Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural and Functional Analysis of the ApolipoproteinA-I A164S Variant.

PloS one - 1 Jan 2015

Dalla-Riva Jonathan, Lagerstedt Jens O, Petrlova Jitka

Abstract excerpt

Apolipoprotein A-I (apoA-I) is the main protein involved in the formation of high-density lipoprotein (HDL), it is the principal mediator of the reverse cholesterol transfer (RCT) pathway and provides cardio-protection. In addition to functional wild-type apoA-I, several variants have been shown to associate with hereditary amyloidosis. In this study we have performed biophysical and biochemical analyses of the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Apolipoprotein A-I
Share to Cholesterol
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Aggregation, Pathological

Share to Protein Stability

Share to Protein Structure, Secondary

Share to Proteolysis

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 26605794
DOI: 10.1371/journal.pone.0143915
PMCID: PMC4659549

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and Functional Analysis of the ApolipoproteinA-I A164S Variant.PMID 26605794Read ↗

Structural Basis for the Pro-amyloidogenic Action and Ligand Binding of a Novel W72R Variant of Human Apolipoprotein A-I.Semantic proximity Read ↗

Structure-function analysis of naturally occurring apolipoprotein A-I L144R, A164S and L178P mutants provides insight on their role on HDL levels and cardiovascular risk.Semantic proximity Read ↗

Synchrotron radiation circular dichroism spectroscopy reveals structural divergences in HDL-bound apoA-I variants.Semantic proximity Read ↗

Structure dynamics of ApoA-I amyloidogenic variants in small HDL increase their ability to mediate cholesterol effluxSemantic proximity Read ↗

Molecular Insights into Human Hereditary Apolipoprotein A-I Amyloidosis Caused by the Glu34Lys Mutation.Semantic proximity Read ↗

Structure, function and amyloidogenic propensity of apolipoprotein A-I.Semantic proximity Read ↗

Leveraging knowledge of HDLs major protein ApoA1: Structure, function, mutations, and potential therapeutics.Semantic proximity Read ↗

Amyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosis.Semantic proximity Read ↗

Structural and functional consequences of the Milano mutation (R173C) in human apolipoprotein A-I.Semantic proximity Read ↗

Mutation in APOA1 predicts increased risk of ischaemic heart disease and total mortality without low HDL cholesterol levels.Semantic proximity Read ↗

Natural variants of apolipoprotein A1 L99P and R173P exhibited a high degree of amyloid fibril formation: Implications for high-density lipoprotein functions and disease pathogenesis.Semantic proximity Read ↗

Structural analysis of APOB variants, p.(Arg3527Gln), p.(Arg1164Thr) and p.(Gln4494del), causing Familial Hypercholesterolaemia provides novel insights into variant pathogenicity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.