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

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.

European journal of biochemistry - 1 Mar 2000

Mehdi H, Naqvi A, Kamboh M I

Abstract excerpt

Apolipoprotein H (apoH, protein; APOH, gene) binds to negatively charged phospholipids, which triggers the production of a subset of autoantibodies against phospholipid in patients with autoimmune diseases. We have demonstrated that two naturally occurring missense mutations in the fifth domain of apoH, Trp316Ser and Cys306Gly, disrupt the binding of native apoH to phosphatidylserine [Sanghera, D. K.,...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Anticardiolipin
Share to beta 2-Glycoprotein I

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

Share to Cardiolipins

Share to Chemical Phenomena

Share to Chemistry, Physical

Share to Chlorocebus aethiops

Share to Glycoproteins

Share to Phosphatidylserines

Source

Identifiers

PMID: 10712609
DOI: 10.1046/j.1432-1327.2000.01174.x

Genes

APOH

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

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.PMID 10712609Read ↗

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

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

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

The carboxyl-terminal segment of apolipoprotein A-V undergoes a lipid-induced conformational change.Semantic proximity Read ↗

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

Genetic analysis of the fluorescein isothiocyanate binding site of the yeast plasma membrane H(+)-ATPase.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 ↗

Correlation between β2-glycoprotein I valine/leucine247 polymorphism and anti-β2-glycoprotein I antibodies in patients with primary antiphospholipid syndromeSemantic 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 ↗

Heterogeneity of the apolipoprotein H*3 allele and its role in affecting the binding of apolipoprotein H (beta 2-glycoprotein I) to anionic phospholipids.Semantic proximity Read ↗

Human apolipoprotein E7:lysine mutations in the carboxy-terminal domain are directly responsible for preferential binding to very low density lipoproteins.Semantic proximity Read ↗

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