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Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase.Effect of structural modulation of polyphenolic compounds on the inhibition of Escherichia coli ATP synthaseCrystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments.Evolutionary primacy of sodium bioenergetics.Structure of the cytosolic part of the subunit b-dimer of Escherichia coli F0F1-ATP synthase.The b subunits in the peripheral stalk of F1F0 ATP synthase preferentially adopt an offset relationshipRole of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase.BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex.The Arabidopsis protein CONSERVED ONLY IN THE GREEN LINEAGE160 promotes the assembly of the membranous part of the chloroplast ATP synthase.Geometric somersaults of a polymer chain through cyclic twisting motions.Role of the asymmetry of the homodimeric b2 stator stalk in the interaction with the F1 sector of Escherichia coli ATP synthase.
P2860
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P2860
description
2007 nî lūn-bûn
@nan
2007年の論文
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2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
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2007年论文
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2007年论文
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2007年论文
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name
ATP synthase--the structure of the stator stalk.
@ast
ATP synthase--the structure of the stator stalk.
@en
type
label
ATP synthase--the structure of the stator stalk.
@ast
ATP synthase--the structure of the stator stalk.
@en
prefLabel
ATP synthase--the structure of the stator stalk.
@ast
ATP synthase--the structure of the stator stalk.
@en
P2860
P1476
ATP synthase--the structure of the stator stalk.
@en
P2093
Joachim Weber
P2860
P356
10.1016/J.TIBS.2006.12.006
P577
2007-01-05T00:00:00Z