Christine P. Macol, Ph.D.
|2001||Boston College, Newton, MA, United States|
Mean distance: 5687.57
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|Chan RS, Sakash JB, Macol CP, et al. (2002) The role of intersubunit interactions for the stabilization of the T state of Escherichia coli aspartate transcarbamoylase. The Journal of Biological Chemistry. 277: 49755-60|
|Macol CP, Tsuruta H, Kantrowitz ER. (2002) Importance of domain closure for the catalysis and regulation of Escherichia coli aspartate transcarbamoylase. The Journal of Biological Chemistry. 277: 26852-7|
|Fetler L, Tauc P, Baker DP, et al. (2002) Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase. Protein Science : a Publication of the Protein Society. 11: 1074-81|
|Fetler L, Vachette P, Macol CP, et al. (2002) Revisiting the allosteric mechanism of aspartate transcarbamoylase Nature Structural Biology. 9: 87-89|
|Macol CP, Kantrowitz ER, Tsuruta H, et al. (2002) Response to Fetler and Vachette Nature Structural Biology. 9: 88-89|
|Macol CP, Tsuruta H, Stec B, et al. (2001) Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase. Nature Structural Biology. 8: 423-6|
|Hack ES, Vorobyova T, Sakash JB, et al. (2000) Characterization of the aspartate transcarbamoylase from Methanococcus jannaschii. The Journal of Biological Chemistry. 275: 15820-7|
|Macol C, Dutta M, Stec B, et al. (1999) The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity Protein Science. 8: 1305-1313|