A. C. Clark

发表

Evaluation of the DNA binding tendencies of the transition state regulator AbrB.

L. Benson, Stephen Naylor, M. Strauch, 2004, Biochemistry.

Targeting cell death in tumors by activating caspases.

A. C. Clark, S. Mackenzie, 2008, Current cancer drug targets.

Mutations in the procaspase-3 dimer interface affect the activity of the zymogen.

A. Tripathy, C. Pop, B. Feeney, 2003, Biochemistry.

Integration of Evolutionary Theory into Cancer Biology and Caspase Signaling

A. C. Clark, R. Grinshpon, A. C. Clark, 2019, Unravelling Cancer Signaling Pathways: A Multidisciplinary Approach.

Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3.

A. Tripathy, C. Pop, B. Feeney, 2004, The Biochemical journal.

Purification of GroEL with low fluorescence background.

Carl Frieden, A. C. Clark, R. Ramanathan, 1998, Methods in enzymology.

Caspases from scleractinian coral show unique regulatory features

L. Mydlarz, P. Swartz, A. C. Clark, 2019, The Journal of Biological Chemistry.

Allosteric modulation of caspase 3 through mutagenesis

C. Mattos, P. Swartz, A. C. Clark, 2012, Bioscience reports.

Minimizing frustration by folding in an aqueous environment.

C. Mattos, A. C. Clark, A. Clark, 2008, Archives of biochemistry and biophysics.

Folding and assembly kinetics of procaspase‐3

A. C. Clark, Sara L. Milam, 2009, Protein science : a publication of the Protein Society.

Characterization and enzymatic degradation of Sup35NM, a yeast prion‐like protein

J. Shih, A. C. Clark, Ching-Ying Chen, 2005, Protein science : a publication of the Protein Society.

Modifications to a common phosphorylation network provide individualized control in caspases.

P. Swartz, A. C. Clark, M. Thomas, 2018 .

The potential for caspases in drug discovery.

A. C. Clark, J. Schipper, S. Mackenzie, 2010, Current opinion in drug discovery & development.

Resurrection of an ancient inflammatory locus reveals switch to caspase-1 specificity on a caspase-4 scaffold

G. Salvesen, M. Poręba, S. Snipas, 2022, The Journal of biological chemistry.

Rapid folding and unfolding of Apaf-1 CARD.

C. Mattos, N. Nicely, B. Feeney, 2007, Journal of molecular biology.

Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3.

C. Mattos, P. Swartz, C. Pop, 2006, Biochemistry.

Novel protein purification system utilizing an N-terminal fusion protein and a caspase-3 cleavable linker.

E. Soderblom, M. Goshe, B. Feeney, 2006, Protein expression and purification.

Comparing the folding landscapes of evolutionarily divergent procaspase-3

A. C. Clark, Li-Zhong Yao, 2022, bioRxiv.

Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3.

C. Mattos, P. Swartz, A. C. Clark, 2011, Archives of biochemistry and biophysics.

Dimeric procaspase-3 unfolds via a four-state equilibrium process.

A. C. Clark, K. Bose, 2001, Biochemistry.

Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer.

Yun-Ru Chen, A. Tripathy, B. Bobay, 2001, Biochemistry.

Organolithium additions to allylic alcohols

A. C. Clark, J. Crandall, 1969 .

Reaction of organolithium reagents with allylic alcohols

A. C. Clark, J. Crandall, 1972 .

Reaction of sodium η-cyclopentadienyldicarbonylferrate(0) with sulfur dioxide. Synthesis of ironsulfur dioxide complexes

A. C. Clark, A. Wojcicki, P. Reich-Rohrwig, 1978 .

Tetracarbonylhydrocobalt and the hydroformylation reaction

A. C. Clark, J. Terapane, M. Orchin, 1974 .

Caspase Allostery and Conformational Selection.

A. C. Clark, A. Clay Clark, A. Clark, 2016, Chemical reviews.

Chapter 2 Caspases – Key Players in Apoptosis

A. C. Clark, C. Cade, 2019 .

Caspases – Key Players in Apoptosis

A. C. Clark, C. Cade, 2015 .

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)

A. C. Clark, I. D'Silva, Manman Chu, 2002, Molecular microbiology.

Modifications to a common phosphorylation network provide individualized control in caspases

P. Swartz, A. C. Clark, M. Thomas, 2018, The Journal of Biological Chemistry.

Resurrection of ancestral effector caspases identifies novel networks for evolution of substrate specificity

P. Swartz, A. C. Clark, R. Grinshpon, 2019, bioRxiv.

Practical approaches to protein folding and assembly: spectroscopic strategies in thermodynamics and kinetics.

