Mutation analysis in 51 patients with haemophilia A: Report of 10 novel mutations and correlations between genotype and clinica phenotype
Hill M, Deam S, Gordon B, et al. Mutation analysis in 51 patients with haemophilia A: report of 10 novel mutations and correlations between genotype and clinica phenotype. Haemophilia 2005; 11: 133-41.
Hypofibrinogenemia in an individual with 2 coding (β82 A>G and Bβ235 PL) and 2 non-coding mutations
Brennan SO, Fellowes AP, Faed JM, et al Hypofibrinogenemia in an individual with 2 coding (β82 A>G and Bβ235 PL) and 2 non-coding mutations. Blood 2000,95:1709-13
Hypofibrinogenemia due to novel 316 Asp>Tyr substitution in the fibrinogen Bβ chain
Brennan SO, Wyatt JM, May S, et al. Hypofibrinogenemia due to novel 316 Asp>Tyr substitution in the fibrinogen Bβ chain. Thromb Haemost 2001; 85: 450-3.
Missense mutations in the human β fibrinogen gene cause congenital afibrinogenemia by impairing fibrinogen secretion
Duga S, Asselta R, Santagostino E, et al. Missense mutations in the human β fibrinogen gene cause congenital afibrinogenemia by impairing fibrinogen secretion. Blood 2000; 95: 1336-41.
Congenital afibrinogenemia: Identification and expression of a missense mutation in FGB impairing fibrinogen secretion
Vu D, Bolton-Maggs PH, Parr JR, et al. Congenital afibrinogenemia: identification and expression of a missense mutation in FGB impairing fibrinogen secretion. Blood 2003; 102: 4413-5.
Congenital afibrinogenemia: Intracellular retention of fibrinogen due to a novel W437G mutation in the fibrinogen Bβ-chain gene
Spena. S, Asselta F, Duga S, et al. Congenital afibrinogenemia: intracellular retention of fibrinogen due to a novel W437G mutation in the fibrinogen Bβ-chain gene. Biochim Biophys Acta 2003; 1639: 87-94.
2.8 A crystal structure of recombinant fibrinogen fragment D with and without two peptide ligands: GHRP binding to the 'b' site disrupts its nearby calcium-binding site
Kostelansky MS, Betts L, Gorkun OV et al. 2.8 A crystal structure of recombinant fibrinogen fragment D with and without two peptide ligands: GHRP binding to the 'b' site disrupts its nearby calcium-binding site. Biochemistry 2002; 41: 12124-32.
Calcium-binding site β2, adjacent to the 'b' polymerization site, modulates lateral aggregation of protofibrils during fibrinogen polymerization
Kostelansky MS, Louncs KC, Ping LF, et al. Calcium-binding site β2, adjacent to the 'b' polymerization site, modulates lateral aggregation of protofibrils during fibrinogen polymerization. Biochemistry 2004; 43:2475-83.