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Volumn 9, Issue 1, 2008, Pages 84-90

Temperature-sensitive reaction intermediate of F1-ATPase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; PHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 37849051356     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7401135     Document Type: Article
Times cited : (46)

References (21)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams JP, Leslie AG, Lutter R, Walker JE (1994) Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370: 621-628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 3
    • 0031027579 scopus 로고    scopus 로고
    • 1 ATP synthase are dependent on the energy of interaction between γ and β subunits
    • 1 ATP synthase are dependent on the energy of interaction between γ and β subunits. J Biol Chem 272: 2300-2306
    • (1997) J Biol Chem , vol.272 , pp. 2300-2306
    • Al-Shawi, M.K.1    Ketchum, C.J.2    Nakamoto, R.K.3
  • 4
    • 0026545104 scopus 로고
    • Temperature dependence and Arrhenius activation energy of F-actin velocity generated in vitro by skeletal myosin
    • Anson M (1992) Temperature dependence and Arrhenius activation energy of F-actin velocity generated in vitro by skeletal myosin. J Mol Biol 224: 1029-1038
    • (1992) J Mol Biol , vol.224 , pp. 1029-1038
    • Anson, M.1
  • 5
    • 34548503612 scopus 로고    scopus 로고
    • 1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits
    • 1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits. Nat Struct Mol Biol 14: 841-846
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 841-846
    • Ariga, T.1    Muneyuki, E.2    Yoshida, M.3
  • 7
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase - some probabilities and possibilities
    • Boyer PD (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
  • 8
    • 33645796449 scopus 로고    scopus 로고
    • Catalytic and mechanical cycles in F-ATP synthases
    • Dimroth P, von Ballmoos C, Meier T (2006) Catalytic and mechanical cycles in F-ATP synthases. EMBO Rep 7: 276-282
    • (2006) EMBO Rep , vol.7 , pp. 276-282
    • Dimroth, P.1    von Ballmoos, C.2    Meier, T.3
  • 12
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • Junge W, Lill H, Engelbrecht S (1997) ATP synthase: An electrochemical transducer with rotatory mechanics. Trends Biochem Sci 22: 420-423
    • (1997) Trends Biochem Sci , vol.22 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 16
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • Sabbert D, Engelbrecht S, Junge W (1996) Intersubunit rotation in active F-ATPase. Nature 381: 623-625
    • (1996) Nature , vol.381 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 20
    • 0032568695 scopus 로고    scopus 로고
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps. Cell 93: 1117-1124
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinosita Jr, K.3    Yoshida, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.