Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase.
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Mechanism of potassium-channel selectivity revealed by Na+ and Li+ binding sites within the KcsA poreStructure of the rotor ring modified with N,N'-dicyclohexylcarbodiimide of the Na+-transporting vacuolar ATPaseCrystal structure of the central axis DF complex of the prokaryotic V-ATPaseA new type of Na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motifRotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structuresOperating principles of rotary molecular motors: differences between F1 and V1 motorsCrystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor.Torque generation of Enterococcus hirae V-ATPase.Loose binding of the DF axis with the A3B3 complex stimulates the initial activity of Enterococcus hirae V1-ATPase.On the principle of ion selectivity in Na+/H+-coupled membrane proteins: experimental and theoretical studies of an ATP synthase rotor.Atomistic simulations indicate the c-subunit ring of the F1Fo ATP synthase is not the mitochondrial permeability transition pore.Insights into the biochemistry of the ubiquitous NhaP family of cation/H+ antiporters.Slow dissociation of a charged ligand: analysis of the primary quinone Q(A) site of photosynthetic bacterial reaction centers.Significance of the glutamate-139 residue of the V-type Na+-ATPase NtpK subunit in catalytic turnover linked with salt tolerance of Enterococcus hirae.Mutant LV(476-7)AA of A-subunit of Enterococcus hirae V1-ATPase: High affinity of A3B3 complex to DF axis and low ATPase activity.Mutagenesis of the residues forming an ion binding pocket of the NtpK subunit of Enterococcus hirae V-ATPaseComplete genome determination and analysis of Acholeplasma oculi strain 19L, highlighting the loss of basic genetic features in the Acholeplasmataceae.Biophysical Characterization of a Thermoalkaliphilic Molecular Motor with a High Stepping Torque Gives Insight into Evolutionary ATP Synthase Adaptation.Structure and dynamics of rotary V1 motor.Rotation Mechanism of Molecular Motor V1-ATPase Studied by Multiscale Molecular Dynamics Simulation.Mussel and mammalian ATP synthase share the same bioenergetic cost of ATP.Genomic Insights Into the Acid Adaptation of Novel Methanotrophs Enriched From Acidic Forest Soils
P2860
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P2860
Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase.
@ast
Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase.
@en
type
label
Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase.
@ast
Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase.
@en
prefLabel
Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase.
@ast
Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase.
@en
P2093
P2860
P50
P356
P1476
Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase
@en
P2093
Ichiro Yamato
Mikako Shirouzu
Yoshimi Kakinuma
P2860
P304
P356
10.1073/PNAS.0800992105
P407
P577
2008-06-16T00:00:00Z