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

Apolipoprotein A-I adopts a belt-like orientation in reconstituted high density lipoproteins.

The Journal of biological chemistry - 16 Nov 2001

Panagotopulos S E, Horace E M, Maiorano J N, Davidson W S

Abstract excerpt

Apolipoprotein A-I (apoA-I) is the major protein associated with high density lipoprotein (HDL), and its plasma levels have been correlated with protection against atherosclerosis. Unfortunately, the structural basis of this phenomenon is not fully understood. Over 25 years of study have produced two general models of apoA-I structure in discoidal HDL complexes. The "belt" model states that the amphipathic...

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 Lipid Bilayers
Share to Lipids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipoproteins, HDL

Share to Nucleic Acid Conformation

Share to Phospholipids

Share to Spectrometry, Fluorescence

Share to Tryptophan

Source

Identifiers

PMID: 11557764
DOI: 10.1074/jbc.M106462200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Apolipoprotein A-I adopts a belt-like orientation in reconstituted high density lipoproteins.PMID 11557764Read ↗

Identification and structural ramifications of a hinge domain in apolipoprotein A-I discoidal high-density lipoproteins of different size.Semantic proximity Read ↗

Apolipoprotein A-I assumes a "looped belt" conformation on reconstituted high density lipoprotein.Semantic proximity Read ↗

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

A thumbwheel mechanism for APOA1 activation of LCAT activity in HDL.Semantic proximity Read ↗

Domain structure and lipid interaction in human apolipoproteins A-I and E, a general model.Semantic proximity Read ↗

Tryptophan probes reveal residue-specific phospholipid interactions of apolipoprotein C-III.Semantic proximity Read ↗

Inter-ring rotation of apolipoprotein A-I protein monomers for the double-belt model using biased molecular dynamics.Semantic proximity Read ↗

The C-terminal domain of apolipoprotein A-I contains a lipid-sensitive conformational trigger.Semantic proximity Read ↗

Structure and stability of apolipoprotein a-I in solution and in discoidal high-density lipoprotein probed by double charge ablation and deletion mutation.Semantic proximity Read ↗

Apolipoprotein interaction induces shape remodeling and lipid phase separation in giant unilamellar vesiclesSemantic proximity Read ↗

Conformational reorganization of the four-helix bundle of human apolipoprotein E in binding to phospholipid.Semantic proximity Read ↗

Crystal structure of C-terminal truncated apolipoprotein A-I reveals the assembly of high density lipoprotein (HDL) by dimerization.Semantic proximity Read ↗

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