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Article

Mutations in the catalytic domain of factor IX that are related to the subclass hemophilia Bm.

Biochemistry - 29 Jun 1993

Hamaguchi N, Roberts H, Stafford D W

Abstract excerpt

Hemophilia Bm, a variant of hemophilia B, results in a marked increase in the ox brain prothrombin time. Mutations known to cause hemophilia Bm occur at residue 180, 181, or 182 near the amino terminus of the heavy chain and at residue 311, 364, 368, 390, 396, or 397 near the activation site of factor IX (Giannelli et al., 1990). In this study we replaced factor IX residues 181, 182, and 390 in separate...

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PMID: 8518277
DOI: 10.1021/bi00076a004

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Mutations in the catalytic domain of factor IX that are related to the subclass hemophilia Bm.PMID 8518277Read ↗

Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX.Semantic proximity Read ↗

A mutation adjacent to the beta cleavage site of factor IX (valine 182 to leucine) results in mild haemophilia Bm.Semantic proximity Read ↗

Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX.Semantic proximity Read ↗

Amino acid substitutions in the factor VIII coagulation protein that cause hemophilia A in man.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 ↗

Identification of a new haemophilia BM case produced by a mutation located at the carboxy terminal cleavage site of activation peptide.Semantic proximity Read ↗

Region of factor IXa protease domain that interacts with factor VIIIa: analysis of select hemophilia B mutants.Semantic 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 ↗

Surface loop 199-204 in blood coagulation factor IX is a cofactor-dependent site involved in macromolecular substrate interaction.Semantic proximity Read ↗

Cleavage at Arg-1689 influences heavy chain cleavages during thrombin-catalyzed activation of factor VIII.Semantic proximity Read ↗

Three distinct point mutations in the factor IX gene of three Japanese CRM+ hemophilia B patients (factor IX BMNagoya 2, factor IX Nagoya 3 and 4).Semantic proximity Read ↗

Residual factor VII activity and different hemorrhagic phenotypes in CRM(+) factor VII deficiencies (Gly331Ser and Gly283Ser).Semantic proximity Read ↗

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