ArticleJournal of lipid research2009
Structural and functional consequences of the Milano mutation (R173C) in human apolipoprotein A-I.
Article in Journal of lipid research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 64 citations in OpenAlex.
- Apolipoprotein A1 and high-density lipoprotein limit low-density lipoprotein transcytosis by binding SR-B1.Journal of lipid research · 2024Article
- Closing the gaps in patient management of dyslipidemia: stepping into cardiovascular precision diagnostics with apolipoprotein profiling.Clinical proteomics · 2024Review
- HDL-Based Therapy: Vascular Protection at All Stages.Biomedicines · 2023Review
- ApoA-I Infusion Therapies Following Acute Coronary Syndrome: Past, Present, and Future.Current atherosclerosis reports · 2022Review
- Apolipoproteins in vascular biology and atherosclerotic disease.Nature reviews. Cardiology · 2022Review
- Sensitive Morphological Characterization of Oriented High-Density Lipoprotein Nanoparticles UsingAngewandte Chemie (International ed. in English) · 2020Article
- Arginine 123 of apolipoprotein A-I is essential for lecithin:cholesterol acyltransferase activity.Journal of lipid research · 2018Article
- Primary genetic disorders affecting high density lipoprotein (HDL).Drugs in context · 2018Review
- Lipid-free Apolipoprotein A-I Structure: Insights into HDL Formation and Atherosclerosis Development.Archives of medical research · 2015Review
- Spectroscopic Characterization of Structural Changes in Membrane Scaffold Proteins Entrapped within Mesoporous Silica Gel Monoliths.ACS applied materials & interfaces · 2015Article
- Analysis of lipid phase behavior and protein conformational changes in nanolipoprotein particles upon entrapment in sol-gel-derived silica.Langmuir : the ACS journal of surfaces and colloids · 2014Article
- Amyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosis.The FEBS journal · 2014Article
- Secondary structure changes in ApoA-I Milano (R173C) are not accompanied by a decrease in protein stability or solubility.PloS one · 2014Article
- Structural basis for distinct functions of the naturally occurring Cys mutants of human apolipoprotein A-I.Journal of lipid research · 2013Review
- Mechanisms responsible for the compositional heterogeneity of nascent high density lipoprotein.The Journal of biological chemistry · 2013Article
- Molecular mechanisms responsible for the differential effects of apoE3 and apoE4 on plasma lipoprotein-cholesterol levels.Arteriosclerosis, thrombosis, and vascular biology · 2013Article
- Effects of the Iowa and Milano mutations on apolipoprotein A-I structure and dynamics determined by hydrogen exchange and mass spectrometry.Biochemistry · 2012Article
- Tweaking the cholesterol efflux capacity of reconstituted HDL.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2012Article
- Expressed protein ligation-mediated template protein extension.Protein expression and purification · 2012Article
- Influence of C-terminal α-helix hydrophobicity and aromatic amino acid content on apolipoprotein A-I functionality.Biochimica et biophysica acta · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Carriers of the apolipoprotein A-I(Milano) (apoA-I(M)) variant, R173C, have reduced levels of plasma HDL but no increase in cardiovascular disease. Despite intensive study, it is not clear whether the removal of the arginine or the introduction of the cysteine is responsible for this altered functionality. We investigated this question using two engineered variations of the apoA-I(M) mutation: R173S apoA-I, similar to apoA-I(M) but incapable of forming a disulfide bond, and R173K apoA-I, a conservative mutation. Characterization of the lipid-free proteins showed that the order of stability was wild type approximately R173K>R173S>R173C. Compared with wild-type apoA-I, apoA-I(M) had a lower affinity for lipids, while R173S apoA-I displayed intermediate affinity. The in vivo effects of the apoA-I variants were measured by injecting apoA-I-expressing adeno-associated virus into apoA-I-null mice. Mice that expressed the R173S variant again showed an intermediate phenotype. Thus, both the loss of the arginine and its replacement by a cysteine contribute to the altered properties of apoA-I(M). The arginine is potentially involved in an intrahelical salt bridge with E169 that is disrupted by the loss of the positively charged arginine and repelled by the cysteine, destabilizing the helix bundle domain in the apoA-I molecule and modifying its lipid binding characteristics.
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