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The Journal of Biological Chemistry|June 2, 1995
Identification of arginine residues in the putative L-aspartate binding site of Escherichia coli adenylosuccinate synthetaseW Wang, B W Poland, R B Honzatko, et al.The Journal of Biological Chemistry|July 18, 2000
Mutations in the hinge of a dynamic loop broadly influence functional properties of fructose-1,6-bisphosphataseS W Nelson, J Y Choe, R B Honzatko, et al.The Journal of Biological Chemistry|October 23, 1997
Major changes in the kinetic mechanism of AMP inhibition and AMP cooperativity attend the mutation of Arg49 in fructose-1,6-bisphosphataseL F Shyur, B W Poland, R B Honzatko, et al.The Journal of Biological Chemistry|November 30, 2000
The N-terminal segment of recombinant porcine fructose-1,6-bisphosphatase participates in the allosteric regulation of catalysisS W Nelson, F T Kurbanov, R B Honzatko, et al.Biochemistry|May 29, 1999
Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coliJ Y Choe, B W Poland, H J Fromm, et al.Journal of Molecular Biology|April 20, 1988
Preliminary X-ray crystallographic study of adenylosuccinate synthetase from Escherichia coliM A Serra, M B Bass, H J Fromm, et al.The Journal of Biological Chemistry|December 27, 1996
Biochemical properties of mutant and wild-type fructose-1,6-bisphosphatases are consistent with the coupling of intra- and intersubunit conformational changes in the T- and R-state transitionL F Shyur, A E Aleshin, R B Honzatko, et al.The Journal of Biological Chemistry|July 4, 1998
Directed mutations in the poorly defined region of porcine liver fructose-1,6-bisphosphatase significantly affect catalysis and the mechanism of AMP inhibitionF T Kurbanov, J Y Choe, R B Honzatko, et al.The Journal of Biological Chemistry|June 20, 1998
Ambiguities in mapping the active site of a conformationally dynamic enzyme by directed mutation. Role of dynamics in structure-function correlations in Escherichia coli adenylosuccinate synthetaseW Wang, A Gorrell, Z Hou, et al.Biochemistry|August 26, 1998
Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphataseJ Y Choe, B W Poland, H J Fromm, et al.Pageof 11