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The Journal of Biological Chemistry|March 15, 2003
A role for native lipids in the stabilization and two-dimensional crystallization of the Escherichia coli NADH-ubiquinone oxidoreductase (complex I)Leonid A Sazanov, Joe Carroll, Peter Holt, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 6, 2013
Assembly factors for the membrane arm of human complex IByron Andrews, Joe Carroll, Shujing Ding, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 23, 2021
TMEM70 and TMEM242 help to assemble the rotor ring of human ATP synthase and interact with assembly factors for complex IJoe Carroll, Jiuya He, Shujing Ding, et al.
Journal of Molecular Biology|January 4, 2011
Binding of the inhibitor protein IF(1) to bovine F(1)-ATPaseJohn V Bason, Michael J Runswick, Ian M Fearnley, et al.
The Journal of Biological Chemistry|April 2, 2004
The phosphorylation of subunits of complex I from bovine heart mitochondriaRuming Chen, Ian M Fearnley, Sew Y Peak-Chew, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 20, 2019
Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthaseJoe Carroll, Jiuya He, Shujing Ding, et al.
Proceedings of the National Academy of Sciences of the United States of America|August 9, 2017
Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthaseJiuya He, Joe Carroll, Shujing Ding, et al.
Biochimica Et Biophysica Acta|July 3, 2003
The nuclear encoded subunits of complex I from bovine heart mitochondriaJudy Hirst, Joe Carroll, Ian M Fearnley, et al.
FEBS Letters|June 16, 2007
Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondriaRuming Chen, Michael J Runswick, Joe Carroll, et al.
FEBS Letters|April 10, 2017
Human METTL12 is a mitochondrial methyltransferase that modifies citrate synthaseVirginie F Rhein, Joe Carroll, Shujing Ding, et al.
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