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

Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation: evidence for nonproteolytic inactivation of factor VIIIa in vivo.

Blood - 1 Jan 1999

Pipe S W, Eickhorst A N, McKinley S H, Saenko E L, Kaufman R J

Abstract excerpt

Approximately 5% of hemophilia A patients have normal amounts of a dysfunctional factor VIII (FVIII) protein and are termed cross-reacting material (CRM)-positive. FVIII is a heterodimer (domain structure A1-A2-B/A3-C1-C2) that requires thrombin cleavage to elicit procoagulant activity. Thrombin-activated FVIII is a heterotrimer with the A2 subunit (amino acid residues 373 to 740) in a weak ionic interaction with...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Arginine

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

Share to COS Cells

Share to Hydrolysis

Share to Mutagenesis, Site-Directed

Share to Phenotype

Share to Protein Binding

Share to Recombinant Proteins

Source

Identifiers

PMID: 9864159

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

Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation: evidence for nonproteolytic inactivation of factor VIIIa in vivo.PMID 9864159Read ↗

Hemophilia A mutations associated with 1-stage/2-stage activity discrepancy disrupt protein-protein interactions within the triplicated A domains of thrombin-activated factor VIIIa.Semantic proximity Read ↗

The molecular basis for cross-reacting material-positive hemophilia A due to missense mutations within the A2-domain of factor VIII.Semantic proximity Read ↗

Substitution of Arg527 and Arg531 in factor VIII associated with mild haemophilia A: characterization in terms of subunit interaction and cofactor function.Semantic proximity Read ↗

Purification and characterization of factor VIII 372-Cys: a hypofunctional cofactor from a patient with moderately severe hemophilia A.Semantic proximity Read ↗

Hemophilia A mutations within the factor VIII A2-A3 subunit interface destabilize factor VIIIa and cause one-stage/two-stage activity discrepancy.Semantic proximity Read ↗

Stable recombinant expression and characterization of the two haemophilic factor VIII variants C329S (CRM(-)) and G1948D (CRM(r)).Semantic proximity Read ↗

Identification of residues contributing to A2 domain-dependent structural stability in factor VIII and factor VIIIa.Semantic proximity Read ↗

Mutations associated with hemophilia A in the 558-565 loop of the factor VIIIa A2 subunit alter the catalytic activity of the factor Xase complex.Semantic proximity Read ↗

Mild hemophilia A patient with novel Pro1809Leu mutation develops an anti-C2 antibody inhibiting allogeneic but not autologous factor VIII activity.Semantic proximity Read ↗

Modification of interdomain interfaces within the A3C1C2 subunit of factor VIII affects its stability and activity.Semantic proximity Read ↗

Partial reconstitution of factor VIII activity from a mild Crm+ hemophilia A patient by replacement of the defective A2 domain.Semantic proximity Read ↗

Enhanced factor VIIIa stability of A2 domain interface variants results from an increased apparent affinity for the A2 subunit. Results from an increased apparent affinity for the A2 subunit.Semantic proximity Read ↗

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