Analysis of fibrinogen variants at gamma 387Ile shows that the side chain of gamma 387 and the tertiary structure of the gamma C-terminal tail are important not only for assembly and secretion of fibrinogen but also for lateral aggregation of protofibrils and XIIIa-catalyzed gamma-gamma dimer formation

Abstract

This research was originally published in Blood. Author(s).Kani, S; Terasawa, F; Yamauchi, K; Tozuka, M; Okumura, N. Title. Blood. 2006;108:1887-1894. © by the American Society of Hematology.ArticleBLOOD. 108(6): 1887-1894 (2006)journal articl