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

Identification of structural mutations in the fifth domain of apolipoprotein H (beta 2-glycoprotein I) which affect phospholipid binding.

Human molecular genetics - 1 Feb 1997

Sanghera D K, Wagenknecht D R, McIntyre J A, Kamboh M I

Abstract excerpt

Apolipoprotein H (apoH), also known as beta 2-glycoprotein-I, is considered to be a cofactor for the binding of certain antiphospholipid autoantibodies to negatively charged phospholipids. Genetically determined structural abnormalities in the lipid binding domain(s) of apoH can affect its ability to bind lipid and consequently the production of the autoantibodies. In this study we have identified two common...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Amino Acid Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Binding

Share to Protein Conformation

Source

Identifiers

PMID: 9063752
DOI: 10.1093/hmg/6.2.311

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of structural mutations in the fifth domain of apolipoprotein H (beta 2-glycoprotein I) which affect phospholipid binding.PMID 9063752Read ↗

Genetics of apolipoprotein H (beta2-glycoprotein I) and anionic phospholipid binding.Semantic proximity Read ↗

A hydrophobic sequence at position 313-316 (Leu-Ala-Phe-Trp) in the fifth domain of apolipoprotein H (beta2-glycoprotein I) is crucial for cardiolipin binding.Semantic proximity Read ↗

Molecular basis of the apolipoprotein H (beta 2-glycoprotein I) protein polymorphism.Semantic proximity Read ↗

Polymorphisms beta2-glycoprotein I: phospholipid binding and multimeric structure.Semantic proximity Read ↗

Primary antiphospholipid antibody syndrome with mutations in the phospholipid binding domain of beta(2)-glycoprotein I.Semantic proximity Read ↗

<i>GPIHBP1</i> Missense Mutations Often Cause Multimerization of GPIHBP1 and Thereby Prevent Lipoprotein Lipase BindingSemantic proximity Read ↗

Genetic variation in apolipoprotein H (beta2-glycoprotein I) affects the occurrence of antiphospholipid antibodies and apolipoprotein H concentrations in systemic lupus erythematosus.Semantic proximity Read ↗

Apolipoprotein A-V N-terminal domain lipid interaction properties in vitro explain the hypertriglyceridemic phenotype associated with natural truncation mutants.Semantic proximity Read ↗

Chimpanzee apolipoprotein H (beta2-glycoprotein I): report on the gene structure, a common polymorphism, and a high prevalence of antiphospholipid antibodies.Semantic proximity Read ↗

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

Deletion of amino acids Glu146-->Arg160 in human apolipoprotein A-I (ApoA-ISeattle) alters lecithin:cholesterol acyltransferase activity and recruitment of cell phospholipid.Semantic proximity Read ↗

Heparin inhibits the binding of beta 2-glycoprotein I to phospholipids and promotes the plasmin-mediated inactivation of this blood protein. Elucidation of the consequences of the two biological events in patients with the anti-phospholipid syndrome.Semantic proximity Read ↗

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