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Methods in Enzymology|March 18, 2009
Practical approaches to protein folding and assembly: spectroscopic strategies in thermodynamics and kineticsJad Walters, Sara L Milam, A Clay ClarkThe Biochemical Journal|August 18, 2004
Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3Brett Feeney, Cristina Pop, Ashutosh Tripathy, et al.Archives of Biochemistry and Biophysics|January 27, 2011
Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3Jad Walters, Paul Swartz, Carla Mattos, et al.Biochemistry|October 22, 2003
An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3Kakoli Bose, Cristina Pop, Brett Feeney, et al.Biochemistry|October 22, 2003
Mutations in the procaspase-3 dimer interface affect the activity of the zymogenCristina Pop, Brett Feeney, Ashutosh Tripathy, et al.Current Opinion in Drug Discovery & Development|September 3, 2010
The potential for caspases in drug discoverySarah H MacKenzie, Joshua L Schipper, A Clay ClarkBioscience Reports|January 15, 2021
Remodeling hydrogen bond interactions results in relaxed specificity of Caspase-3Liqi Yao, Paul Swartz, Paul T Hamilton, et al.Biochemistry|October 25, 2014
Modifying caspase-3 activity by altering allosteric networksChristine Cade, Paul Swartz, Sarah H MacKenzie, et al.The Journal of Biological Chemistry|February 8, 2018
Modifications to a common phosphorylation network provide individualized control in caspasesMelvin E Thomas, Robert Grinshpon, Paul Swartz, et al.Biochemistry|November 1, 2006
Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3Brett Feeney, Cristina Pop, Paul Swartz, et al.Pageof 5