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Article

Antithrombin Padua. I: Impaired heparin binding caused by an Arg47 to his (CGT to CAT) substitution.

Thrombosis research - 15 Apr 1990

Caso R, Lane D A, Thompson E, Zangouras D, Panico M, Morris H, Olds R J, Thein S L, Girolami A

Abstract excerpt

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Share to Amino Acid Sequence
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 2349545
DOI: 10.1016/0049-3848(90)90175-c

Genes

CAT

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

Antithrombin Padua. I: Impaired heparin binding caused by an Arg47 to his (CGT to CAT) substitution.PMID 2349545Read ↗

Prothrombin Padua I: incomplete activation due to an amino acid substitution at a factor Xa cleavage site.Semantic proximity Read ↗

Antithrombin III Sudbury: an Ala384----Pro mutation with abnormal thrombin-binding activity and thrombotic diathesis.Semantic proximity Read ↗

Investigation of the Differences in Antithrombin to Heparin Binding among Antithrombin Budapest 3, Basel, and Padua Mutations by Biochemical and In Silico Methods.Semantic proximity Read ↗

Report of a novel kindred with antithrombin heparin-binding site variant (47 Arg to His): demand for an automated progressive antithrombin assay to detect molecular variants with low thrombotic risk.Semantic proximity Read ↗

Molecular and functional characterization of a natural homozygous Arg67His mutation in the prothrombin gene of a patient with a severe procoagulant defect contrasting with a mild hemorrhagic phenotype.Semantic proximity Read ↗

Antithrombin gene mutation 5356-5364*delCTT with type I deficiency and early-onset thrombophilia and a brief review of the antithrombin alpha-helix D molecular pathology.Semantic proximity Read ↗

A novel dysfunctional protein C (protein C Padua 2) associated with a thrombotic tendency: substitution of Cys for Arg-1 results in a strongly reduced affinity for binding of Ca++.Semantic proximity Read ↗

Antithrombin: structure and function.Semantic proximity Read ↗

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Antithrombin III Padua 2: a single base substitution in exon 2 detected with PCR and direct genomic sequencing.Semantic proximity Read ↗

Atypical pulmonary thromboembolism caused by the mutation site SERPINC1 of the antithrombin III gene: A case report.Semantic proximity Read ↗

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