Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite.
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The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxidePathways of As(III) detoxification in Saccharomyces cerevisiae.The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexesPhosphate exchange and ATP synthesis by DMSO-pretreated purified bovine mitochondrial ATP synthaseAstrocytic mitochondrial membrane hyperpolarization following extended oxygen and glucose deprivationMaking ATP.F1-ATPase of Escherichia coli: the ε- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands.High-resolution single-molecule characterization of the enzymatic states in Escherichia coli F1-ATPaseLoss of mitochondrial membrane potential is associated with increase in mitochondrial volume: physiological role in neurones.Rapid hydrolysis of ATP by mitochondrial F1-ATPase correlates with the filling of the second of three catalytic sitesA research journey with ATP synthase.How azide inhibits ATP hydrolysis by the F-ATPases.A LC-MS/MS method for the analysis of intracellular nucleoside triphosphate levels.ε subunit of Bacillus subtilis F1-ATPase relieves MgADP inhibition.A functionally inactive, cold-stabilized form of the Escherichia coli F1Fo ATP synthase.Direct interaction of Na-azide with the KATP channel.Cytoskeletal "jellyfish" structure of Mycoplasma mobile.ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas.Molecular processes of inhibition and stimulation of ATP synthase caused by the phytotoxin tentoxin.Frontiers in ATP synthase research: understanding the relationship between subunit movements and ATP synthesis.Substitution of betaGlu(201) in the alpha(3)beta(3)gamma subcomplex of the F(1)-ATPase from the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides.Kinetic mechanism of mitochondrial adenosine triphosphatase. ADP-specific inhibition as revealed by the steady-state kinetics.Interaction of Mg2+ with F0.F1 mitochondrial ATPase as related to its slow active/inactive transition.Severe MgADP inhibition of Bacillus subtilis F1-ATPase is not due to the absence of nucleotide binding to the noncatalytic nucleotide binding sites.Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase.The alpha3beta3gamma subcomplex of the F1-ATPase from the thermophilic bacillus PS3 with the betaT165S substitution does not entrap inhibitory MgADP in a catalytic site during turnover.Catalytic activity of the alpha3beta3gamma complex of F1-ATPase without noncatalytic nucleotide binding site.ATP synthesis by F0F1-ATP synthase independent of noncatalytic nucleotide binding sites and insensitive to azide inhibition.Cross-linking of two beta subunits in the closed conformation in F1-ATPase.The noncatalytic site-deficient alpha3beta3gamma subcomplex and FoF1-ATP synthase can continuously catalyse ATP hydrolysis when Pi is present.The fluorescence spectrum of the introduced tryptophans in the alpha 3(beta F155W)3gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 cannot be used to distinguish between the number of nucleoside di- and triphosphates bound to catThe presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F(1)-ATPase.The affinity purification and characterization of ATP synthase complexes from mitochondria.The mechanism of stimulation of MgATPase activity of chloroplast F1-ATPase by non-catalytic adenine-nucleotide binding. Acceleration of the ATP-dependent release of inhibitory ADP from a catalytic site.Energy-dependent transformation of F0.F1-ATPase in Paracoccus denitrificans plasma membranes.The vacuolar ATPase: sulfite stabilization and the mechanism of nitrate inactivation.Mitochondrial ATP synthase. Crystal structure of the catalytic F1 unit in a vanadate-induced transition-like state and implications for mechanism.Interaction of the clathrin-coated vesicle V-ATPase with ADP and sodium azide.Characterization of a chemical anoxia model in cerebellar granule neurons using sodium azide: protection by nifedipine and MK-801.Chemomechanical coupling of human mitochondrial F1-ATPase motor.
P2860
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P2860
Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite.
description
1982 nî lūn-bûn
@nan
1982年の論文
@ja
1982年論文
@yue
1982年論文
@zh-hant
1982年論文
@zh-hk
1982年論文
@zh-mo
1982年論文
@zh-tw
1982年论文
@wuu
1982年论文
@zh
1982年论文
@zh-cn
name
Kinetic mechanism of mitochond ...... de and activation by sulphite.
@en
Kinetic mechanism of mitochond ...... de and activation by sulphite.
@nl
type
label
Kinetic mechanism of mitochond ...... de and activation by sulphite.
@en
Kinetic mechanism of mitochond ...... de and activation by sulphite.
@nl
prefLabel
Kinetic mechanism of mitochond ...... de and activation by sulphite.
@en
Kinetic mechanism of mitochond ...... de and activation by sulphite.
@nl
P2093
P2860
P356
P1433
P1476
Kinetic mechanism of mitochond ...... de and activation by sulphite.
@en
P2093
Vasilyeva EA
Vinogradov AD
P2860
P356
10.1042/BJ2020015
P407
P577
1982-01-01T00:00:00Z