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

Evolutionary and structural constraints influencing apolipoprotein A-I amyloid behavior.

Proteins - 1 Jan 2022

Gisonno Romina A, Masson Tomas, Ramella Nahuel A, Barrera Exequiel E, Romanowski Víctor, Tricerri M Alejandra

Abstract excerpt

Apolipoprotein A-I (apoA-I) has a key function in the reverse cholesterol transport. However, aggregation of apoA-I single point mutants can lead to hereditary amyloid pathology. Although several studies have tackled the biophysical and structural consequences introduced by these mutations, there is little information addressing the relationship between the evolutionary and structural features that contribute to...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Amyloid
Share to Apolipoprotein A-I

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Conserved Sequence

Share to Evolution, Molecular

Share to Molecular Dynamics Simulation

Share to Protein Stability

Share to Thermodynamics

Source

Identifiers

PMID: 34414600
DOI: 10.1002/prot.26217

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

Evolutionary and structural constraints influencing apolipoprotein A-I amyloid behavior.PMID 34414600Read ↗

Evolutionary and Structural Constraints Influencing Apolipoprotein A-I Amyloid BehaviourSemantic 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 ↗

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

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

Molecular simulation unravels the amyloidogenic misfolding of nascent ApoA1 protein, driven by deleterious point mutations occurring in between 170-178 hotspot region.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 ↗

New variants of alpha-1-antitrypsin: structural simulations and clinical expression.Semantic proximity Read ↗

Protein conformational perturbations in hereditary amyloidosis: Differential impact of single point mutations in ApoAI amyloidogenic variantsSemantic proximity Read ↗

Effects of the known pathogenic mutations on the aggregation pathway of the amyloidogenic peptide of apolipoprotein A-I.Semantic proximity Read ↗

Structural stability and local dynamics in disease-causing mutants of human apolipoprotein a-I: what makes the protein amyloidogenic?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 ↗

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