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Literature DB >> 692730

A two-step fibrinogen--fibrin transition in blood coagulation.

B Blombäck, B Hessel, D Hogg, L Therkildsen.

Abstract

The kinetics of the thrombin-catalysed release of fibrino-peptides A and B from human fibrinogen have been investigated and a mechanism correlating the release of fibrinopeptides to fibrin formation is presented. The sequential release of fibrinopeptides results in sequential activation of two sets of polymerisation sites.

Entities: Disease Gene Species

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Year: 1978 PMID： 692730 DOI： 10.1038/275501a0

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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Cited

78 in total

1. The structure of soluble fibrin oligomers.

Authors: M A Rosenfeld; V B Leonova; M I Biryukova; M V Vasileva
Journal: Dokl Biochem Biophys Date: 2011-11-19 Impact factor: 0.788

2. Identification of covalently linked trimeric and tetrameric D domains in crosslinked fibrin.

Authors: M W Mosesson; K R Siebenlist; D L Amrani; J P DiOrio
Journal: Proc Natl Acad Sci U S A Date: 1989-02 Impact factor: 11.205

3. Studies on the basis for the properties of fibrin produced from fibrinogen-containing gamma' chains.

Authors: Kevin R Siebenlist; Michael W Mosesson; Irene Hernandez; Leslie A Bush; Enrico Di Cera; John R Shainoff; James P Di Orio; Laurie Stojanovic
Journal: Blood Date: 2005-07-07 Impact factor: 22.113

4. Polymerization of fibrin: specificity, strength, and stability of knob-hole interactions studied at the single-molecule level.

Authors: Rustem I Litvinov; Oleg V Gorkun; Scott F Owen; Henry Shuman; John W Weisel
Journal: Blood Date: 2005-07-05 Impact factor: 22.113

A two-step fibrinogen--fibrin transition in blood coagulation.

1. The structure of soluble fibrin oligomers.

2. Identification of covalently linked trimeric and tetrameric D domains in crosslinked fibrin.

3. Studies on the basis for the properties of fibrin produced from fibrinogen-containing gamma' chains.

4. Polymerization of fibrin: specificity, strength, and stability of knob-hole interactions studied at the single-molecule level.

5. Polymerization of fibrin: Direct observation and quantification of individual B:b knob-hole interactions.

6. Quantitative estimation of Serum Fibrinogen Degradation Product levels in Oral Premalignant and Malignant lesions.

7. Fibrinogen variant BbetaD432A has normal polymerization but does not bind knob "B".

8. Cleavage of blood coagulation factor XIII and fibrinogen by thrombin during in vitro clotting.

9. Fibrinogen-fibrin conversion. The mechanism of fibrin-polymer formation in solution.

10. Fibrinogen and fibrin structure and fibrin formation measured by using magnetic orientation.