Simultaneous measurements of dynamic modulus and turbidity and effects of calcium ions on the process of thrombin-induced fibrin gel formation
Author:
Affiliation:
1. Faculty of Agriculture, Takasaki University of Health and Welfare
2. Graduate School of Science and Technology, Gunma University
Publisher
Japanese Society of Biorheology
Subject
Mechanical Engineering,Mechanics of Materials,General Materials Science
Link
https://www.jstage.jst.go.jp/article/jbr/34/2/34_71/_pdf
Reference21 articles.
1. 1. Weisel JW, Litvinov IR. Mechanisms of fibrin polymerization and clinical implication. Blood. 2013; 121: 1712–9.
2. 2. Kostelansky SM, Lounes CK, Ping FLi, Dickerson KS, Gorkun VO, Lord TS. Probing the γ2 calcium-binding site: Studies with γD298, 301A fibrinogen reveal changes in the γ294–301 loop that alter the integrity of the “a” polymerization site. Biochemistry. 2004; 43: 2475–83.
3. 3. Kostelansky SM, Lounes CK, Ping FLi, Dickerson KS, GorkunVO, Lord TS. Calcium-binding site β2, adjacent to the “b” polymerization site, modulates lateral aggregation of protofibrils during fibrin polymerization. Biochemistry. 2007; 46: 5114–23.
4. 4. Lounes CK, Ping L, Gorkun VO, Lord TS. Analysis of engineered fibrinogen variants suggests that an additional site mediates platelet aggregation and that “B-b” interactions have a role in protofibril formation. Biochemistry. 2002; 41: 5291–9.
5. 5. Averett EL, Akhremitchev BB, Schoenfisch HM, Gorkun VO. Calcium dependence of fibrin nanomechanics: the γ1 calcium mediates the unfolding of fibrinogen induced by force applied to the “A-a” bond. Lngmuir. 2010; 26: 14716–22.
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