A. Clay Clark

Raleigh, North Carolina, USA

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Mailing Address:

   Dr. A. Clay Clark
   Associate Professor
   128 Polk Hall, CB 7622
   Department of Molecular
       & Structural Biochemistry
   NC State University
   Raleigh, NC 27695-7622

   Send Email: Clay Clark

  Lab: Rooms 339 & 341 Polk Hall
  Office: Room 339A Polk Hall

  919-515-5805 (office)
  919-515-5806 (lab)
  919-515-2047 (fax)

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

Publications

  1. MacKenzie, Sarah H. & A. Clay Clark (2008) Targeting cell death in tumors by activating caspases. Current Cancer Drug Targets, in press.

  2. MacKenzie, Sarah H. & A. Clay Clark (2008) Death by caspase dimerization, in Protein Dimerization (and Oligomerization) in Biology, J. Matthews, ed., Landes Bioscience, in press.

  3. Clark, A. Clay (2008) Protein folding: Are we there yet?. Archives of Biochemistry and Biophysics 469, 1-3.

  4. Mattos, Carla & A. Clay Clark (2008) Minimizing frustration by folding in an aqueous environment. Archives of Biochemistry and Biophysics 469, 118-131.

  5. Milam, Sara L., Nathan I. Nicely, Brett Feeney, Carla Mattos & A. Clay Clark (2007) Rapid folding and unfolding of APAF-1 CARD. Journal of Molecular Biology 369, 290-304.

  6. Feeney, Brett, Cristina Pop, Paul Swartz, Carla Mattos & A. Clay Clark (2006) Role of loop bundle hydrogen bonds in the maturation and activity of (pro)caspase-3. Biochemistry 45, 13249-13263.

  7. Chen, Yun-Ru & A. Clay Clark (2006) Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICK. Protein Science 15, 395-409.

  8. Feeney, Brett, Erik J. Soderblom, Michael B. Goshe & A. Clay Clark (2006) Novel protein purification system utilizing an N-terminal fusion protein and a caspase-3 cleavable linker. Protein Expression and Purification 47, 311-318.

  9. Feeney, Brett & A. Clay Clark (2005) Reassembly of active caspase-3 is facilitated by the pro-peptide. J. Biol. Chem. 280, 39772-39785.

  10. Chen, Ching-Ying, Kawan Rojanatavorn, A. Clay Clark & Jason C. H. Shih (2005) Characterization and enzymatic degradation of Sup35NM, a yeast prion-like protein. Protein Science 14, 2228-2235.

  11. Bose, K. & A. Clay Clark (2005) pH effects on the stability and dimerization of procaspase-3. Protein Science 14, 24-36.

  12. Bobay, Benjamin B., Linda Benson, Steven Naylor, Brett Feeney, A. Clay Clark, Mark A. Strauch, Richele Thompson & John Cavanagh (2004) Evaluation of the DNA binding tendencies of the transition state regulator AbrB. Biochemistry 43, 16106-16118.

  13. Feeney, Brett, Cristina Pop, Ashutosh Tripathy & A. Clay Clark (2004) Ionic interactions near loop L4 are important for maintaining the active site environment and the dimer stability of (pro)caspase-3. Biochemical Journal 384, 515-525.

  14. Chen, Yun-Ru & A. Clay Clark (2004) Kinetic traps in the folding/unfolding of procaspase-1 CARD domain. Protein Science 13, 2196-2206.

  15. Bose, Kakoli, Cristina Pop, Brett Feeney & A. Clay Clark (2003) An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3. Biochemistry 42, 12298-12310.

  16. Pop, Cristina, Brett Feeney, Ashutosh Tripathy & A. Clay Clark (2003) Mutations in the procaspase-3 dimer interface affect the activity of the zymogen. Biochemistry 42,12311-12320.

  17. Chen, Yun-Ru & A. Clay Clark (2003) Equilibrium and kinetic folding of a a-helical Greek key protein domain: caspase recruitment domain (CARD) of RICK. Biochemistry 42, 6310-6320.

  18. Shen, Wei, A. Clay Clark & Steven C. Huber (2003) The C-terminal tail of Arabidopsis 14-3-3w functions as an autoinhibitor and may contain a tenth a-helix. The Plant Journal 34, 473-484.

  19. Cobley, J.G, A.C. Clark, W. Weerasurya, F.A. Queseda, J.Y. Xiao, N. Bandrapali, I. D'Silva, M. Thounaojam, J.F. Oda, T. Sumiyoshi (2002) CpeR is an activator required for expression of the phycoerythrin operon (cpeBA) in the chromatically-adapting cyanobacterium, Fremyella diplosiphon. Molecular Microbiology 44, 1517-1531.

  20. C. Pop, Y-R. Chen, B. Smith, K. Bose, B. Bobay, A. Tripathy, S. Franzen, & A.C Clark (2001) Removal of the Pro-domain Does Not Affect the Conformation of the Procaspase-3 Dimer. Biochemistry 40, 14224-14235.

  21. Bose, Kakoli & A. Clay Clark (2001) Dimeric Procaspase-3 Unfolds via a Four-State Equilibrium Process. Biochemistry 40, 14236-14242.