Pressure Effects on the Interaction between Natural Inhibitor Protein and Mitochondrial F1–ATPase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference46 articles.
1. Methods in Enzymology, Energetics, of Biological Macromolecules;Robinson,1995
2. The use of hydrostatic pressure as a tool to study viruses and other macromolecular assemblages
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5. Amino acid sequence of the protein inhibitor of mitochondrial adenosine triphosphatase.
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1. Single-Molecule Analysis of the Rotation of F1-ATPase under High Hydrostatic Pressure;Biophysical Journal;2013-10
2. Regulation of the F1F0-ATP Synthase Rotary Nanomotor in its Monomeric-Bacterial and Dimeric-Mitochondrial Forms;Journal of Biological Physics;2008-04
3. The Inhibitor Protein (IF1) Promotes Dimerization of the Mitochondrial F1F0-ATP Synthase;Biochemistry;2006-09-29
4. High hydrostatic pressure perturbs the interactions between CF0F1 subunits and induces a dual effect on activity;The International Journal of Biochemistry & Cell Biology;2004-05
5. Cross-linking of the endogenous inhibitor protein (IF1) with rotor (gamma, epsilon) and stator (alpha) subunits of the mitochondrial ATP synthase;Journal of Bioenergetics and Biomembranes;2002
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