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Masasuke Yoshida
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Articles

Functional analysis of membranous F o - a subunit of F 1 F o -ATP synthase by in vitro protein synthesis

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Yutetsu Kuruma, Toshiharu Suzuki, Sakurako Ono, Masasuke Yoshida, Takuya Ueda
Journal: Biochemical Journal
Biochem J (2012) 442 (3): 631–638.
https://doi.org/10.1042/BJ20111284
Published: 24 February 2012
View articletitled, Functional analysis of membranous F o - a subunit of F 1 F o -ATP synthase by in vitro protein synthesis
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Articles

Essential arginine residue of the F o - a subunit in F o F 1 -ATP synthase has a role to prevent the proton shortcut without c -ring rotation in the F o proton channel

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Noriyo Mitome, Sakurako Ono, Hiroki Sato, Toshiharu Suzuki, Nobuhito Sone, Masasuke Yoshida
Journal: Biochemical Journal
Biochem J (2010) 430 (1): 171–177.
https://doi.org/10.1042/BJ20100621
Published: 28 July 2010
View articletitled, Essential arginine residue of the F o - a subunit in F o F 1 -ATP synthase has a role to prevent the proton shortcut without c -ring rotation in the F o proton channel
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Articles

Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity

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Yo-hei Watanabe, Yosuke Nakazaki, Ryoji Suno, Masasuke Yoshida
Journal: Biochemical Journal
Biochem J (2009) 421 (1): 71–77.
https://doi.org/10.1042/BJ20082238
Published: 12 June 2009
View articletitled, Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity
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Articles

α3β3γ complex of F1-ATPase from thermophilic Bacillus PS3 can maintain steady-state ATP hydrolysis activity depending on the number of non-catalytic sites

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Toyoki AMANO, Tadashi MATSUI, Eiro MUNEYUKI, Hiroyuki NOJI, Kiyotaka HARA, Masasuke YOSHIDA, Toru HISABORI
Journal: Biochemical Journal
Biochem J (1999) 343 (1): 135–138.
https://doi.org/10.1042/bj3430135
Published: 24 September 1999
View articletitled, α3β3γ complex of F1-ATPase from thermophilic Bacillus PS3 can maintain steady-state ATP hydrolysis activity depending on the number of non-catalytic sites
Open the PDF for α3β3γ complex of F1-ATPase from thermophilic Bacillus PS3 can maintain steady-state ATP hydrolysis activity depending on the number of non-catalytic sites in another window