Follow
A. Clay Clark
A. Clay Clark
Department of Biology, University of Texas at Arlington
Verified email at uta.edu - Homepage
Title
Cited by
Cited by
Year
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
2152009
Death by caspase dimerization
SH MacKenzie, AC Clark
Protein dimerization and oligomerization in biology, 55-73, 2012
1472012
The potential for caspases in drug discovery
SH MacKenzie, JL Schipper, AC Clark
Current opinion in drug discovery & development 13 (5), 568, 2010
1402010
Targeting cell death in tumors by activating caspases
AC Clark, SH MacKenzie
Current cancer drug targets 8 (2), 98-109, 2008
1232008
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
1152002
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
1121993
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
952009
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
872001
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
861996
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
792003
Caspase allostery and conformational selection
AC Clark
Chemical reviews 116 (11), 6666-6706, 2016
772016
Dimeric procaspase-3 unfolds via a four-state equilibrium process
K Bose, AC Clark
Biochemistry 40 (47), 14236-14242, 2001
732001
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
682006
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
661993
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
622004
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
542003
GroEL-mediated folding of structurally homologous dihydrofolate reductases
AC Clark, C Frieden
Journal of molecular biology 268 (2), 512-525, 1997
521997
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
511997
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
452003
Reassembly of active caspase-3 is facilitated by the propeptide
B Feeney, AC Clark
Journal of Biological Chemistry 280 (48), 39772-39785, 2005
442005
The system can't perform the operation now. Try again later.
Articles 1–20