Enrico Di Cera, M.D.
|Biochemistry and Molecular Biology||Saint Louis University, St. Louis, MO, United States|
Google:"Enrico Di Cera, M.D."
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|Vogt AD, Chakraborty P, Di Cera E. (2015) Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold. The Journal of Biological Chemistry. 290: 22435-45|
|Pelc LA, Chen Z, Gohara DW, et al. (2015) Why Ser and not Thr brokers catalysis in the trypsin fold. Biochemistry. 54: 1457-64|
|Vogt AD, Pozzi N, Chen Z, et al. (2014) Essential role of conformational selection in ligand binding. Biophysical Chemistry. 186: 13-21|
|Barranco-Medina S, Pozzi N, Vogt AD, et al. (2013) Histone H4 promotes prothrombin autoactivation. The Journal of Biological Chemistry. 288: 35749-57|
|Vogt AD, Di Cera E. (2013) Conformational selection is a dominant mechanism of ligand binding. Biochemistry. 52: 5723-9|
|Vogt AD, Di Cera E. (2012) Conformational selection or induced fit? A critical appraisal of the kinetic mechanism. Biochemistry. 51: 5894-902|
|Pozzi N, Vogt AD, Gohara DW, et al. (2012) Conformational selection in trypsin-like proteases. Current Opinion in Structural Biology. 22: 421-31|
|Niu W, Chen Z, Gandhi PS, et al. (2011) Crystallographic and kinetic evidence of allostery in a trypsin-like protease. Biochemistry. 50: 6301-7|
|Gandhi PS, Chen Z, Appelbaum E, et al. (2011) Structural basis of thrombin-protease-activated receptor interactions. Iubmb Life. 63: 375-82|
|Pozzi N, Chen R, Chen Z, et al. (2011) Rigidification of the autolysis loop enhances Na(+) binding to thrombin. Biophysical Chemistry. 159: 6-13|