ArticleJournal of lipid research2010
Surface plasmon resonance analysis of the mechanism of binding of apoA-I to high density lipoprotein particles.
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 22 papers.
What it found
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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
22 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- Different Pathways of Cellular Cholesterol Efflux.Cell biochemistry and biophysics · 2022Review
- Interaction of human hemoglobin and semi-hemoglobins with the Staphylococcus aureus hemophore IsdB: a kinetic and mechanistic insight.Scientific reports · 2019Article
- Docking, thermodynamics and molecular dynamics (MD) studies of a non-canonical protease inhibitor, MP-4, from Mucuna pruriens.Scientific reports · 2018Article
- HDL structure and function is profoundly affected when stored frozen in the absence of cryoprotectants.Journal of lipid research · 2017Article
- Immunochemical Approach for Monitoring of Structural Transition of ApoA-I upon HDL Formation Using Novel Monoclonal Antibodies.Scientific reports · 2017Article
- ApoA1 and ApoA1-specific self-antibodies in cardiovascular disease.Laboratory investigation; a journal of technical methods and pathology · 2016Review
- On the acquisition and analysis of microscale thermophoresis data.Analytical biochemistry · 2016Article
- Structural stability and functional remodeling of high-density lipoproteins.FEBS letters · 2015Review
- Acidification of the intimal fluid: the perfect storm for atherogenesis.Journal of lipid research · 2015Review
- An in-silico model of lipoprotein metabolism and kinetics for the evaluation of targets and biomarkers in the reverse cholesterol transport pathway.PLoS computational biology · 2014Article
- Article
- 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
- Interactions of apolipoprotein A-I with high-density lipoprotein particles.Biochemistry · 2013Article
- Structural and functional analysis of APOA5 mutations identified in patients with severe hypertriglyceridemia.Journal of lipid research · 2013Article
- A sensitive assay for ABCA1-mediated cholesterol efflux using BODIPY-cholesterol.Journal of lipid research · 2011Article
- Apolipoprotein A-I structural organization in high-density lipoproteins isolated from human plasma.Nature structural & molecular biology · 2011Article
- Enhanced binding of apolipoprotein A-I variants associated with hypertriglyceridemia to triglyceride-rich particles.Biochemistry · 2011Article
- Molecular basis for the differences in lipid and lipoprotein binding properties of human apolipoproteins E3 and E4.Biochemistry · 2010Article
- Speciated human high-density lipoprotein protein proximity profiles.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The partitioning of apolipoprotein A-I (apoA-I) molecules in plasma between HDL-bound and -unbound states is an integral part of HDL metabolism. We used the surface plasmon resonance (SPR) technique to monitor in real time the reversible binding of apoA-I to HDL. Biotinylated human HDL(2) and HDL(3) were immobilized on a streptavidin-coated SPR sensor chip, and apoA-I solutions at different concentrations were flowed across the surface. The wild-type (WT) human and mouse apoA-I/HDL interaction involves a two-step process; apoA-I initially binds to HDL with fast association and dissociation rates, followed by a step exhibiting slower kinetics. The isolated N-terminal helix bundle domains of human and mouse apoA-I also exhibit a two-step binding process, consistent with the second slower step involving opening of the helix bundle domain. The results of fluorescence experiments with pyrene-labeled apoA-I are consistent with the N-terminal helix bundle domain interacting with proteins resident on the HDL particle surface. Dissociation constants (K(d)) measured for WT human apoA-I interactions with HDL(2) and HDL(3) are about 10 microM, indicating that the binding is low affinity. This K(d) value does not apply to all of the apoA-I molecules on the HDL particle but only to a relatively small, labile pool.
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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.