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Results: 1-3 |
Results: 3
Catalytic acid-base groups in yeast pyruvate decarboxylase. 1. Site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, H115F, and E477Q substitutions
Authors: Liu, M Sergienko, EA Guo, FS Wang, J Tittmann, K Hubner, G Furey, W Jordan, F
Citation: M. Liu et al., Catalytic acid-base groups in yeast pyruvate decarboxylase. 1. Site-directed mutagenesis and steady-state kinetic studies on the enzyme with the D28A, H114F, H115F, and E477Q substitutions, BIOCHEM, 40(25), 2001, pp. 7355-7368
The role of the non-conserved residue at position 104 of class A beta-lactamases in susceptibility to mechanism-based inhibitors
Authors: Guo, FS Huynh, J Dmitrienko, GI Viswanatha, T Clarke, AJ
Citation: Fs. Guo et al., The role of the non-conserved residue at position 104 of class A beta-lactamases in susceptibility to mechanism-based inhibitors, BBA-PROT ST, 1431(1), 1999, pp. 132-147
ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease
Authors: Singh, SK Guo, FS Maurizi, MR
Citation: Sk. Singh et al., ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease, BIOCHEM, 38(45), 1999, pp. 14906-14915
Risultati: 1-3 |