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

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

Biochemistry - 4 Jun 2013

Wakabayashi Hironao, Fay Philip J

Abstract excerpt

Factor (F)VIII consists of a heavy chain [A1(a1)A2(a2)B domains] and a light chain [(a3)A3C1C2 domains]. Several reports have shown significant changes in FVIII stability and/or activity following selected mutations at the A1-A2, A1-A3, A2-A3, and A1-C2 domain interfaces. In this study, the remaining inter-FVIII subunit interfaces (A3-C1 and C1-C2) were examined for their contributions to the stability and...

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 Disulfides
Share to Factor VIII

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Factor X

Share to Hydrophobic and Hydrophilic Interactions

Share to Kinetics

Share to Protein Stability

Share to Static Electricity

Source

Open in PubMed Open full text

Identifiers

PMID: 23659383
DOI: 10.1021/bi400295x
PMCID: PMC3731059

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

Modification of interdomain interfaces within the A3C1C2 subunit of factor VIII affects its stability and activity.PMID 23659383Read ↗

Stabilizing interactions between D666-S1787 and T657-Y1792 at the A2-A3 interface support factor VIIIa stability in the blood clotting pathway.Semantic proximity Read ↗

Increasing hydrophobicity or disulfide bridging at the factor VIII A1 and C2 domain interface enhances procofactor stability.Semantic proximity Read ↗

Combining mutations that modulate inter-subunit interactions and proteolytic inactivation enhance the stability of factor VIIIa.Semantic proximity Read ↗

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

Intrinsic stability and functional properties of disulfide bond-stabilized coagulation factor VIIIa variants.Semantic proximity Read ↗

Identification of amino acid residues that are crucial for FXIII-A intersubunit interactions and stability.Semantic proximity Read ↗

Identification of residues in the 558-loop of factor VIIIa A2 subunit that interact with factor IXa.Semantic proximity Read ↗

Computational analysis of Asp519 and Glu665 mutations of coagulation factor FVIIIa: Implications for enhanced binding affinity of A2-domain.Semantic proximity Read ↗

Cofactor activity in factor VIIIa of the blood clotting pathway is stabilized by an interdomain bond between His281 and Ser524 formed in factor VIII.Semantic proximity Read ↗

Functional mapping of the A2 domain from human factor VIII.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 ↗

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