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The Journal of Biological Chemistry|September 8, 1995
alpha-Aspartate 261 is a key residue in noncatalytic sites of Escherichia coli F1-ATPaseJ Weber, C Bowman, S Wilke-Mounts, et al.
Biochemistry|November 26, 1999
Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilizationS Nadanaciva, J Weber, S Wilke-Mounts, et al.
Archives of Biochemistry and Biophysics|March 1, 1994
Tryptophan-free Escherichia coli F1-ATPaseS Wilke-Mounts, J Weber, E Grell, et al.
The Journal of Biological Chemistry|February 7, 1997
F1-ATPase, roles of three catalytic site residuesS Löbau, J Weber, S Wilke-Mounts, et al.
The Journal of Biological Chemistry|April 15, 1994
Tryptophan fluorescence provides a direct probe of nucleotide binding in the noncatalytic sites of Escherichia coli F1-ATPaseJ Weber, S Wilke-Mounts, E Grell, et al.
The Journal of Biological Chemistry|August 18, 1995
P-glycoprotein is stably inhibited by vanadate-induced trapping of nucleotide at a single catalytic siteI L Urbatsch, B Sankaran, J Weber, et al.
Biochemistry|February 21, 1998
Mg2+ coordination in catalytic sites of F1-ATPaseJ Weber, S T Hammond, S Wilke-Mounts, et al.
Biochemistry|September 2, 1998
Tryptophan substitutions surrounding the nucleotide in catalytic sites of F1-ATPaseJ Weber, S Wilke-Mounts, S T Hammond, et al.
Archives of Biochemistry and Biophysics|September 1, 1992
Catalytic properties of Escherichia coli F1-ATPase depleted of endogenous nucleotidesA E Senior, R S Lee, M K al-Shawi, et al.
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