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Proceedings of the National Academy of Sciences of the United States of America|October 1, 1979
A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferaseR B Honzatko, H L Monaco, W N LipscombBiochemical and Biophysical Research Communications|February 13, 1987
The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a molecular modelling studyJ E Gouaux, K L Krause, W N LipscombProceedings of the National Academy of Sciences of the United States of America|August 2, 2001
Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanismH Guo, Q Cui, W N Lipscomb, et al.Biochemistry|August 21, 1990
Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolutionR C Stevens, J E Gouaux, W N LipscombProceedings of the National Academy of Sciences of the United States of America|October 1, 1972
Similarities between the conformation of arsanilazotyrosine 248 of carboxypeptidase A in the crystalline state and in solutionF A Quiocho, C H McMurray, W N LipscombProceedings of the National Academy of Sciences of the United States of America|June 1, 1980
Structure of an actively exchanging complex between carboxypeptidase A and a substrate analogueD C Rees, R B Honzatko, W N LipscombActa Crystallographica. Section D, Biological Crystallography|August 16, 2000
Crystallization and structure determination of the catalytic trimer of Methanococcus jannaschii aspartate transcarbamoylaseJ Vitali, T Vorobyova, G Webster, et al.Biochemistry|March 24, 1992
Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylaseC J Newton, R C Stevens, E R KantrowitzBiochemistry|April 17, 1990
Function of serine-171 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamoylaseN J Dembowski, C J Newton, E R KantrowitzJournal of Molecular Biology|November 3, 1995
Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatasesJ E Murphy, T T Tibbitts, E R KantrowitzPageof 22