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The structure-function relationship of hereditary dysfibrinogens.

M Matsuda
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Abstract

Fibrinogen is a 340-kDa multi-subunit glycoprotein present in plasma and tissues of all classes of vertebrates. Fibrinogen exerts a variety of physiologically important functions, and most of them, if not all, are assigned to certain structures of fibrin including double-stranded fibrin protofibrils and highly crosslinked fibrin networks. Fibrin formation is indeed a series of highly ordered molecular interactions. The mechanisms underlying these molecular interactions have been extensively studied in the last 40 years, but there still remain many enigmas. In this mini-review, the structure-function relationships of hereditary dysfibrinogens are discussed.

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AfibrinogenemiaFibrinFibrinogenFibrinogens, AbnormalHumansPolymersProtein BindingStructure-Activity RelationshipJournal ArticleResearch Support, Non-U.S. Gov'tReview

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BibTeXRIS

M Matsuda. 1996. The structure-function relationship of hereditary dysfibrinogens.. https://doi.org/10.1016/0925-5710(96)00482-3

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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↗
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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↗