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

Enhanced binding of apolipoprotein A-I variants associated with hypertriglyceridemia to triglyceride-rich particles.

Biochemistry - 29 Mar 2011

Gorshkova Irina N, Atkinson David

Abstract excerpt

Hypertriglyceridemia (HTG) is a common lipid abnormality in humans. However, its etiology remains largely unknown. It was shown that severe HTG can be induced in mice by overexpression of wild-type (WT) apolipoprotein E (apoE) or specific apoA-I mutants. Certain mutations in apoE4 were found to affect plasma triglyceride (TG) levels in mice overexpressing the protein. HTG appeared to positively correlate with 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 Hypertriglyceridemia
Share to Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutant Proteins

Share to Protein Binding

Share to Protein Conformation

Share to Protein Stability

Share to Triglycerides

Source

Open in PubMed Open full text

Identifiers

PMID: 21288012
DOI: 10.1021/bi200158b
PMCID: PMC6128146

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

Enhanced binding of apolipoprotein A-I variants associated with hypertriglyceridemia to triglyceride-rich particles.PMID 21288012Read ↗

Biophysical properties of apolipoprotein E4 variants: implications in molecular mechanisms of correction of hypertriglyceridemia.Semantic proximity Read ↗

ApoC-III helical structure determines its ability to bind plasma lipoproteins and inhibit Lipoprotein Lipase-mediated triglyceride lipolysisSemantic proximity Read ↗

Effects of polymorphism on the lipid interaction of human apolipoprotein E.Semantic proximity Read ↗

Alteration of negatively charged residues in the 89 to 99 domain of apoA-I affects lipid homeostasis and maturation of HDL.Semantic proximity Read ↗

Structural insights on the deformations induced by various mutations on cholesteryl ester transfer protein.Semantic proximity Read ↗

Bulky hydrophobic side chains in the β1-sandwich of microsomal triglyceride transfer protein are critical for the transfer of both triglycerides and phospholipids.Semantic proximity Read ↗

Plasma apoAV levels are markedly elevated in severe hypertriglyceridemia and positively correlated with the APOA5 S19W polymorphism.Semantic proximity Read ↗

Molecular basis for the differences in lipid and lipoprotein binding properties of human apolipoproteins E3 and E4.Semantic proximity Read ↗

Allele-dependent thermodynamic and structural perturbations in ApoE variants associated with the correction of dyslipidemia and formation of spherical ApoE-containing HDL particles.Semantic proximity Read ↗

Novel N-terminal mutation of human apolipoprotein A-I reduces self-association and impairs LCAT activation.Semantic proximity Read ↗

Mutation of F417 but not of L418 or L420 in the lipid binding domain decreases the activity of triacylglycerol hydrolase.Semantic proximity Read ↗

The composition, structural properties and binding of very-low-density and low-density lipoproteins to the LDL receptor in normo- and hypertriglyceridemia: relation to the apolipoprotein E phenotype.Semantic proximity Read ↗

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