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Journal of Molecular Biology|July 29, 1998
A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase results in an extreme T-state structureM K Williams, B Stec, E R KantrowitzActa 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 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 LipscombJournal 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 KantrowitzBiochemistry|February 21, 1989
A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylaseS A Middleton, J W Stebbins, E R KantrowitzProceedings 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 KantrowitzJournal of Molecular Biology|December 2, 2000
Characterization of heterodimeric alkaline phosphatases from Escherichia coli: an investigation of intragenic complementationM J Hehir, J E Murphy, E R KantrowitzProtein Science : a Publication of the Protein Society|August 1, 1996
Crystal structures of the active site mutant (Arg-243-->Ala) in the T and R allosteric states of pig kidney fructose-1,6-bisphosphatase expressed in Escherichia coliB Stec, R Abraham, E Giroux, et al.Pageof 14