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

ABCA1 and amphipathic apolipoproteins form high-affinity molecular complexes required for cholesterol efflux.

Journal of lipid research - 1 Feb 2004

Fitzgerald M L, Morris A L, Chroni A, Mendez A J, Zannis V I, Freeman M W

Abstract excerpt

Apolipoproteins, such as apolipoprotein A-I (apoA-I), can stimulate cholesterol efflux from cells expressing the ATP binding cassette transporter A1 (ABCA1). The nature of the molecular interaction between these cholesterol acceptors and ABCA1 is controversial, and models suggesting a direct protein-protein interaction or indirect association have been proposed. To explore this issue, we performed competition...

Read the complete abstract on PubMed

Topics

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

Share to Adenoviridae
Share to Apolipoproteins
Share to ATP Binding Cassette Transporter 1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Line, Transformed

Share to Cholesterol

Share to Lipid Metabolism

Share to Macromolecular Substances

Share to Transduction, Genetic

Source

Identifiers

PMID: 14617740
DOI: 10.1194/jlr.M300355-JLR200

Genes

ABCA1

Variants

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

ABCA1 and amphipathic apolipoproteins form high-affinity molecular complexes required for cholesterol efflux.PMID 14617740Read ↗

ATP-binding cassette transporter A1 (ABCA1) functions as a cholesterol efflux regulatory protein.Semantic proximity Read ↗

Naturally occurring mutations in the largest extracellular loops of ABCA1 can disrupt its direct interaction with apolipoprotein A-I.Semantic proximity Read ↗

Influence of ApoA-I structure on the ABCA1-mediated efflux of cellular lipids.Semantic proximity Read ↗

An amphipathic helical region of the N-terminal barrel of phospholipid transfer protein is critical for ABCA1-dependent cholesterol efflux.Semantic proximity Read ↗

ABCA1 mutants reveal an interdependency between lipid export function, apoA-I binding activity, and Janus kinase 2 activation.Semantic proximity Read ↗

Phospholipid transfer protein interacts with and stabilizes ATP-binding cassette transporter A1 and enhances cholesterol efflux from cells.Semantic proximity Read ↗

Carboxyl terminus of apolipoprotein A-I (ApoA-I) is necessary for the transport of lipid-free ApoA-I but not prelipidated ApoA-I particles through aortic endothelial cells.Semantic proximity Read ↗

The effects of mutations in helices 4 and 6 of ApoA-I on scavenger receptor class B type I (SR-BI)-mediated cholesterol efflux suggest that formation of a productive complex between reconstituted high density lipoprotein and SR-BI is required for efficient lipid transport.Semantic proximity Read ↗

The central helices of ApoA-I can promote ATP-binding cassette transporter A1 (ABCA1)-mediated lipid efflux. Amino acid residues 220-231 of the wild-type ApoA-I are required for lipid efflux in vitro and high density lipoprotein formation in vivo.Semantic proximity Read ↗

ABCA1 dimer-monomer interconversion during HDL generation revealed by single-molecule imaging.Semantic proximity Read ↗

ApoA-I dissociated from human HDL retains its acceptor properties in ABCA1-mediated cholesterol efflux from RAW 264.7 macrophages in coronary artery diseaseSemantic proximity Read ↗

Specific docking of apolipoprotein A-I at the cell surface requires a functional ABCA1 transporter.Semantic proximity Read ↗

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