Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Makoto Ushimaru"'
Autor:
Haruo Homareda, Kei Suga, Sachiko Yamamoto-Hijikata, Yoshinobu Eishi, Makoto Ushimaru, Yukichi Hara
Publikováno v:
Biochemistry and Biophysics Reports, Vol 32, Iss , Pp 101347- (2022)
The affinity for K+ of silkworm Na+/K+-ATPase, which is composed of α and β subunits, is remarkably lower than that of mammalian Na+/K+-ATPase, with a slightly higher affinity for Na+. Because the α subunit had more than 70% identity to the mammal
Externí odkaz:
https://doaj.org/article/af0a7ae88d5943a080220e7644874c64
Publikováno v:
Biochemical and Biophysical Research Communications. 614:56-62
Publikováno v:
Molecular and Cellular Neuroscience. 121:103754
The involvement of secretory pathways and Golgi dysfunction in neuronal cells during Alzheimer's disease progression is poorly understood. Our previous overexpression and knockdown studies revealed that the intracellular protein level of Syntaxin-5,
Autor:
Yoshinobu Eishi, Sayaka Ito, Yukichi Hara, Masahiro Otsu, Toshiyuki Fukutomi, Sachiko Yamamoto, Taeho Jo, Makoto Ushimaru, Haruo Homareda
Publikováno v:
Journal of Bioenergetics and Biomembranes. 49:463-472
The affinity for K+ of silkworm nerve Na+/K+-ATPase is markedly lower than that of mammalian Na+/K+-ATPase (Homareda 2010). In order to obtain clues on the molecular basis of the difference in K+ affinities, we cloned cDNAs of silkworm (Bombyx mori)
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1861:3399-3405
Background SERCA maintains intracellular Ca 2+ homeostasis by sequestering cytosolic Ca 2+ into SR/ER stores. Two primary fatty acid amides (PFAAs), oleamide (18:1 9- cis ) and linoleamide (18:2 9,12- cis ), induce an increase in intracellular Ca 2+
Autor:
Haruo, Homareda, Masahiro, Otsu, Sachiko, Yamamoto, Makoto, Ushimaru, Sayaka, Ito, Toshiyuki, Fukutomi, Taeho, Jo, Yoshinobu, Eishi, Yukichi, Hara
Publikováno v:
Journal of bioenergetics and biomembranes. 49(6)
The affinity for K
Autor:
Sachiko Yamamoto, Takashi Tachiki, Toru Kimura, Takuya Sakurai, Makoto Ushimaru, Naohiko Anzai
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 76:2230-2235
L-Theanine has favorable physiological effects in terms of human health, but the mechanisms that transport it to its target organs or cells are not completely defined. To identify the major transport mechanisms of L-theanine, we screened for candidat
Publikováno v:
Biochemical and biophysical research communications. 477(2)
To identify specific inhibitors of the human secretary pathway Ca(2+)-ATPase 2 (hSPCA2), a recombinant hSPCA2 was expressed in Saccharomyces cerevisiae, and purified by Co(2+)-chelating chromatography. The isolated hSPCA2 catalyzed ATP hydrolysis in
Publikováno v:
Biochimica et biophysica acta. General subjects. 1861(1 Pt)
SERCA maintains intracellular CaThree major SERCA isoforms, rSERCA1a, hSERCA2b, and hSERCA3a, were individually overexpressed in COS-1 cells, and the inhibitory action of PFAAs on CaThe CaLinoleamide and oleamide inhibit SERCA activity in the micromo
Autor:
Yoshihiro Fukushima, Makoto Ushimaru
Publikováno v:
Biochemical Journal. 414:357-361
To identify the functional unit of Ca2+-ATPase in the sarcoplasmic reticulum, we assessed Ca2+-transport activities occurring on sarcoplasmic reticulum membranes with different combinations of active and inactive Ca2+-ATPase molecules. We prepared he