receptors.…”

Section: Introductionmentioning

confidence: 99%

Expression and disulfide‐bond connectivity of the second ligand‐binding repeat of the human LDL receptor

et al. 1995

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The human LDL receptor (LDLR) has a binding domain which consists of seven contiguous ligand-binding (LB) repeats, each -40 amino acids long with three disulfide bonds. The second LB repeat, which is required for full binding of LDL, has been expressed, purified and folded to yield a single, fully oxidized isomer. By selective reduction and alkylation, we have shown that the cysteine residues have a I-III, II-V, IV-VI connectivity, matching that recently determined for the amino-terminal repeat. We suggest that the first two LB repeats of the LDLR, with their unique disulfide-bonding pattern, serve as a structural paradigm for other LB repeats.

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“…The concentration of LDL-cholesterol is to a large extent regulated by the interaction between apolipoprotein B^lOÖ-containhig LDL particles and LDL receptors (4,5). Different genetic defects in the LDL receptor gene redüce the removal of LDL particles via the LDL receptor pathway and lead to the disorder of familial hypercholesterolaemia (6).…”

Section: Introductionmentioning

confidence: 99%