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

Role of the hydrophobic and charged residues in the 218-226 region of apoA-I in the biogenesis of HDL.

Journal of lipid research - 1 Dec 2013

Fotakis Panagiotis, Kateifides Andreas K, Gkolfinopoulou Christina, Georgiadou Dimitra, Beck Melissa, Gründler Katharina, Chroni Angeliki, Stratikos Efstratios, Kardassis Dimitris, Zannis Vassilis I

Abstract excerpt

We investigated the significance of hydrophobic and charged residues 218-226 on the structure and functions of apoA-I and their contribution to the biogenesis of HDL. Adenovirus-mediated gene transfer of apoA-I[L218A/L219A/V221A/L222A] in apoA-I⁻/⁻ mice decreased plasma cholesterol and apoA-I levels to 15% of wild-type (WT) control mice and generated pre-β- and α4-HDL particles. In apoA-I⁻/⁻ × apoE⁻/⁻ mice, the...

Read the complete abstract on PubMed

Topics

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

Share to Adenoviridae
Share to Apolipoprotein A-I

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Lipoproteins, HDL

Share to Protein Structure, Secondary

Share to Protein Unfolding

Share to Temperature

Share to Transgenes

Source

Open in PubMed Open full text

Identifiers

PMID: 23990662
DOI: 10.1194/jlr.M038356
PMCID: PMC3826676

Genes

ABCA1
LCAT

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of the hydrophobic and charged residues in the 218-226 region of apoA-I in the biogenesis of HDL.PMID 23990662Read ↗

Significance of the hydrophobic residues 225-230 of apoA-I for the biogenesis of HDL.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 ↗

In vivo studies of HDL assembly and metabolism using adenovirus-mediated transfer of ApoA-I mutants in ApoA-I-deficient mice.Semantic proximity Read ↗

Point mutations in apolipoprotein A-I mimic the phenotype observed in patients with classical lecithin:cholesterol acyltransferase deficiency.Semantic proximity Read ↗

Naturally occurring and bioengineered apoA-I mutations that inhibit the conversion of discoidal to spherical HDL: the abnormal HDL phenotypes can be corrected by treatment with LCAT.Semantic proximity Read ↗

Distinct central amphipathic alpha-helices in apolipoprotein A-I contribute to the in vivo maturation of high density lipoprotein by either activating lecithin-cholesterol acyltransferase or binding lipids.Semantic proximity Read ↗

LCAT can rescue the abnormal phenotype produced by the natural ApoA-I mutations (Leu141Arg)Pisa and (Leu159Arg)FIN.Semantic proximity Read ↗

Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL.Semantic proximity Read ↗

HDL Dysfunction Caused by Mutations in apoA-I and Other Genes that are Critical for HDL Biogenesis and Remodeling.Semantic proximity Read ↗

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

Residues Leu261, Trp264, and Phe265 account for apolipoprotein E-induced dyslipidemia and affect the formation of apolipoprotein E-containing high-density lipoprotein.Semantic proximity Read ↗

Effect of apoA-I Mutations in the Capacity of Reconstituted HDL to Promote ABCG1-Mediated Cholesterol Efflux.Semantic proximity Read ↗

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