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PubMed · 12188894

Structural alterations in hereditary dysfibrinogens.

Teruko Sugo·Yoichi Sakata·Michio Matsuda
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Abstract

Dysfibrinogens can be grossly divided in two groups: (1) defective thrombin-catalyzed conversion of fibrinogen molecules to fibrin monomers, and (2) defective fibrin polymerization due to structural alterations in polymerization sites, that include "A" and "a" sites, end-to-end D:D abutment surfaces, and lateral association sites involving the carboxyl terminal region of the fibrin alpha-chain. Recently, a number of mutations in the fibrinogen genes have been identified, and many of these encode changes that occur in regions of fibrinogen that have been elucidated by high-resolution structural studies. Here we focus on the structure-function relationships of fibrinogen that can be inferred from studies involving these abnormal molecules.

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AfibrinogenemiaCalciumFibrinogens, AbnormalGenetic Diseases, InbornHumansModels, MolecularProtein ConformationStructure-Activity RelationshipJournal ArticleResearch Support, Non-U.S. Gov'tReview

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Teruko Sugo, Yoichi Sakata, Michio Matsuda. 2002. Structural alterations in hereditary dysfibrinogens.. https://doi.org/10.2174/1389203023380648

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In vitro fibrin clot formation and fibrinolysis using heterozygous plasma fibrinogen from gammaAsn319, Asp320 deletion dysfibrinogen, Otsu I.

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Afibrinogenemia↗
PubMed2006

Fibrinogen Guarenas, an abnormal fibrinogen with an Aalpha-chain truncation due to a nonsense mutation at Aalpha 467 Glu (GAA)-->stop (TAA).

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Afibrinogenemia↗