ArticleJournal of lipid research2010
Mechanism of LDL binding and release probed by structure-based mutagenesis of the LDL receptor.
Article in Journal of lipid research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 54 citations in OpenAlex.
- Century of Progress on the Structure of APOB-100 in Atherogenic Lipoproteins.Circulation research · 2026Review
- Exploring the Role of Transcriptomics, Proteomics, and Machine Learning in HPV Infection and Cardiovascular Disease.Biomedicines · 2025Review
- In silico prediction of the binding structure between vitellogenin and vitellogenin receptor of Haemaphysalis longicornis.The Journal of veterinary medical science · 2025Article
- Structural dynamics of LDL receptor interactions with E498A and R499G variants of PCSK9.Journal of molecular modeling · 2025Article
- AFM reveals differential effects of acidification on LDL- and oxidized LDL-receptor interactions: biomechanical implications in atherogenesis.Cellular & molecular biology letters · 2025Article
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- Endosome rupture enables enteroviruses from the family Picornaviridae to infect cells.Communications biology · 2024Article
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- A New Structural Model of Apolipoprotein B100 Based on Computational Modeling and Cross Linking.International journal of molecular sciences · 2022Article
- New Treatment Targets and Innovative Lipid-Lowering Therapies in Very-High-Risk Patients with Cardiovascular Disease.Biomedicines · 2022Review
- Protective effects of mitochondrial fission inhibition on ox-LDL induced VSMC foaming via metabolic reprogramming.Frontiers in pharmacology · 2022Article
- PCSK9 promotes tumor growth by inhibiting tumor cell apoptosis in hepatocellular carcinoma.Experimental hematology & oncology · 2021Article
- Lipoprotein metabolism in familial hypercholesterolemia.Journal of lipid research · 2021Review
- Article
- Mutation type classification and pathogenicity assignment of sixteen missense variants located in the EGF-precursor homology domain of the LDLR.Scientific reports · 2020Article
- Molecular dissection of the Erv41-Erv46 retrograde receptor reveals a conserved cysteine-rich region in Erv46 required for retrieval activity.Molecular biology of the cell · 2020Article
- Lipids in Children and Links to Adult Vascular Disease.The Clinical biochemist. Reviews · 2018Review
- Site-specificThe Journal of biological chemistry · 2018Article
- Replacement of cysteine at position 46 in the first cysteine-rich repeat of the LDL receptor impairs apolipoprotein recognition.PloS one · 2018Article
- PCSK9 as a therapeutic target for cardiovascular disease.Experimental and therapeutic medicine · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The LDL receptor (LDL-R) mediates cholesterol metabolism in humans by binding and internalizing cholesterol transported by LDL. Several different molecular mechanisms have been proposed for the binding of LDL to LDL-R at neutral plasma pH and for its release at acidic endosomal pH. The crystal structure of LDL-R at acidic pH shows that the receptor folds back on itself in a closed form, obscuring parts of the ligand binding domain with the epidermal growth factor (EGF)-precursor homology domain. We have used a structure-based site-directed mutagenesis approach to examine 12 residues in the extracellular domain of LDL-R for their effect on LDL binding and release. Our studies show that the interface between the ligand binding domain and the EGF-precursor homology domain seen at acidic pH buries residues mediating both LDL binding and release. Our results are consistent with an alternative model of LDL-R whereby multiple modules of the extracellular domain interact with LDL at neutral pH, concurrently positioning key residues so that at acidic pH the LDL-R:LDL interactions become unfavorable, triggering release. After LDL release, the closed form of LDL-R may target its return to the cell surface.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.