ArticlePloS one2015
Amyloidogenic propensity of a natural variant of human apolipoprotein A-I: stability and interaction with ligands.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 31 citations in OpenAlex.
- Studying biological events using biopolymeric matrices.Biophysical reviews · 2025Review
- Effects of superoxide anion attack on the lipoprotein HDL.Molecular and cellular biochemistry · 2023Article
- On the Aggregation of Apolipoprotein A-I.International journal of molecular sciences · 2022Article
- Lipids and Lipoproteins in Health and Disease: Focus on Targeting Atherosclerosis.Biomedicines · 2021Review
- Effects of Ionic Liquids on Metalloproteins.Molecules (Basel, Switzerland) · 2021Review
- Probing the Structure-Function relationship and amyloidogenic propensities in natural variants of apolipoprotein A-I.Biochemistry and biophysics reports · 2020Article
- Data regarding the sensibility to proteolysis of a natural apolipoprotein A-I mutant.Data in brief · 2020Article
- Molecular Insights into Human Hereditary Apolipoprotein A-I Amyloidosis Caused by the Glu34Lys Mutation.Biochemistry · 2018Article
- Effect of Phosphatidylserine and Cholesterol on Membrane-mediated Fibril Formation by the N-terminal Amyloidogenic Fragment of Apolipoprotein A-I.Scientific reports · 2018Article
- Learning from Synthetic Models of Extracellular Matrix; Differential Binding of Wild Type and Amyloidogenic Human Apolipoprotein A-I to Hydrogels Formed from Molecules Having Charges Similar to Those Found in Natural GAGs.The protein journal · 2017Article
- Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A number of naturally occurring mutations of human apolipoprotein A-I (apoA-I) have been associated with hereditary amyloidoses. The molecular mechanisms involved in amyloid-associated pathology remain largely unknown. Here we examined the effects of the Arg173Pro point mutation in apoA-I on the structure, stability, and aggregation propensity, as well as on the ability to bind to putative ligands. Our results indicate that the mutation induces a drastic loss of stability, and a lower efficiency to bind to phospholipid vesicles at physiological pH, which could determine the observed higher tendency to aggregate as pro-amyloidogenic complexes. Incubation under acidic conditions does not seem to induce significant desestabilization or aggregation tendency, neither does it contribute to the binding of the mutant to sodium dodecyl sulfate. While the binding to this detergent is higher for the mutant as compared to wt apoA-I, the interaction of the Arg173Pro variant with heparin depends on pH, being lower at pH 5.0 and higher than wt under physiological pH conditions. We suggest that binding to ligands as heparin or other glycosaminoglycans could be key events tuning the fine details of the interaction of apoA-I variants with the micro-environment, and probably eliciting the toxicity of these variants in hereditary amyloidoses.
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