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H J Fromm

Showing results (91-100 of 126) with videos related to

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The Journal of Biological Chemistry|July 5, 1991
Evidence for an arginine residue at the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesisQ Dong, F Liu, A M Myers, et al.
Archives of Biochemistry and Biophysics|November 24, 1999
8-(4-Bromo-2,3-dioxobutylthio)guanosine 5'-triphosphate: a new affinity label for purine nucleotide sites in proteinsP Lee, A Gorrell, H J Fromm, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 12, 1995
Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphataseV Villeret, S Huang, H J Fromm, et al.
The Journal of Biological Chemistry|September 30, 1994
Replacement of Asp333 with Asn by site-directed mutagenesis changes the substrate specificity of Escherichia coli adenylosuccinate synthetase from guanosine 5'-triphosphate to xanthosine 5'-triphosphateC Kang, N Sun, R B Honzatko, et al.
Biochemistry|March 5, 1996
Kinetics and mechanisms of activation and inhibition of porcine liver fructose-1,6-bisphosphatase by monovalent cationsR Zhang, V Villeret, W N Lipscomb, et al.
The Journal of Biological Chemistry|June 13, 1997
Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coliB W Poland, C Bruns, H J Fromm, et al.
FEBS Letters|August 5, 1996
Crystallization and preliminary X-ray analysis of human brain hexokinaseA E Aleshin, C Zeng, H J Fromm, et al.
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.
Pageof 13

Showing results (91-100 of 126) with videos related to

Sort By:
Pageof 13
The Journal of Biological Chemistry|July 5, 1991
Evidence for an arginine residue at the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesisQ Dong, F Liu, A M Myers, et al.
Archives of Biochemistry and Biophysics|November 24, 1999
8-(4-Bromo-2,3-dioxobutylthio)guanosine 5'-triphosphate: a new affinity label for purine nucleotide sites in proteinsP Lee, A Gorrell, H J Fromm, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 12, 1995
Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphataseV Villeret, S Huang, H J Fromm, et al.
The Journal of Biological Chemistry|September 30, 1994
Replacement of Asp333 with Asn by site-directed mutagenesis changes the substrate specificity of Escherichia coli adenylosuccinate synthetase from guanosine 5'-triphosphate to xanthosine 5'-triphosphateC Kang, N Sun, R B Honzatko, et al.
Biochemistry|March 5, 1996
Kinetics and mechanisms of activation and inhibition of porcine liver fructose-1,6-bisphosphatase by monovalent cationsR Zhang, V Villeret, W N Lipscomb, et al.
The Journal of Biological Chemistry|June 13, 1997
Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coliB W Poland, C Bruns, H J Fromm, et al.
FEBS Letters|August 5, 1996
Crystallization and preliminary X-ray analysis of human brain hexokinaseA E Aleshin, C Zeng, H J Fromm, et al.
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.
Pageof 13