A. C. Clark, Jad Walters, Sara L. Milam, 2009, Methods in enzymology.

Modifying Caspase-3 Activity by Altering Allosteric Networks

P. Swartz, A. C. Clark, S. Mackenzie, 2014, Biochemistry.

Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICK

Yun-Ru Chen, A. C. Clark, 2006, Protein science : a publication of the Protein Society.

Tunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selection

P. Swartz, A. C. Clark, J. Schipper, 2016, Proceedings of the National Academy of Sciences.

A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis

C. Mattos, G. Salvesen, P. Swartz, 2009, The Biochemical journal.

An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3.

C. Pop, B. Feeney, A. C. Clark, 2003, Biochemistry.

Conserved folding landscape of monomeric initiator caspases

A. C. Clark, Mithun Nag, 2023, bioRxiv.

Evolution of the folding landscape of effector caspases

A. C. Clark, S. Shrestha, 2021, bioRxiv.

Slow folding and assembly of a procaspase-3 interface variant.

A. C. Clark, S. Mackenzie, 2013, Biochemistry.

Death by caspase dimerization.

A. C. Clark, Sarah H MacKenzie, A Clay Clark, 2012, Advances in experimental medicine and biology.

Cooperative effects of potassium, magnesium, and magnesium‐ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL

Carl Frieden, B. Karon, A. C. Clark, 1999, Protein science : a publication of the Protein Society.

Kinetic traps in the folding/unfolding of procaspase‐1 CARD domain

Yun-Ru Chen, A. C. Clark, 2004, Protein science : a publication of the Protein Society.

Lengthening the intersubunit linker of procaspase 3 leads to constitutive activation.

P. Swartz, K. Blackburn, A. C. Clark, 2013, Biochemistry.

Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures.

Carl Frieden, A. C. Clark, 1999, Journal of molecular biology.

GroEL-mediated folding of structurally homologous dihydrofolate reductases.

Carl Frieden, A. C. Clark, 1997, Journal of molecular biology.

The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases.

Carl Frieden, A. C. Clark, 1999, Journal of molecular biology.

Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL.

Carl Frieden, A. C. Clark, E. Hugo, 1996, Biochemistry.

Protein folding: how the mechanism of GroEL action is defined by kinetics.

Carl Frieden, A. C. Clark, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Equilibrium and Kinetic Folding of a α-Helical Greek Key Protein Domain: Caspase Recruitment Domain (CARD) of RICK

Yun-Ru Chen, A. C. Clark, 2003 .

Equilibrium and kinetic folding of an alpha-helical Greek key protein domain: caspase recruitment domain (CARD) of RICK.

Yun-Ru Chen, A. C. Clark, 2003, Biochemistry.

A bifunctional allosteric site in the dimer interface of procaspase-3.

A. C. Clark, J. Schipper, S. Mackenzie, 2011, Biophysical chemistry.

Reassembly of Active Caspase-3 Is Facilitated by the Propeptide*

B. Feeney, A. C. Clark, 2005, Journal of Biological Chemistry.

The C-terminal tail of Arabidopsis 14-3-3omega functions as an autoinhibitor and may contain a tenth alpha-helix.

S. Huber, A. C. Clark, W. Shen, 2003, The Plant journal : for cell and molecular biology.

Remodeling hydrogen bond interactions results in relaxed specificity of Caspase-3

P. Swartz, A. C. Clark, P. Hamilton, 2020, bioRxiv.

Kinetic destabilization of the hydroperoxy flavin intermediate by site-directed modification of the reactive thiol in bacterial luciferase.

F. Raushel, T. Baldwin, A. C. Clark, 1993, The Journal of biological chemistry.

Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits.

T. Baldwin, A. C. Clark, J. Sinclair, 1993, The Journal of biological chemistry.

pH effects on the stability and dimerization of procaspase‐3

A. C. Clark, K. Bose, 2005, Protein science : a publication of the Protein Society.

A rapid chromatographic method to separate the subunits of bacterial luciferase in urea-containing buffer.

T. Baldwin, B. Noland, A. C. Clark, 2000, Methods in enzymology.

Sequential unfolding mechanisms of monomeric caspases

A. C. Clark, Isha Joglekar, 2023, bioRxiv.

Effect of p-methoxybenzonitrile on the course of the stoichiometric hydroformylation of cyclopentene

A. C. Clark, M. Orchin, 1973 .