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The Journal of Biological Chemistry|September 25, 1993
Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupiedJ Weber, S Wilke-Mounts, R S Lee, et al.The Journal of Biological Chemistry|January 25, 1992
On the location and function of tyrosine beta 331 in the catalytic site of Escherichia coli F1-ATPaseJ Weber, R S Lee, E Grell, et al.The Journal of Biological Chemistry|March 25, 1993
Combined application of site-directed mutagenesis, 2-azido-ATP labeling, and lin-benzo-ATP binding to study the noncatalytic sites of Escherichia coli F1-ATPaseJ Weber, R S Lee, S Wilke-Mounts, et al.Journal of Fluorescence|November 16, 2013
lin-Benzo-ATP and-ADP: Versatile fluorescent probes for spectroscopic and biochemical studiesE Grell, E Lewitzki, C Bremer, et al.Annual Review of Biophysics and Biophysical Chemistry|January 1, 1990
The proton-translocating ATPase of Escherichia coliA E SeniorThe Journal of Biological Chemistry|May 25, 1981
Divalent metals in beef heart mitochondrial adenosine triphosphatase. Demonstration of the metals in membrane-bound enzyme and studies of the interconversion of the "1-Mg" and "2-Mg" forms of the enzymeA E SeniorThe Journal of Biological Chemistry|November 25, 1979
Tightly bound magnesium in mitochondrial adenosine triphosphatase from beef heartA E SeniorActa Physiologica Scandinavica. Supplementum|October 28, 1998
Catalytic mechanism of P-glycoproteinA E SeniorBiochemistry|February 25, 1975
Mitochondrial adenosine triphosphatase. Location of sulfhydryl groups and disulfide bonds in soluble enzyme from beef heartA E SeniorJournal of Bioenergetics and Biomembranes|October 1, 1992
Catalytic sites of Escherichia coli F1-ATPaseA E SeniorPageof 304