Mitochondrial ATP Synthase Residue βArginine-408, Which Interacts with the Inhibitory Site of Regulatory Protein IF_1, Is Essential for the Function of the Enzyme
スポンサーリンク
概要
- 論文の詳細を見る
- Japanese Biochemical Societyの論文
- 2005-08-01
著者
-
Ichikawa Naoki
Department Of Food And Nutrition Faculty Of Human Life Science Osaka City University
-
Nakamura Mai
Department Of Food And Nutrition Faculty Of Human Life Science Osaka City University
-
CHISUWA Naomi
Department of Food and Nutrition, Faculty of Human Life Science, Osaka City University
-
TANASE Mamiko
Department of Food and Nutrition, Faculty of Human Life Science, Osaka City University
-
Ichikawa Naoki
Department Of Food And Human Health Sciences Graduate School Of Human Life Science Osaka City Univer
-
Tanase Mamiko
Department Of Food And Nutrition Faculty Of Human Life Science Osaka City University
-
Chisuwa Naomi
Department Of Food And Nutrition Faculty Of Human Life Science Osaka City University
-
Ichikawa Naoki
Department Of Chemistry Graduate School Of Science Hiroshima University
関連論文
- Structural and Catalytic Properties of Silica-Coated Alumina
- Comparison of Multiple Access Schemes in Multibeam Non-GEO Satellite Communication Systems
- Improved Hypolipidemic Effects of Xanthan Gum-Galactomannan Mixtures in Rats
- Deletion of Mitochondrial ATPase Inhibitor in the Yeast Saccharomyces cerevisiae Decreased Cellular and Mitochondrial ATP Levels under Non-Nutritional Conditions and Induced a Respiration-Deficient Cell-Type
- Binding of an Intrinsic ATPase Inhibitor to the F_1FoATPase in Phosphorylating Conditions of Yeast Mitochondria^1
- The Region from Phenylalanine-17 to Phenylalanine-28 of a Yeast Mitochondrial ATPase Inhibitor Is Essential for Its ATPase Inhibitory Activity
- Nucleotide Sequence of cDNA Coding the Mitochondrial Precursor Protein of the ATPase Inhibitor from Humans
- Mitochondrial ATP Synthase Residue βArginine-408, Which Interacts with the Inhibitory Site of Regulatory Protein IF_1, Is Essential for the Function of the Enzyme
- The Carboxyl-Terminal Region of the Yeast ATPase Inhibitor Is Indispensable for the Stability of the Protein in Mitochondria
- An Intrinsic ATPase Inhibitor Binds near the Active Site of Yeast Mitochondrial F_1-ATPase^1
- Binding of an Intrinsic ATPase Inhibitor to the Interface between α- and β-Subunits of F_1F_oATPase upon De-Energization of Mitochondria
- Study of Capillary Driven Flow in a Tube
- Flow Structure of Thermal Counterflow Jet : I. QUANTUM LIQUIDS AND SOLIDS : Superfluid Flow
- Flow of He II through Porous-Plug Phase Sparators
- Application of Porous Solid Nitrogen to Space Borne Cooling Missions
- A Yeast Mitochondrial ATPase Inhibitor Interacts with Three Proteins That Are Easy to Dissociate from the Mitochondrial Inner Membrane
- Application of ^Fe Mossbauer Spectroscopy to a Study of the Difference in Interactions between Guest and Host Molecules among (R),(S) and Racemic Isomers for (2-Methylbutyl)-,(2-Phenylpropyl)- and (2-Phenylbutyl)ferrocenes Enclathrated in Deoxycholic
- Glutamic Acid in the Inhibitory Site of Mitochondrial ATPase Inhibitor, IF_1, Participates in pH Sensing in Both Mammals and Yeast
- Requirement for Lysine-19 of the Yeast Mitochondrial ATPase Inhibitor for the Stability of the Inactivated Inhibitor-F_1Fo Complex at Higher pH
- The Region from Phenylalanine-17 to Phenylalanine-28 of a Yeast Mitochondrial ATPase Inhibitor Is Essential for Its ATPase Inhibitory Activity.