Multiple and Distinct Effects of Mutations of Tyr122, Glu123, Arg324, and Arg334 Involved in Interactions between the Top Part of Second and Fourth Transmembrane Helices in Sarcoplasmic Reticulum Ca2+-ATPase: CHANGES IN CYTOPLASMIC DOMAIN ORGANIZATION ・・・. Journal of Biological Chemistry. 2004. in press
Only half of the Ca<sup>2+</sup>-ATPase molecules present in sarcoplasmic reticulum vesicles can be phosphorylated with ATP or inorganic phosphate(jointly worked)
"Na/K-ATPase and Related ATPases"Elsevier Science B.V.(Netherland) 2000
Deletion on specific substitutions of a few residues in the NH<sub>2</sub>-terminal Ala3-Thr9 region of sarcoplasmic reticulum Ca<sup>2+</sup>-ATPase cause inactivation and rapid degradation of the enzyme expressed in COS-1 cells(jointly worked)
"Na/K-ATPase and Related ATPases"Elsevier Science B.V.(Netherland) 2000