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Volumn 35, Issue , 2000, Pages 3-18

F1-ATPase: A highly efficient rotary ATP machine

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; MOLECULAR MOTOR; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 0034351409     PISSN: 00711365     EISSN: None     Source Type: Journal    
DOI: 10.1042/bse0350003     Document Type: Article
Times cited : (40)

References (21)
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  • 2
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    • (Selman, B.R. & Selman-Reimer, S., eds.), Elsevier, Amsterdam
    • Boyer, P.D. & Kohlbrenner, W.E. (1981) The present status of the binding-change mechanism and its relation to ATP formation by chloroplasts, in Energy Coupling in Photosynthesis (Selman, B.R. & Selman-Reimer, S., eds.), pp. 231-240, Elsevier, Amsterdam
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  • 6
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  • 9
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    • The binding change mechanism for ATP synthase - Some probabilities and possibilities
    • Boyer, P.D. (1993) The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140, 215-250
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 10
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    • Hunt, A.J.1    Gittes, F.2    Howard, J.3
  • 13
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    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps. Cell 93, 1117-1124
    • (1998) Cell , vol.93 , pp. 1117-1124
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  • 17
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.