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F1-ATPase

Known as: F 1 ATPase, F-1-ATPase, Proton-Translocating ATPase, F1 Sector 
The catalytic sector of proton-translocating ATPase complexes. It contains five subunits named alpha, beta, gamma, delta and eta.
National Institutes of Health

Papers overview

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Highly Cited
2011
Highly Cited
2011
F1-ATPase is a nanosized biological energy transducer working as part of FoF1-ATP synthase. Its rotary machinery transduces… Expand
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Review
2006
Review
2006
Purpose of review Until recently, F1Fo ATP synthase expression was believed to be strictly confined to mitochondria where it… Expand
Highly Cited
2004
Highly Cited
2004
The structure of bovine F1‐ATPase inhibited with ADP and beryllium fluoride at 2.0 Å resolution contains two ADP.BeF3− complexes… Expand
Highly Cited
2003
Highly Cited
2003
F1Fo-ATP synthase is the enzyme responsible for most of the ATP synthesis in living systems. The catalytic domain F1 of the F1Fo… Expand
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Highly Cited
2000
Highly Cited
2000
The central stalk in ATP synthase, made of γ, δ and ɛ subunits in the mitochondrial enzyme, is the key rotary element in the… Expand
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Review
1997
Review
1997
The structure of the core catalytic unit of ATP synthase, alpha 3 beta 3 gamma, has been determined by X-ray crystallography… Expand
Highly Cited
1996
Highly Cited
1996
In the structure of bovine mitochondrial F1-ATPase that was previously determined with crystals grown in the presence of adenylyl… Expand
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Highly Cited
1994
Highly Cited
1994
In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution, the three catalytic β-subunits differ… Expand
Highly Cited
1992
Highly Cited
1992
Manganese is known to accumulate in mitochondria and in mitochondria-rich tissues in vivo. Although Ca2+ enhances mitochondrial… Expand
Highly Cited
1986
Highly Cited
1986
The structure of soluble F1-ATPase (EC 3.6.1.3) has been investigated by computer analysis of individual molecular images… Expand
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