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

Salt bridge relay triggers defective LDL receptor binding by a mutant apolipoprotein.

Structure (London, England : 1993) - 15 Aug 1994

Wilson C, Mau T, Weisgraber K H, Wardell M R, Mahley R W, Agard D A

Abstract excerpt

BACKGROUND: Apolipoprotein-E (apo-E), a 34kDa blood plasma protein, plays a key role in directing cholesterol transport via its interaction with the low density lipoprotein (LDL) receptor. The amino-terminal domain of apo-E forms an unusually elongated four-helix bundle arranged such that key basic residues involved in LDL receptor binding form a cluster at the end of one of the helices. A common apo-E variant,...

Read the complete abstract on PubMed

Topics

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

Share to Apolipoprotein E2
Share to Apolipoproteins E
Share to Computer Simulation

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

Share to Models, Molecular

Share to Mutation

Share to Peptide Fragments

Share to Protein Conformation

Share to Receptors, LDL

Source

Identifiers

PMID: 7994571
DOI: 10.1016/s0969-2126(00)00072-1

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

Salt bridge relay triggers defective LDL receptor binding by a mutant apolipoprotein.PMID 7994571Read ↗

Familial dysbetalipoproteinemia: a genetically heterogenous disease caused by mutations of the ligand apolipoprotein E.Semantic proximity Read ↗

Low-density lipoprotein receptor structure and folding.Semantic proximity Read ↗

Characterization of five new mutants in the carboxyl-terminal domain of human apolipoprotein E: no cosegregation with severe hyperlipidemia.Semantic proximity Read ↗

The APOL1 variant p.N264K blocks ion flow by occluding a pore at the cell surfaceSemantic proximity Read ↗

Diminished LDL receptor and high heparin binding of apolipoprotein E2 Sendai associated with lipoprotein glomerulopathy.Semantic proximity Read ↗

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

The functional characteristics of a human apolipoprotein E variant (cysteine at residue 142) may explain its association with dominant expression of type III hyperlipoproteinemia.Semantic proximity Read ↗

Apolipoprotein E2-Dunedin (228 Arg replaced by Cys): an apolipoprotein E2 variant with normal receptor-binding activity.Semantic proximity Read ↗

Structure and functional properties of apolipoprotein C-II.Semantic proximity Read ↗

Molecular mechanisms of type III hyperlipoproteinemia: The contribution of the carboxy-terminal domain of ApoE can account for the dyslipidemia that is associated with the E2/E2 phenotype.Semantic proximity Read ↗

Mechanism of LDL binding and release probed by structure-based mutagenesis of the LDL receptor.Semantic proximity Read ↗

TM6SF2 binds cholesterol, interacts with apolipoprotein B, and promotes hepatic lipid secretionSemantic proximity Read ↗

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