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ATP-driven proton fluxes across membranes of secretory organelles.
S. Cidon
*
, H. Ben-David,
N. Nelson
*
Corresponding author for this work
Biochemistry Molecular Biology
Research output
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Contribution to journal
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Article
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peer-review
46
Scopus citations
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Keyphrases
Chromaffin Granules
100%
Proton Uptake
100%
Secretory Organelles
100%
Proton Flux
100%
ATP-dependent
66%
Chloride
50%
Lysosome
50%
Synaptosomes
50%
Reconstitution
16%
Proton
16%
Cholate
16%
Phenazine Methosulfate
16%
Minor Effect
16%
Sodium Cholate
16%
Carbonyl
16%
Translocator
16%
Cyanide
16%
Submitochondrial Particles
16%
Dicyclohexylcarbodiimide
16%
Sodium Bromide
16%
Mitochondrial ATPase
16%
Delta pH
16%
ATPase Enzyme
16%
Medicine and Dentistry
Adenosine Triphosphate
100%
Chromaffin Granule
100%
Proton Transport
100%
Lysosome
33%
Cholic Acid
33%
Synaptosome
33%
Carbonyl Cyanide 4 (Trifluoromethoxy)phenylhydrazone
16%
Adenosine Triphosphatase
16%
Mitochondrial Membrane Transport Protein
16%
Ascorbic Acid
16%
Proton Transporting Adenosine Triphosphate Synthase
16%
Dicyclohexylcarbodiimide
16%
Sodium Bromide
16%
Lysosome Membrane
16%
Synaptic Membrane
16%
Phenazine Methosulfate
16%
Submitochondrial Particle
16%
Solubilization
16%
Neuroscience
Adenosine Triphosphate
100%
Proton Transport
100%
Lysosome
50%
Synaptosome
50%
Cholic Acid
33%
Carrier Protein
16%
Vitamin C
16%
Adenosine Triphosphatase
16%
ATP Synthase
16%
V-ATPase
16%
Submitochondrial Particle
16%
Phenazine
16%
Biochemistry, Genetics and Molecular Biology
Adenosine Triphosphate
100%
Proton Transport
100%
Lysosome
50%
Enzyme
16%
ATP Synthase
16%
ATPase
16%
Dilution
16%
Mitochondrial Membrane Transport Protein
16%
V-ATPase
16%
Sodium Bromide
16%
Carrier Protein
16%
Vitamin C
16%
Solubilization
16%