Literature DB >> 6388985

Dysfibrinogenemia. A current perspective.

D K Galanakis.   

Abstract

At least 24 single amino acid substitution dysfibrinogens are currently known. Emerging evidence supports conclusions reached from studies on normal fibrinogen, which relate to the importance of release of A peptides to formation of a physiologically adequate fibrin clot; the existence of "D-D" or (b-b) polymerization sites; and the importance of the gamma chain carboxy terminal segment in fibrin assembly.

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Year:  1984        PMID: 6388985

Source DB:  PubMed          Journal:  Clin Lab Med        ISSN: 0272-2712            Impact factor:   1.935


  2 in total

1.  Fibrinogen Stony Brook, a heterozygous A alpha 16Arg----Cys dysfibrinogenemia. Evaluation of diminished platelet aggregation support and of enhanced inhibition of fibrin assembly.

Authors:  D K Galanakis; A Henschen; E I Peerschke; M Kehl
Journal:  J Clin Invest       Date:  1989-07       Impact factor: 14.808

2.  A novel mutation in exon 2 of FGB caused by c.221G>T substitution, predicting the replacement of the native Arginine at position 74 with a Leucine (p.Arg74Leu ) in a proband from a Kurdish family with dysfibrinogenaemia and familial venous and arterial thrombosis.

Authors:  Abdul A Shlebak; Alexia D Katsarou; George Adams; Fiona Fernando
Journal:  J Thromb Thrombolysis       Date:  2017-02       Impact factor: 2.300

  2 in total

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