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Biochemistry|November 26, 1999
Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamilyJ B Thoden, T J Kappock, J Stubbe, et al.Structure (London, England : 1993)|November 27, 1999
Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathwayI I Mathews, T J Kappock, J Stubbe, et al.Journal of Bacteriology|March 13, 2001
Altered pathway routing in a class of Salmonella enterica serovar Typhimurium mutants defective in aminoimidazole ribonucleotide synthetaseJ L Zilles, T J Kappock, J Stubbe, et al.Proceedings of the National Academy of Sciences of the United States of America|March 1, 1989
Mechanism-based inhibition of a mutant Escherichia coli ribonucleotide reductase (cysteine-225----serine) by its substrate CDPS S Mao, M I Johnston, J M Bollinger, et al.Biochemistry|December 21, 1993
A non-heme iron protein with heme tendencies: an investigation of the substrate specificity of thymine hydroxylaseL D Thornburg, M T Lai, J S Wishnok, et al.Biochemistry|March 21, 1989
Formylglycinamide ribonucleotide synthetase from Escherichia coli: cloning, sequencing, overproduction, isolation, and characterizationF J Schendel, E Mueller, J Stubbe, et al.Nucleic Acids Research|April 11, 2000
Accurate and rapid modeling of iron-bleomycin-induced DNA damage using tethered duplex oligonucleotides and electrospray ionization ion trap mass spectrometric analysisA Harsch, L A Marzilli, R C Bunt, et al.Biochemistry|April 5, 2000
Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: characterization of the functional residues in Chromatium vinosum PHB synthaseY Jia, T J Kappock, T Frick, et al.Biochemistry|June 2, 1992
Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathwayE Meyer, N J Leonard, B Bhat, et al.Biochemistry|March 1, 1994
N5-carboxyaminoimidazole ribonucleotide: evidence for a new intermediate and two new enzymatic activities in the de novo purine biosynthetic pathway of Escherichia coliE J Mueller, E Meyer, J Rudolph, et al.Pageof 11