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 combination of Asp519Val/Glu665Val and Lys1813Ala mutations in FVIII markedly increases coagulation potential.

Blood advances - 13 Aug 2024

Nakajima Yuto, Oda Akihisa, Baatartsogt Nemekhbayar, Kashiwakura Yuji, Ohmori Tsukasa, Nogami Keiji

Abstract excerpt

ABSTRACT: A2 domain dissociation in activated factor VIII (FVIIIa) results in reduced activity. Previous studies demonstrated that some FVIII mutants (D519V/E665V and K1813A) with delayed A2 dissociation enhanced coagulation potential. We speculated, therefore, that FVIII encompassing a combination of these mutations might further enhance coagulant activity. The aim was to assess the D519V/E665V/K1813A-FVIII...

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 Blood Coagulation

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

Share to Cell Line

Share to Cricetinae

Share to Disease Models, Animal

Share to Factor VIII

Share to Hemophilia A

Share to Thrombin

Source

Open in PubMed Open full text

Identifiers

PMID: 38820442
DOI: 10.1182/bloodadvances.2023012391
PMCID: PMC11321387

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 combination of Asp519Val/Glu665Val and Lys1813Ala mutations in FVIII markedly increases coagulation potential.PMID 38820442Read ↗

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

Disulfide bond-stabilized factor VIII has prolonged factor VIIIa activity and improved potency in whole blood clotting assays.Semantic proximity Read ↗

The mild phenotype in severe hemophilia A with Arg1781His mutation is associated with enhanced binding affinity of factor VIII for factor X.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 ↗

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 ↗

Effects of replacement of factor VIII amino acids Asp519 and Glu665 with Val on plasma survival and efficacy in vivo.Semantic proximity Read ↗

Coagulation factor VIII: biological basis of emerging hemophilia A therapiesSemantic proximity Read ↗

The factor (F)VIII K1693N mutation (FVIII-Nara) in a patient with moderate hemophilia A confers resistance to thrombin-catalyzed cleavage at Arg1689 involving P4' position.Semantic proximity Read ↗

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

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

Effect of F8 B domain gene variants on synthesis, secretion, activity and stability of factor VIII protein.Semantic proximity Read ↗

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