Binding of subunit E into the A–B interface of the A1AO ATP synthase
Author:
Funder
A*STAR BMRC
SFB 807
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference29 articles.
1. Connecting stalks in V-type ATPase;Boekema;Nature,1999
2. ATP synthases: structure function and evolution of unique secondary energy converters;Müller;Cell. Mol. Life Sci.,2003
3. New insights into structure–function relationships between archeal ATP synthase (A1AO) and vacuolar type ATPase (V1VO);Grüber;BioEssays,2008
4. Three-dimensional structure of A1AO ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus by electron microscopy;Vonck;J. Biol. Chem.,2009
5. Structural and functional analysis of the coupling subunit F in solution and topological arrangement of the stalk domains of the methanogenic A1AO ATP synthase;Schäfer;J. Bioenerg. Biomembr.,2006
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1. The stimulating role of subunit F in ATPase activity inside the A 1 -complex of the Methanosarcina mazei Gö1 A 1 A O ATP synthase;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2016-02
2. Adaptations of anaerobic archaea to life under extreme energy limitation;FEMS Microbiology Reviews;2014-05
3. Conformational Properties of Secondary Amino Acids: Replacement of Pipecolic Acid byN-Methyl-L-alanine in Efrapeptin C;Chemistry & Biodiversity;2013-05
4. Structural elements of the C-terminal domain of subunit E (E133-222) from the Saccharomyces cerevisiae V1VO ATPase determined by solution NMR spectroscopy;Journal of Bioenergetics and Biomembranes;2011-08-09
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