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Publications by V. N. Kasho

Vacuolar ATPases, Like F1,f0-ATPases, Show a Strong Dependence of the Reaction Velocity on the Binding of More Than One ATP Per Enzyme.

Proceedings of the National Academy of Sciences of the United States of America

Multidisciplinary

English

Related publications

Cryo-Em Studies of the Structure and Dynamics of Vacuolar-Type ATPases

Science advances

Multidisciplinary

English

How Azide Inhibits ATP Hydrolysis by the F-ATPases

Proceedings of the National Academy of Sciences of the United States of America

Multidisciplinary

English

On the History of Ecto-ATPases: The Role of W. A. Engelhardt

Purinergic Signalling

Molecular Neuroscience

Molecular Biology

English

Identification of the Transmembrane Metal Binding Site in Cu+-Transporting PIB-type ATPases

Journal of Biological Chemistry

Molecular Biology

English

Letter: Vonoprazan, a Long-Lasting Acid Suppressor of the Gastric H+, K+-ATPases With - Implications for Renal H+, K+-ATPases

Alimentary Pharmacology and Therapeutics

Gastroenterology

English

The C15 Ring of the Spirulina Platensis F-Atp Synthase: F1/F0 Symmetry Mismatch Is Not Obligatory

Molecular Biology

English

Enzyme Specificity in Reactions of More Than One Co-Substrate

Biochemical Journal

Molecular Biology

English

Ubiquitinated Proteins Activate the Proteasomal ATPases by Binding to Usp14 or Uch37 Homologs

Journal of Biological Chemistry

Molecular Biology

English

Vacuolar Import of Phosphatidylcholine Requires the ATP-Binding Cassette Transporter Ybt1

Molecular Biology

Structural Biology

English