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Biochemistry|July 1, 1999
The role of beta-Arg-182, an essential catalytic site residue in Escherichia coli F1-ATPaseS Nadanaciva, J Weber, A E SeniorThe Journal of Biological Chemistry|March 6, 1999
Binding of the transition state analog MgADP-fluoroaluminate to F1-ATPaseS Nadanaciva, J Weber, A E SeniorBiochemistry|August 7, 1998
Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthaseS Löbau, J Weber, A E SeniorThe Journal of Biological Chemistry|August 2, 1996
Specific tryptophan substitution in catalytic sites of Escherichia coli F1-ATPase allows differentiation between bound substrate ATP and product ADP in steady-state catalysisJ Weber, C Bowman, A E SeniorJournal of Bioenergetics and Biomembranes|July 16, 2004
The catalytic transition state in ATP synthaseA E Senior, J Weber, S NadanacivaFEBS Letters|October 18, 2000
ATP-driven rotation of the gamma subunit in F(1)-ATPaseJ Weber, S Nadanaciva, A E SeniorThe Journal of Experimental Biology|December 22, 1999
Rate acceleration of ATP hydrolysis by F(1)F(o)-ATP synthaseA E Senior, S Nadanaciva, J WeberBiochemistry|August 5, 2000
New probes of the F1-ATPase catalytic transition state reveal that two of the three catalytic sites can assume a transition state conformation simultaneouslyS Nadanaciva, J Weber, A E SeniorThe Journal of Biological Chemistry|August 12, 1994
Cooperativity and stoichiometry of substrate binding to the catalytic sites of Escherichia coli F1-ATPase. Effects of magnesium, inhibitors, and mutationJ Weber, S Wilke-Mounts, A E SeniorThe Journal of Biological Chemistry|June 26, 1999
Effect of the epsilon-subunit on nucleotide binding to Escherichia coli F1-ATPase catalytic sitesJ Weber, S D Dunn, A E SeniorPageof 304