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Article

Molecular bases of CRM+ factor X deficiency: a frequent mutation (Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain.

British journal of haematology - 1 Aug 1995

Marchetti G, Castaman G, Pinotti M, Lunghi B, Di Iasio M G, Ruggieri M, Rodeghiero F, Bernardi F

Abstract excerpt

The presence of gene lesions in coagulation factor X (FX, Stuart factor) was investigated in asymptomatic subjects with FX deficiency characterized by the presence of dysfunctional molecules in plasma, as demonstrated by the discrepancy between clotting activity and antigen level. A missense mutation (Ser334Pro) in the catalytic domain was found in three unrelated families in both the homozygous and the...

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Identifiers

PMID: 7669671
DOI: 10.1111/j.1365-2141.1995.tb05214.x

Genes

EGF

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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.

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Molecular bases of CRM+ factor X deficiency: a frequent mutation (Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain.PMID 7669671Read ↗

A new factor X defect (factor X Padua 3): a compound heterozygous between true deficiency (Gly(380)-->Arg) and an abnormality (Ser(334)-->Pro).Semantic proximity Read ↗

Gene mutations and three-dimensional structural analysis in 13 families with severe factor X deficiency.Semantic proximity Read ↗

Impaired prothrombinase activity of factor X Gly381Asp results in severe familial CRM+ FX deficiency.Semantic proximity Read ↗

A recurrent Gly43Asp substitution in coagulation Factor X rigidifies its catalytic pocket and impairs catalytic activity and intracellular trafficking.Semantic proximity Read ↗

A novel type I factor X variant (factor X Cys350Phe) due to loss of a disulfide bond in the catalytic domain.Semantic proximity Read ↗

Factor X Nagoya 1 and Nagoya 2: a CRM- factor X deficiency and a dysfunctional CRM+ factor X deficiency characterized by substitution of Arg306 by Cys and of Gly366 by Ser, respectively.Semantic proximity Read ↗

Molecular defects in CRM+ factor VII deficiencies: modelling of missense mutations in the catalytic domain of FVII.Semantic proximity Read ↗

A dysfunctional factor X (factor X San Giovanni Rotondo) present at homozygous and double heterozygous level: identification of a novel microdeletion (delC556) and missense mutation (Lys(408)-->Asn) in the factor X gene. A study of an Italian family.Semantic proximity Read ↗

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

The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys).Semantic proximity Read ↗

A family with factor X deficiency from Argentina: a compound heterozygosis because of the combination of a new mutation (Gln138Arg) with an already known one (Glu350Lys).Semantic proximity Read ↗

Persistent validity of a classification of congenital factor X defects based on clotting, chromogenic and immunological assays even in the molecular biology era.Semantic proximity Read ↗

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