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Volumn 43, Issue 9, 2004, Pages 2533-2540

The Ionic Track in the F1-ATPase from the Thermophilic Bacillus PS3

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; COPPER COMPOUNDS; CROSSLINKING; HYDROLYSIS; MUTAGENESIS;

EID: 1542297711     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036058i     Document Type: Article
Times cited : (10)

References (26)
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    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps. Cell 93, 1117-1124.
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    • A dynamic analysis of the rotation mechanism for conformational change in F(1)-ATPase
    • Ma, J., Flynn, T. C., Cui, Q., Leslie, A. G. W., Walker, J. E., and Karplus, M. (2002) A dynamic analysis of the rotation mechanism for conformational change in F(1)-ATPase. Structure 10, 921-931.
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  • 11
    • 0037015829 scopus 로고    scopus 로고
    • 1-ATPase from the thermophilic Bacillus PS3 affects catalytic cooperativity by destabilizing the closed conformation of the catalytic site
    • 1-ATPase from the thermophilic Bacillus PS3 affects catalytic cooperativity by destabilizing the closed conformation of the catalytic site. Biochemistry 41, 14421-14429.
    • (2002) Biochemistry , vol.41 , pp. 14421-14429
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    • Bradford, M.M.1
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    • i by beef heart mitochondrial adenosine triphosphatase
    • i by beef heart mitochondrial adenosine triphosphatase. J. Biol. Chem. 252, 2891-2899.
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  • 17
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    • 1-ATPase from the thermophilic Bacillus PS3 has altered ATPase activity after cross-linking α and β subunits at noncatalytic site interfaces
    • 1-ATPase from the thermophilic Bacillus PS3 has altered ATPase activity after cross-linking α and β subunits at noncatalytic site interfaces. Biochemistry 41, 3226-3234.
    • (2002) Biochemistry , vol.41 , pp. 3226-3234
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.