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Fumiko Terasawa
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Analysis of fibrinogen variants at γ387Ile shows that the side chain of γ387 and the tertiary structure of the γC-terminal tail are important not only for assembly and secretion of fibrinogen but also for lateral aggregation of protofibrils and XIIIa-catalyzed γ-γ dimer formation

Satomi Kani, Fumiko Terasawa, Kazuyoshi Yamauchi, Minoru Tozuka, Nobuo Okumura
Journal: Blood
Blood (2006) 108 (6): 1887–1894.
https://doi.org/10.1182/blood-2006-04-016485
Published: 2006
Includes: Supplemental data
Journal Articles

Substitution of the γ-chain Asn308 disturbs the D:D interface affecting fibrin polymerization, fibrinopeptide B release, and FXIIIa-catalyzed cross-linking

Nobuo Okumura, Oleg V. Gorkun, Fumiko Terasawa, Susan T. Lord
Journal: Blood
Blood (2004) 103 (11): 4157–4163.
https://doi.org/10.1182/blood-2003-12-4296
Published: 2004
Journal Articles

Analysis of fibrinogen γ-chain truncations shows the C-terminus, particularly γIle387, is essential for assembly and secretion of this multichain protein

Nobuo Okumura, Fumiko Terasawa, Hitoshi Tanaka, Masako Hirota, Hiroyoshi Ota, Kiyoshi Kitano, Kendo Kiyosawa, Susan T. Lord
Journal: Blood
Blood (2002) 99 (10): 3654–3660.
https://doi.org/10.1182/blood.V99.10.3654
Published: 2002
Journal Articles

Hypofibrinogenemia Associated With a Heterozygous Missense Mutation γ153Cys to Arg (Matsumoto IV): In Vitro Expression Demonstrates Defective Secretion of the Variant Fibrinogen

Fumiko Terasawa, Nobuo Okumura, Kiyoshi Kitano, Nobuaki Hayashida, Makoto Shimosaka, Mitsuo Okazaki, Susan T. Lord
Journal: Blood
Blood (1999) 94 (12): 4122–4131.
https://doi.org/10.1182/blood.V94.12.4122
Published: 1999