SubunitE of mitochondrial ATP synthase: A bioinformatic analysis reveals a phosphopeptide binding motif supporting a multifunctional regulatory role and identifies a related human brain protein with the same motif
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry,Structural Biology
Reference37 articles.
1. Structure of the ATP-Synthase from Chloroplasts and Mitochondria Studied by Electron Microscopy
2. Molecular Rotary Motors
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1. Mitochondrial and cell-surface F0F1ATPsynthase in innate and acquired cardioprotection;Journal of Bioenergetics and Biomembranes;2009-04
2. ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas;Microbiology and Molecular Biology Reviews;2008-12
3. Functional and stoichiometric analysis of subunit e in bovine heart mitochondrial F0F1ATP synthase;Journal of Bioenergetics and Biomembranes;2008-08
4. Identification of a Conserved Calmodulin-Binding Motif ∊ the Sequence of F0F1ATPsynthase Inhibitor Protein;Journal of Bioenergetics and Biomembranes;2005-10
5. Functional Analysis of Subunit e of the F 1 F o -ATP Synthase of the Yeast Saccharomyces cerevisiae : Importance of the N-Terminal Membrane Anchor Region;Eukaryotic Cell;2005-02
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