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

The orientation of beta2GPI on the plate is important for the binding of anti-beta2GPI autoantibodies by ELISA.

Journal of autoimmunity - 1 Jun 2002

Iverson G Michael, Matsuura Eiji, Victoria Edward J, Cockerill Keith A, Linnik Matthew D

Abstract excerpt

(Beta2-glycoprotein I (beta2GPI) is a plasma protein that plays an important role in the antigenic specificity of antiphospholipid autoantibodies (aPL). These antibodies are associated with an increased risk for thrombosis and recurrent foetal loss in humans. Crystallographic analysis of beta2GPI showed that its five complement control protein (CCP) or 'sushi' domains are arranged in an elongated, fish-hook...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Monoclonal
Share to Antibody Specificity

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

Share to Antiphospholipid Syndrome

Share to Autoantibodies

Share to beta 2-Glycoprotein I

Share to Enzyme-Linked Immunosorbent Assay

Share to Epitope Mapping

Share to Glycoproteins

Source

Identifiers

PMID: 12144810
DOI: 10.1006/jaut.2002.0590

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

The orientation of beta2GPI on the plate is important for the binding of anti-beta2GPI autoantibodies by ELISA.PMID 12144810Read ↗

The Significance of Antibodies against Domain I of Beta-2 Glycoprotein I in Antiphospholipid SyndromeSemantic proximity Read ↗

Autoantibodies Directed Against Domain I of Beta2-Glycoprotein ISemantic proximity Read ↗

β2-Glycoprotein I/HLA class II complexes are novel autoantigens in antiphospholipid syndromeSemantic proximity Read ↗

T cells that are autoreactive to beta2-glycoprotein I in patients with antiphospholipid syndrome and healthy individuals.Semantic proximity Read ↗

Use of Single Point Mutations in Domain I of β2-Glycoprotein I to Determine Fine Antigenic Specificity of Antiphospholipid AutoantibodiesSemantic proximity Read ↗

Selective blockade of glycoprotein VI clustering on collagen helices.Semantic proximity Read ↗

Interaction of beta2-glycoprotein I with members of the low density lipoprotein receptor family.Semantic proximity Read ↗

Binding of antiphospholipid antibodies to discontinuous epitopes on domain I of human beta(2)-glycoprotein I: mutation studies including residues R39 to R43.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 ↗

Preference for IgG mAb binding insulin in solution or on surfaces is related to immunoglobulin variable region structures.Semantic proximity Read ↗

Threonine-145/methionine-145 variants of baculovirus produced recombinant ligand binding domain of GPIbalpha express HPA-2 epitopes and show equal binding of von Willebrand factor.Semantic proximity Read ↗

Identification of the Fc gamma receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies.Semantic proximity Read ↗

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