A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis J Walters, C Pop, FL Scott, M Drag, P Swartz, C Mattos, GS Salvesen, ... Biochemical Journal 424 (3), 335-345, 2009 | 215 | 2009 |
Death by caspase dimerization SH MacKenzie, AC Clark Protein dimerization and oligomerization in biology, 55-73, 2012 | 147 | 2012 |
The potential for caspases in drug discovery SH MacKenzie, JL Schipper, AC Clark Current opinion in drug discovery & development 13 (5), 568, 2010 | 140 | 2010 |
Targeting cell death in tumors by activating caspases AC Clark, SH MacKenzie Current cancer drug targets 8 (2), 98-109, 2008 | 123 | 2008 |
CpeR is an activator required for expression of the phycoerythrin operon (cpeBA) in the cyanobacterium Fremyella diplosiphon and is encoded in the phycoerythrin linker … JG Cobley, AC Clark, S Weerasurya, FA Queseda, JY Xiao, N Bandrapali, ... Molecular microbiology 44 (6), 1517-1531, 2002 | 115 | 2002 |
Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits AC Clark, JF Sinclair, TO Baldwin Journal of Biological Chemistry 268 (15), 10773-10779, 1993 | 112 | 1993 |
Practical approaches to protein folding and assembly: spectroscopic strategies in thermodynamics and kinetics J Walters, SL Milam, AC Clark Methods in enzymology 455, 1-39, 2009 | 95 | 2009 |
Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer C Pop, YR Chen, B Smith, K Bose, B Bobay, A Tripathy, S Franzen, ... Biochemistry 40 (47), 14224-14235, 2001 | 87 | 2001 |
Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL AC Clark, E Hugo, C Frieden Biochemistry 35 (18), 5893-5901, 1996 | 86 | 1996 |
An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3 K Bose, C Pop, B Feeney, AC Clark Biochemistry 42 (42), 12298-12310, 2003 | 79 | 2003 |
Caspase allostery and conformational selection AC Clark Chemical reviews 116 (11), 6666-6706, 2016 | 77 | 2016 |
Dimeric procaspase-3 unfolds via a four-state equilibrium process K Bose, AC Clark Biochemistry 40 (47), 14236-14242, 2001 | 73 | 2001 |
Role of loop bundle hydrogen bonds in the maturation and activity of (Pro) caspase-3 B Feeney, C Pop, P Swartz, C Mattos, AC Clark Biochemistry 45 (44), 13249-13263, 2006 | 68 | 2006 |
Kinetic destabilization of the hydroperoxy flavin intermediate by site-directed modification of the reactive thiol in bacterial luciferase. HM Abu-Soud, AC Clark, WA Francisco, TO Baldwin, FM Raushel Journal of Biological Chemistry 268 (11), 7699-7706, 1993 | 66 | 1993 |
Evaluation of the DNA binding tendencies of the transition state regulator AbrB BG Bobay, L Benson, S Naylor, B Feeney, AC Clark, MB Goshe, ... Biochemistry 43 (51), 16106-16118, 2004 | 62 | 2004 |
Mutations in the procaspase-3 dimer interface affect the activity of the zymogen C Pop, B Feeney, A Tripathy, AC Clark Biochemistry 42 (42), 12311-12320, 2003 | 54 | 2003 |
GroEL-mediated folding of structurally homologous dihydrofolate reductases AC Clark, C Frieden Journal of molecular biology 268 (2), 512-525, 1997 | 52 | 1997 |
Kinetic mechanism of luciferase subunit folding and assembly AC Clark, SW Raso, JF Sinclair, MM Ziegler, AF Chaffotte, TO Baldwin Biochemistry 36 (7), 1891-1899, 1997 | 51 | 1997 |
The C‐terminal tail of Arabidopsis 14‐3‐3ω functions as an autoinhibitor and may contain a tenth α‐helix W Shen, AC Clark, SC Huber The Plant Journal 34 (4), 473-484, 2003 | 45 | 2003 |
Reassembly of active caspase-3 is facilitated by the propeptide B Feeney, AC Clark Journal of Biological Chemistry 280 (48), 39772-39785, 2005 | 44 | 2005 |