@misc{oai:repo.qst.go.jp:00072460,
 author = {松尾, 龍人 and 松尾龍人 and 河野, 史明 and 藤原, 悟 and 松尾 龍人 and 河野 史明 and 藤原 悟},
 month = {Sep},
 note = {In order to investigate the effects of a cardiomyopathy-causing mutation E244D of troponin (Tn) T on the structure of thin filaments, small-angle x-ray scattering measurements were carried out on bovine cardiac thin filaments, in which the endogenous Tn was exchanged with human cardiac Tn containing the wild-type (WT) or E244D mutant (MT) of TnT, in the –Ca2+ and +Ca2+ states. Analysis by model calculation shows that while there are no structural differences between the WT and MT in the –Ca2+ state, tropomyosin (Tm) of the MT moves closer to the fiber axis than that of the WT in the +Ca2+ state. Since Tm directly controls myosin binding, this change would modulate the force production process, leading to functional aberration reported for the E244D mutation., 第55回日本生物物理学会年会},
 title = {Effects of E244D mutation of cardiac troponin T on the structure of thin filaments by small-angle x-ray scattering},
 year = {2017}
}