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Biochemistry|March 3, 1992
Conversion of the noncooperative Bacillus subtilis aspartate transcarbamoylase into a cooperative enzyme by a single amino acid substitutionJ W Stebbins, E R KantrowitzProtein Engineering|May 1, 1994
The use of alanine scanning mutagenesis to determine the role of the N-terminus of the regulatory chain in the heterotropic mechanism of Escherichia coli aspartate transcarbamoylaseN J Dembowski, E R KantrowitzProteins|July 17, 2001
Binding of AMP to two of the four subunits of pig kidney fructose-1,6-bisphosphatase induces the allosteric transitionN Kelley-Loughnane, E R KantrowitzBiochimica Et Biophysica Acta|June 19, 2001
Use of silicate sol-gels to trap the R and T quaternary conformational states of pig kidney fructose-1,6-bisphosphataseJ K McIninch, E R KantrowitzMolecular Microbiology|May 1, 1994
Why are mammalian alkaline phosphatases much more active than bacterial alkaline phosphatases?J E Murphy, E R KantrowitzBiochimica Et Biophysica Acta|July 14, 2001
AMP inhibition of pig kidney fructose-1,6-bisphosphataseN Kelley-Loughnane, E R KantrowitzScience (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|March 1, 1990
The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chainC J Newton, E R KantrowitzProtein Engineering|January 1, 1993
Overproduction and purification of the regulatory subunit of Escherichia coli aspartate transcarbamoylaseN J Dembowski, E R KantrowitzPageof 14