ArticleJournal of lipid research2013
Helical domains that mediate lipid solubilization and ABCA1-specific cholesterol efflux in apolipoproteins C-I and A-II.
Article in Journal of lipid research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.
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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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Who cites it
16 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.
- Role of apolipoprotein C1 in lipoprotein metabolism, atherosclerosis and diabetes: a systematic review.Cardiovascular diabetology · 2022Pooled it
- Pharmacological Inhibition of CETP (Cholesteryl Ester Transfer Protein) Increases HDL (High-Density Lipoprotein) That Contains ApoC3 and Other HDL Subspecies Associated With Higher Risk of Coronary Heart Disease.Arteriosclerosis, thrombosis, and vascular biology · 2022Trial
- Identifying the Lipidomic Effects of a Rare Loss-of-Function Deletion inCirculation. Genomic and precision medicine · 2021Trial
- Albiflorin Alleviates Ox-LDL-Induced Human Umbilical Vein Endothelial Cell Injury through IRAK1/TAK1 Pathway.BioMed research international · 2022Article
- Apolipoprotein Mimetic Peptide Inhibits Neutrophil-Driven Inflammatory Damage via Membrane Remodeling and Suppression of Cell Lysis.ACS nano · 2021Article
- Protein-Defined Subspecies of HDLs (High-Density Lipoproteins) and Differential Risk of Coronary Heart Disease in 4 Prospective Studies.Arteriosclerosis, thrombosis, and vascular biology · 2020Article
- MicroRNA-144 Silencing Protects Against Atherosclerosis in Male, but Not Female Mice.Arteriosclerosis, thrombosis, and vascular biology · 2020Article
- Apolipoprotein C1: Its Pleiotropic Effects in Lipid Metabolism and Beyond.International journal of molecular sciences · 2019Review
- Development and application of a high throughput one-pot extraction protocol for quantitative LC-MS/MS analysis of phospholipids in serum and lipoprotein fractions in normolipidemic and dyslipidemic subjects.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2019Article
- From a Highly Disordered to a Metastable State: Uncovering Insights of α-Synuclein.ACS chemical neuroscience · 2018Article
- Characterization of covalent modifications of HDL apoproteins by endogenous oxidized phospholipids.Free radical biology & medicine · 2018Article
- Mapping Atheroprotective Functions and Related Proteins/Lipoproteins in Size Fractionated Human Plasma.Molecular & cellular proteomics : MCP · 2017Article
- On-column trypsin digestion coupled with LC-MS/MS for quantification of apolipoproteins.Journal of proteomics · 2017Article
- Article
- The roles of C-terminal helices of human apolipoprotein A-I in formation of high-density lipoprotein particles.Biochimica et biophysica acta · 2014Article
- Proteogenomic Review of the Changes in Primate apoC-I during Evolution.Frontiers in biology · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Many of the apolipoproteins in HDL can elicit cholesterol efflux via ABCA1, a critical initial step in HDL formation. Recent work has indicated that omnipresent amphipathic helices play a critical role, and these have been studied intensively in the most common HDL protein, apolipoprotein (apo)A-I. However, little information exists about helical domain arrangement in other apolipoproteins. We studied two of the smallest apolipoproteins known to interact with ABCA1, human apoA-II and apoC-I, in terms of ability to reorganize phospholipid (PL) bilayers and to promote ABCA1-mediated cholesterol. We found that both proteins contained helical domains that were fast and slow with respect to solubilizing PL. ABCA1-medated efflux required a minimum of a bihelical polypeptide comprised of at least one each of a slow and fast lipid reorganizing domain. In both proteins, the fast helix was located at the C terminus preceded by a slow helix. Helical placement in apoC-I was not critical for ABCA1 activity, but helix swaps in apoA-II dramatically disrupted cholesterol efflux, indicating that the tertiary structure of the longer apolipoprotein is important for the pathway. This work has implications for a more complete molecular understanding of apolipoprotein-mediated cholesterol efflux.
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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.