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

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

Scientific reports - 19 Oct 2017

Giudice Rita Del, Nilsson Oktawia, Domingo-Espín Joan, Lagerstedt Jens O

Abstract excerpt

Apolipoprotein A-I (apoA-I) in high-density lipoprotein (HDL) provides cardiovascular protection. Synchrotron radiation circular dichroism (SRCD) spectroscopy was used to analyze the dynamic solution structure of the apoA-I protein in the apo- and HDL-states and the protein structure conversion in HDL formation. Wild-type apoA-I protein was compared to human variants that either are protective (R173C, Milano) or...

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 Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipoproteins, HDL

Share to Polymorphism, Single Nucleotide

Share to Protein Binding

Share to Protein Conformation, beta-Strand

Share to Protein Stability

Share to Transition Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 29051568
DOI: 10.1038/s41598-017-13878-z
PMCID: PMC5648894

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

Synchrotron radiation circular dichroism spectroscopy reveals structural divergences in HDL-bound apoA-I variants.PMID 29051568Read ↗

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

Structural and Functional Analysis of the ApolipoproteinA-I A164S Variant.Semantic proximity Read ↗

Structural basis for distinct functions of the naturally occurring Cys mutants of human apolipoprotein A-I.Semantic proximity Read ↗

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

Understanding the role of apolipoproteinA-I in atherosclerosis. Post-translational modifications synergize dysfunction?Semantic proximity Read ↗

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

Delineating the impact of pathogenic mutations on the conformational dynamics of HDL's vital protein ApoA1: a combined computational and molecular dynamic simulation approach.Semantic proximity Read ↗

The structure-function relationship of atheroprotective ApoA-I mutants in high-density lipoproteinsSemantic proximity Read ↗

Biomedical applications of synchrotron radiation circular dichroism spectroscopy: identification of mutant proteins associated with disease and development of a reference database for fold motifs.Semantic proximity Read ↗

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

A model structure for the heterodimer apoA-IMilano-apoA-II supports its peculiar susceptibility to proteolysis.Semantic proximity Read ↗

Structure and functional properties of apolipoprotein C-II.Semantic proximity Read ↗

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