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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Serpin peptidase inhibitor, clade C

antithrombin III, AT III
The protein encoded by this gene is a plasma protease inhibitor and a member of the serpin superfamily. This protein inhibits thrombin as well as other activated serine proteases of the coagulation system, and it regulates the blood coagulation cascade. The protein includes two functional domains: the heparin binding-domain at the N-terminus of the mature protein, and the reactive site domain at the C-terminus. The inhibitory activity is enhanced by the presence of heparin. More than 120 mutations have been identified for this gene, many of which are known to cause antithrombin-III deficiency. [provided by RefSeq, Jul 2009] (from NCBI)
Papers on antithrombin III
Amelioration of the severity of heparin-binding antithrombin mutations by posttranslational mosaicism.
Corral et al., Murcia, Spain. In Blood, 2012
Heparin-binding antithrombin mutations are associated with thrombosis.
Molecular basis of type I antithrombin deficiency in two women with recurrent venous thromboembolism in the first trimester of pregnancy.
Wang et al., Shanghai, China. In Blood Cells Mol Dis, 2012
results revealed that the type I AT deficiency in two patients was caused by impaired secretion of the AT-Trp225Cys and AT-Ala404Asp mutant proteins.
Molecular analysis and genotype-phenotype correlation in patients with antithrombin deficiency from Southern Italy.
Di Minno et al., Napoli, Italy. In Thromb Haemost, 2012
analysis of genotype-phenotype correlation of SERPIN C1 in patients with antithrombin deficiency from Southern Italy
Regulatory regions of SERPINC1 gene: identification of the first mutation associated with antithrombin deficiency.
Corral et al., Murcia, Spain. In Thromb Haemost, 2012
identification of the first mutation located in regulatory region, which is associated with antithrombin deficiency
The infective polymerization of conformationally unstable antithrombin mutants may play a role in the clinical severity of antithrombin deficiency.
Corral et al., Murcia, Spain. In Mol Med, 2011
Under mild heating conditions, purified antithrombin London recruited WT monomers into growing polymers, reducing the anticoagulant activity.
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