ArticleCommunications biology2020
Structural analysis of lecithin:cholesterol acyltransferase bound to high density lipoprotein particles.
Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 50 citations in OpenAlex.
- Integrated Transcriptomic and Metabolomic Profiling Reveals Candidate Genes and Metabolites Associated with Abdominal Fat Deposition in Pekin Ducks.Animals : an open access journal from MDPI · 2026Article
- Cholesterol Crystallization Tests the Limits of Microscopic Reversibility for Molecular Pathways of Growth and Dissolution.ACS central science · 2026Article
- Lecithin:cholesterol acyltransferase binds a discontinuous binding site on adjacent apolipoprotein A-I belts in HDL.Journal of lipid research · 2025Article
- Apolipoprotein-A1 transports and regulates MMP2 in the blood.Nature communications · 2025Article
- Direct observation of cholesterol monohydrate crystallization.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Role of Lipids in Atherosclerosis: Focus on Molecular Biology Mechanisms and Therapeutic Approaches.Current medicinal chemistry · 2025Review
- Understanding the heterogeneity and dysfunction of HDL in chronic kidney disease: insights from recent reviews.BMC nephrology · 2024Review
- Multimodal Mass Spectrometry Identifies a Conserved Protective Epitope inAnalytical chemistry · 2024Article
- Systematic evaluation of lecithin:cholesterol acyltransferase binding sites in apolipoproteins via peptide based nanodiscs: regulatory role of charged residues at positions 4 and 7.PLoS computational biology · 2024Article
- Purple perilla frutescens extracts containing α-asarone inhibit inflammatory atheroma formation and promote hepatic HDL cholesterol uptake in dyslipidemic apoE-deficient mice.Nutrition research and practice · 2023Article
- Cross-Linking Mass Spectrometry Uncovers Interactions Between High-Density Lipoproteins and the SARS-CoV-2 Spike Glycoprotein.Molecular & cellular proteomics : MCP · 2023Article
- Mechanistic Insights into the Activation of Lecithin-Cholesterol Acyltransferase in Therapeutic Nanodiscs Composed of Apolipoprotein A-I Mimetic Peptides and Phospholipids.Molecular pharmaceutics · 2022Article
- Alterations of HDL's to piHDL's Proteome in Patients with Chronic Inflammatory Diseases, and HDL-Targeted Therapies.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Influence of lecithin cholesterol acyltransferase alteration during different pathophysiologic conditions: A 45 years bibliometrics analysis.Frontiers in pharmacology · 2022Article
- Apolipoprotein A1-Related Proteins and Reverse Cholesterol Transport in Antiatherosclerosis Therapy: Recent Progress and Future Perspectives.Cardiovascular therapeutics · 2022Review
- Pathways and Mechanisms of Cellular Cholesterol Efflux-Insight From Imaging.Frontiers in cell and developmental biology · 2022Review
- Glycosylation of HDL-Associated Proteins and Its Implications in Cardiovascular Disease Diagnosis, Metabolism and Function.Frontiers in cardiovascular medicine · 2022Review
- Effects of Elaidic Acid on HDL Cholesterol Uptake Capacity.Nutrients · 2021Article
- Positive allosteric modulators of lecithin: Cholesterol acyltransferase adjust the orientation of the membrane-binding domain and alter its spatial free energy profile.PLoS computational biology · 2021Article
- rHDL modeling and the anchoring mechanism of LCAT activation.Journal of lipid research · 2021Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
Lecithin:cholesterol acyltransferase (LCAT) catalyzes a critical step of reverse cholesterol transport by esterifying cholesterol in high density lipoprotein (HDL) particles. LCAT is activated by apolipoprotein A-I (ApoA-I), which forms a double belt around HDL, however the manner in which LCAT engages its lipidic substrates and ApoA-I in HDL is poorly understood. Here, we used negative stain electron microscopy, crosslinking, and hydrogen-deuterium exchange studies to refine the molecular details of the LCAT-HDL complex. Our data are consistent with LCAT preferentially binding to the edge of discoidal HDL near the boundary between helix 5 and 6 of ApoA-I in a manner that creates a path from the lipid bilayer to the active site of LCAT. Our results provide not only an explanation why LCAT activity diminishes as HDL particles mature, but also direct support for the anti-parallel double belt model of HDL, with LCAT binding preferentially to the helix 4/6 region.
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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.