Factor IX Fukuoka. Substitution of ASN92 by His in the second epidermal growth factor-like domain results in defective interaction with factors VIIa/X.

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

Back to search

Article

Factor IX Fukuoka. Substitution of ASN92 by His in the second epidermal growth factor-like domain results in defective interaction with factors VIIa/X.

The Journal of biological chemistry - 15 Nov 1993

Nishimura H, Takeya H, Miyata T, Suehiro K, Okamura T, Niho Y, Iwanaga S

Abstract excerpt

Hemophilia B Fukuoka, a moderately severe bleeding disorder, is a naturally occurring mutant of factor IX. Plasma from our patient had 3% clotting activity even though 64% of factor IX antigen was present. The purified mutant protein was cleaved normally by factor Xla, factor VIIa-tissue factor complex, or RVV-X (factor X-activating enzyme from Russell's viper venom), yielding a two-chain factor IXa. Amino acid...

Topics

Adult
Asparagine
Benzamidines
Blood Coagulation Factors
Epidermal Growth Factor
Esterases
Factor IX
Factor VIIa
Factor X
Hemophilia B
Histidine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Humans

Hydrolysis

Kinetics

Male

Mutation

Peptide Mapping

Source

Open in PubMed

Identifiers

PMID: 8226948

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8226948-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Factor IX Fukuoka. Substitution of ASN92 by His in the second epidermal growth factor-like domain results in defective interaction with factors VIIa/X.PMID 8226948Read ↗

Factor IX Bm Kiryu: a Val-313-to-Asp substitution in the catalytic domain results in loss of function due to a conformational change of the surface loop: evidence obtained by chimaeric modelling.Semantic proximity Read ↗

Identification of residues Asn89, Ile90, and Val107 of the factor IXa second epidermal growth factor domain that are essential for the assembly of the factor X-activating complex on activated platelets.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 ↗

Protease and EGF1 domains of factor IXa play distinct roles in binding to factor VIIIa. Importance of helix 330 (helix 162 in chymotrypsin) of protease domain of factor IXa in its interaction with factor VIIIa.Semantic proximity Read ↗

Factor IX Amagasaki: a new mutation in the catalytic domain resulting in the loss of both coagulant and esterase activities.Semantic proximity Read ↗

Factor IXHollywood: substitution of Pro55 by Ala in the first epidermal growth factor-like domain.Semantic proximity Read ↗

The role of β-barrels 1 and 2 in the enzymatic activity of factor XIII A-subunit.Semantic proximity Read ↗

Identification of a Putative Binding Site for Negatively Charged Surfaces in the Fibronectin Type II Domain of Human Factor XIISemantic proximity Read ↗

The distinct roles that Gln-192 and Glu-217 of factor IX play in selectivity for macromolecular substrates and inhibitors.Semantic proximity Read ↗

Contribution of residue 192 in factor Xa to enzyme specificity and function.Semantic proximity Read ↗

Factor XII Osaka: abnormal factor XII with partially defective prekallikrein cleavage activity.Semantic proximity Read ↗

Analysis of the factor XI variant Arg184Gly suggests a structural basis for factor IX binding to factor XIa.Semantic proximity Read ↗

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