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The Journal of Biological Chemistry|May 10, 1976
An essential residue at the active site of aspartate transcarbamylaseE R Kantrowitz, W N LipscombThe Journal of Biological Chemistry|May 10, 1977
Functionally important arginine residues of aspartate transcarbamylaseE R Kantrowitz, W N LipscombScience (New York, N.Y.)|August 5, 1988
Escherichia coli aspartate transcarbamylase: the relation between structure and functionE R Kantrowitz, W N LipscombTrends in Biochemical Sciences|February 1, 1990
Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transitionE R Kantrowitz, W N LipscombProceedings of the National Academy of Sciences of the United States of America|April 1, 1982
Zn(II)-induced cooperativity of Escherichia coli ornithine transcarbamoylaseL C Kuo, W N Lipscomb, E R KantrowitzThe Journal of Biological Chemistry|December 25, 1975
Interaction of tetraiodofluorescein with aspartate transcarbamylase and its isolated catalytic and regulatory subunitsL B Jacobsverg, E R Kantrowitz, W N LipscombProceedings of the National Academy of Sciences of the United States of America|September 29, 1999
A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidaseN Sträter, L Sun, E R Kantrowitz, et al.Proteins|January 29, 2000
Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 AL Jin, B Stec, W N Lipscomb, et al.Proceedings of the National Academy of Sciences of the United States of America|January 1, 1977
Interaction of tetraiodofluorescein with a modified form of aspartate transcarbamylaseE R Kantrowitz, L B Jacobsberg, S M Landfear, et al.Biochemistry|February 21, 1989
Structure of a single amino acid mutant of aspartate carbamoyltransferase at 2.5-A resolution: implications for the cooperative mechanismJ E Gouaux, W N Lipscomb, S A Middleton, et al.Pageof 22