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Thromb Haemost 2002; 88(03): 533-534
DOI: 10.1055/s-0037-1613248
DOI: 10.1055/s-0037-1613248
Letters to the Editor
Low Expression of Truncated Aα Chain Variant in Circulating Fibrinogen
Further Information
Publication History
Received
11 February 2002
Accepted after revision
29 May 2002
Publication Date:
27 December 2017 (online)
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References
- 1 Ridgway H, Brennan SO, Gibbons S, George PM. Fibrinogen Lincoln: A new mutation causing α chain truncation and defective polymerisation. Br J Haematol 1996; 93: 117-84.
- 2 Brennan SO, Hammonds B, George PM. Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (Aα20 Val→Asp). J Clin Invest 1995; 96: 2854-8.
- 3 Mullin J, Gorkun O, Lord S. Decreased lateral aggregation of a variant recombinant fibrinogen provides insights into the polymerisation mechanism. Biochemistry 2000; 9843-9.
- 4 Brennan SO. Electrospray ionisation analysis of human fibrinogen. Thromb Haemost 1997; 78: 1055-8.
- 5 Fellowes AP, Brennan SO, Stromorken H, Holme R, Brosstad F, George PM. Homozygous truncation of the fibrinogen Aα chain within the coiled coil causes congenital afibrinogenaemia. Blood 2000; 96: 773-5.
- 6 Gorkun OV, Veklich YI, Medved LV, Henchen AH, Weiel JW. Role of the αC domains of fibrin in clot formation. Biochemistry 1994; 33: 6986-97.