ArticleThe Journal of biological chemistry2012
Apolipoprotein A-II-mediated conformational changes of apolipoprotein A-I in discoidal high density lipoproteins.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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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Who cites it
12 citing papers in PubMed, 14 citations in OpenAlex.
- Apolipoprotein(a)-rich electronegative HDL accelerates vascular aging and atherosclerosis by inducing endothelial senescence.GeroScience · 2026Article
- Altered High-Density Lipoprotein Expression Pattern in the Aqueous Humor From Eyes With Age-Related Macular Degeneration.Investigative ophthalmology & visual science · 2025Article
- Predictive Value of Second-Trimester Maternal Lipid Profiling in Early-Onset Pre-eclampsia: A Prospective Cohort Study and Nomogram.Frontiers in medicine · 2021Article
- A thumbwheel mechanism for APOA1 activation of LCAT activity in HDL.Journal of lipid research · 2018Article
- Modification by isolevuglandins, highly reactive γ-ketoaldehydes, deleteriously alters high-density lipoprotein structure and function.The Journal of biological chemistry · 2018Article
- Apolipoprotein A-II alters the proteome of human lipoproteins and enhances cholesterol efflux from ABCA1.Journal of lipid research · 2017Article
- Depletion in LpA-I:A-II particles enhances HDL-mediated endothelial protection in familial LCAT deficiency.Journal of lipid research · 2017Article
- Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Analytical chemistry · 2015Review
- Influence of apolipoprotein A-I and apolipoprotein A-II availability on nascent HDL heterogeneity.Journal of lipid research · 2013Article
- New insights into the determination of HDL structure by apolipoproteins: Thematic review series: high density lipoprotein structure, function, and metabolism.Journal of lipid research · 2013Review
- Role of apolipoprotein A-II in the structure and remodeling of human high-density lipoprotein (HDL): protein conformational ensemble on HDL.Biochemistry · 2012Article
- Naturally occurring variant of mouse apolipoprotein A-I alters the lipid and HDL association properties of the protein.Journal of lipid research · 2012Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
It is well accepted that HDL has the ability to reduce risks for several chronic diseases. To gain insights into the functional properties of HDL, it is critical to understand the HDL structure in detail. To understand interactions between the two major apolipoproteins (apos), apoA-I and apoA-II in HDL, we generated highly defined benchmark discoidal HDL particles. These particles were reconstituted using a physiologically relevant phospholipid, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) incorporating two molecules of apoA-I and one homodimer of apoA-II per particle. We utilized two independent mass spectrometry techniques to study these particles. The techniques are both sensitive to protein conformation and interactions and are namely: 1) hydrogen deuterium exchange combined with mass spectrometry and 2) partial acetylation of lysine residues combined with MS. Comparison of mixed particles with apoA-I only particles of similar diameter revealed that the changes in apoA-I conformation in the presence of apoA-II are confined to apoA-I helices 3-4 and 7-9. We discuss these findings with respect to the relative reactivity of these two particle types toward a major plasma enzyme, lecithin:cholesterol acyltransferase responsible for the HDL maturation process.
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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.