Published in Biochemistry on May 27, 2003
Protein folding: then and now. Arch Biochem Biophys (2007) 1.18
Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICK. Protein Sci (2006) 0.91
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain. Protein Sci (2004) 0.87
Topology is the principal determinant in the folding of a complex all-alpha Greek key death domain from human FADD. J Mol Biol (2009) 0.86
Rapid folding and unfolding of Apaf-1 CARD. J Mol Biol (2007) 0.83
Interaction between soluble and membrane-embedded potassium channel peptides monitored by Fourier transform infrared spectroscopy. PLoS One (2012) 0.77
Folding of an all-helical Greek-key protein monitored by quenched-flow hydrogen-deuterium exchange and NMR spectroscopy. Eur Biophys J (2011) 0.77
Woes of proline: a cautionary kinetic tale. Protein Sci (2006) 0.75
An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3. Biochemistry (2003) 1.39
A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis. Biochem J (2009) 1.33
CpeR is an activator required for expression of the phycoerythrin operon (cpeBA) in the cyanobacterium Fremyella diplosiphon and is encoded in the phycoerythrin linker-polypeptide operon (cpeCDESTR). Mol Microbiol (2002) 1.16
Evaluation of the DNA binding tendencies of the transition state regulator AbrB. Biochemistry (2004) 1.16
Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3. Biochemistry (2006) 1.12
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen. Biochemistry (2003) 1.11
Targeting cell death in tumors by activating caspases. Curr Cancer Drug Targets (2008) 1.10
Death by caspase dimerization. Adv Exp Med Biol (2012) 1.04
Reassembly of active caspase-3 is facilitated by the propeptide. J Biol Chem (2005) 1.03
Practical approaches to protein folding and assembly: spectroscopic strategies in thermodynamics and kinetics. Methods Enzymol (2009) 0.96
pH effects on the stability and dimerization of procaspase-3. Protein Sci (2004) 0.96
Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3. Biochem J (2004) 0.95
Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICK. Protein Sci (2006) 0.91
The C-terminal tail of Arabidopsis 14-3-3omega functions as an autoinhibitor and may contain a tenth alpha-helix. Plant J (2003) 0.88
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain. Protein Sci (2004) 0.87
The potential for caspases in drug discovery. Curr Opin Drug Discov Devel (2010) 0.86
Protein folding: are we there yet? Arch Biochem Biophys (2008) 0.84
Novel protein purification system utilizing an N-terminal fusion protein and a caspase-3 cleavable linker. Protein Expr Purif (2005) 0.84
Allosteric modulation of caspase 3 through mutagenesis. Biosci Rep (2012) 0.84
Rapid folding and unfolding of Apaf-1 CARD. J Mol Biol (2007) 0.83
A bifunctional allosteric site in the dimer interface of procaspase-3. Biophys Chem (2011) 0.83
Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3. Arch Biochem Biophys (2011) 0.80
Minimizing frustration by folding in an aqueous environment. Arch Biochem Biophys (2007) 0.80
Lengthening the intersubunit linker of procaspase 3 leads to constitutive activation. Biochemistry (2013) 0.80
Folding and assembly kinetics of procaspase-3. Protein Sci (2009) 0.78
Modifying caspase-3 activity by altering allosteric networks. Biochemistry (2014) 0.78
Slow folding and assembly of a procaspase-3 interface variant. Biochemistry (2013) 0.77
Redesigning the procaspase-8 dimer interface for improved dimerization. Protein Sci (2014) 0.75
Characterization and enzymatic degradation of Sup35NM, a yeast prion-like protein. Protein Sci (2005) 0.75