Research Topics
| Mayumi Nakanishi-MatsuiSummaryAffiliation: Iwate Medical University Country: Japan Publications
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Detail Information
Publications
Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamicsMayumi Nakanishi-Matsui
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University, and Futai Special Laboratory, Yahaba, Iwate, Japan
IUBMB Life 65:247-54. 2013..Single Molecule Enzymology" is a new trend for understanding enzyme mechanisms in biochemistry and physiology...- Lipopolysaccharide induces multinuclear cell from RAW264.7 line with increased phagocytosis activityMayumi Nakanishi-Matsui
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University, Futai Special Laboratory, Yahaba, Iwate 028 3694, Japan
Biochem Biophys Res Commun 425:144-9. 2012..The internalized beads were located in lysosome-marker positive organelles, which were probably phagolysosomes. The LPS-induced multinuclear cell could be a good model system to study phagocytosis of large foreign bodies... - The mechanism of rotating proton pumping ATPasesMayumi Nakanishi-Matsui
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University, Yahaba, Iwate 028 3694, Japan
Biochim Biophys Acta 1797:1343-52. 2010..In this review, we focus on the mechanism of steady-state F1-ATPase rotation, which maximizes the coupling efficiency between catalysis and rotation... - Roles of the beta subunit hinge domain in ATP synthase F(1) sector: hydrophobic network formed by introduced betaPhe174 inhibits subunit rotationMayumi Nakanishi-Matsui
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University, Yahaba, Iwate 028 3694, Japan
Biochem Biophys Res Commun 395:173-7. 2010..These results indicate that the smooth conformational change of the beta subunit hinge domain is pertinent for the rotational catalysis... 
Single molecule behavior of inhibited and active states of Escherichia coli ATP synthase F1 rotationMizuki Sekiya
Department of Biochemistry, Faculty of Pharmaceutical Sciences, and Futai Special Laboratory, Iwate Medical University, Yahaba, Iwate 028 3694, Japan
J Biol Chem 285:42058-67. 2010..These results suggest that the ε subunit plays a role in guiding the enzyme through the proper and efficient catalytic and transport rotational pathway but does not influence the transition to the inhibited state...- Binding of phytopolyphenol piceatannol disrupts β/γ subunit interactions and rate-limiting step of steady-state rotational catalysis in Escherichia coli F1-ATPaseMizuki Sekiya
Department of Biochemistry, Faculty of Pharmaceutical Sciences, and Futai Special Laboratory, Iwate Medical University, Yahaba, Iwate 028 3694, Japan
J Biol Chem 287:22771-80. 2012.... 
Rotational catalysis of Escherichia coli ATP synthase F1 sector. Stochastic fluctuation and a key domain of the beta subunitMayumi Nakanishi-Matsui
Futai Special Laboratory, Microbial Chemistry Research Center, Microbial Chemistry Research Foundation, Tokyo 141 0021, Japan
J Biol Chem 282:20698-704. 2007..These results indicate that the domain between beta-sheet 4 (betaSer-174) and P-loop (betaGly-149) is important to drive rotation...- Temperature dependence of single molecule rotation of the Escherichia coli ATP synthase F1 sector reveals the importance of gamma-beta subunit interactions in the catalytic dwellMizuki Sekiya
Department of Biochemistry, Faculty of Pharmaceutical Sciences, and Futai Special Laboratory, Iwate Medical University, Yahaba, Iwate 028 3694, Japan
J Biol Chem 284:22401-10. 2009..The gammaM23K enzyme must overcome an abrupt activation energy barrier, forcing it onto a less favored pathway that results in uncoupling catalysis from rotation... - [Proton pumping ATPases: from single molecule analysis to diverse biological functions]Mayumi Nakanishi-Matsui
Faculty of Pharmaceutical Sciences, Iwate Medical University, 2-1-1 Nishi-tokuta, Yahaba, Iwate 028-3694, Japan
Seikagaku 79:512-9. 2007 - Effects of mutations in the beta subunit hinge domain on ATP synthase F1 sector rotation: interaction between Ser 174 and Ile 163Sachiko Kashiwagi
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University, Iwate 028 3694, Japan
Biochem Biophys Res Commun 365:227-31. 2008..Importance of the hinge domain [phosphate-binding loop (P-loop)/alpha-helixB/loop/beta-sheet4, betaPhe148-betaGly186] as to driving rotational catalysis is discussed... - Rotational catalysis in proton pumping ATPases: from E. coli F-ATPase to mammalian V-ATPaseMasamitsu Futai
Department of Biochemistry, Iwate Medical University, Yahaba, Iwate, Japan
Biochim Biophys Acta 1817:1711-21. 2012..This article is part of a Special Issue entitled: 17th European Bioenergetics Conference (EBEC 2012)... - Defective assembly of a hybrid vacuolar H(+)-ATPase containing the mouse testis-specific E1 isoform and yeast subunitsKazuhiro Hayashi
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University, Iwate, Japan
Biochim Biophys Acta 1777:1370-7. 2008..These results suggest that subunit E, especially its amino-terminal domain, plays a pertinent role in the assembly of V-ATPase subunits in vacuolar membranes... - Stochastic proton pumping ATPases: from single molecules to diverse physiological rolesMayumi Nakanishi-Matsui
Futai Special Laboratory, Microbial Chemistry Research Center, Microbial Chemistry Research Foundation, CREST, Japan Science, and Technology Agency, Kamiosaki, Shinagawa-ku, Tokyo, Japan
IUBMB Life 58:318-22. 2006..Emphasis is placed on the stochastic rotational catalysis of F-ATPase and isoforms of V-ATPase...