Charles Craik

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Charles Craik

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Professor, School of Pharmacy
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My research interests focus on defining the roles and the mechanisms of enzymes and other challenging proteins in complex biological processes and on developing technologies to facilitate these studies. The current research in the Craik lab focuses on the chemical biology of proteolytic and protein degradation enzymes, receptors and membrane transporters. A particular emphasis of our work is on identifying the roles and regulating the activity of key proteins associated with infectious diseases, neurodegeneration and cancer. I am also interested in developing novel methods to biophysically characterize challenging proteins as well as their complexes. These studies coupled with our global substrate profiling, antibody engineering and noninvasive imaging efforts are providing a better understanding of both the chemical make-up and the biological importance of these critical proteins to aid in the rapid detection, monitoring and control of infectious disease, neurological disorders and cancer. This in turn is leading to the development of strategies for regulating these activities as a means of therapeutic intervention. Further study of these proteins holds promise for better understanding, rapid detection and eventual control of infectious diseases, cancer and neurodegeneration.
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  1. W.S. Willett, L.S. Brinen, R.J. Fletterick & C.S. Craik. Delocalizing Trypsin Specificity with Metal-Activation. Biochem; 35. 1996; 5992-5998.
    http://www.ncbi.nlm.nih.gov/pubmed/8448149
  2. E. Rutenber, E.B. Fauman, R.J. Keenan, S. Fong, P.S. Furth, P.R. Ortiz de Montellano, E. Meng, I.D. Kuntz, D.L. DeCamp, R. Salto, J.R. Rosé, C.S. Craik, R.M. Stroud. . J. Bio. Chem. Structure of a Non-Peptide Inhibitor Complexed with HIV-1 Protease: Developing a Cycle of Structure-Based Drug Design. 1993; 15343-15346.
  3. Z. Sui, J. DeVoss, D. DeCamp, J. Li, C.S. Craik & P.R. Ortiz de Montellano. Synthesis. Synthesis of Haloperidol Ethanedithioketal HIV-1 Protease Inhibitors: Magnesium Chloride Facilitated Addition of Grignard Reagents. 1993; 8:803-808.
  4. D.L. Decamp, S.B. Kahl & C.S. Craik. Boronated Porphyrins—A New Class of HIV Proteinase Inhibitors. Intl. Antiviral News 1. 1993; 19-20 .
  5. J.J. Perona, C.A. Tsu, M.E. McGrath, C.S. Craik & R.J. Fletterick. Relocating a Negative Charge in the Binding Pocket of Trypsin. J. Mol. Bio. 230. 1993; 934-949.
  6. T.K. Sawyer, J.F. Fisher, J.B. Hester, C.W. Smith, A.G. Tomasselli, W.G. Tarpley, P.S. Burton, J.O. Hui T.J. McQuade, R.A. Conradi, V.S. Bradford, L. Liu, J.H. Kinner, J.Tustin,D.L. Alexander, A.W. Harrison, D.E. Emmert, D.J. Staples, L.I. Maggira, Y.Z. Zhang, R.A. Poorman, BM. Dunn, C. Rao, .E. Scarborough, W.T. Lowther, C.S. Craik, D. DeCamp, J.Moon, W.H. Howe & R.L. Heinrikson. Peptidomimetic Inhibitors of Human Immunodeficiency Virus Protease (HIV-PR): Design, Enzyme Binding and Selectivity, Antiviral Efficacy and Cell Permeability Properties. Bioorg. Med. Chem. Letts 3. 1993; 819-824 .
  7. Z. Sui, R. Salto, C.S. Craik, P. Ortiz de Montellano. Inhibition of the HIV1 and the HIV2 Proteases by Curcumin and Curcumin Boron Complexes. Bioorg. & Med. Chem. Let. 1 . 1993; 415-422 .
  8. McGrath ME, Eakin AE, Engel JC, McKerrow JH, Craik CS, Fletterick RJ. The crystal structure of cruzain: a therapeutic target for Chagas' disease. J Mol Biol. 1995 Mar 24; 247(2):251-9.
    http://www.ncbi.nlm.nih.gov/pubmed/1338945
  9. Sloane DL, Leung R, Barnett J, Craik CS, Sigal E. Conversion of human 15-lipoxygenase to an efficient 12-lipoxygenase: the side-chain geometry of amino acids 417 and 418 determine positional specificity. Protein Eng. 1995 Mar; 8(3):275-82.
    http://www.ncbi.nlm.nih.gov/pubmed/1527792
  10. Perona JJ, Craik CS. Structural basis of substrate specificity in the serine proteases. Protein Sci. 1995 Mar; 4(3):337-60.
    http://www.ncbi.nlm.nih.gov/pubmed/1559982
  11. Willett WS, Gillmor SA, Perona JJ, Fletterick RJ, Craik CS. Engineered metal regulation of trypsin specificity. Biochemistry. 1995 Feb 21; 34(7):2172-80.
    http://www.ncbi.nlm.nih.gov/pubmed/1554694
  12. A.E. Eakin, J.H. McKerrow & C.S.Craik. A Cysteine Protease is a Target for the Enzyme Structure-based Design of Antiparasitic Drugs. Drug Information Journal 29. 1995; 29:1501S-1517S.
    http://www.ncbi.nlm.nih.gov/pubmed/1329276
  13. Rosé JR, Craik CS. Structure-assisted design of nonpeptide human immunodeficiency virus-1 protease inhibitors. Am J Respir Crit Care Med. 1994 Dec; 150(6 Pt 2):S176-82.
    http://www.ncbi.nlm.nih.gov/pubmed/1537814
  14. T.K. Sawyer, D.J. Staples, L. Liu, A.G. Tomasselli, J.O. Hui, K. O’Connell, H. Schostarez, J.B. Hester, J. Moon, W.J. Howe, C.W. Smith, D. L. DeCamp, C.S. Craik, B.M. Dunn,W. T. Lowther, J. Harris, R.A. Poorman, A. Wlodawer, M. Jaskolski & R.L. Heinrikson. . Int. J. Pep. Protein Res. HIV Protease (HIV PR) Inhibitor Structure-Activity-Selectivity and Active Site Molecular Modeling of High Affinity Leu [CH(OH)CH2] Val Modified Viral and Nonviral Substrate Analogs. 1992; 274-281 .
  15. D.R. Corey, M.E. McGrath, J.R. Vasquez, R.J. Fletterick & C.S. Craik. An Alternate Geometry for the Catalytic Triad of Serine Proteases. J. Amer. Chem. Soc. 114. 1992; 4906-4907 .
  16. Tsu CA, Perona JJ, Schellenberger V, Turck CW, Craik CS. The substrate specificity of Uca pugilator collagenolytic serine protease 1 correlates with the bovine type I collagen cleavage sites. J Biol Chem. 1994 Jul 29; 269(30):19565-72.
    http://www.ncbi.nlm.nih.gov/pubmed/1944593
  17. Matthews BW, Craik CS, Neurath H. Can small cyclic peptides have the activity and specificity of proteolytic enzymes? Proc Natl Acad Sci U S A. 1994 May 10; 91(10):4103-5.
    http://www.ncbi.nlm.nih.gov/pubmed/1904942
  18. Salto R, Babé LM, Li J, Rosé JR, Yu Z, Burlingame A, De Voss JJ, Sui Z, Ortiz de Montellano P, Craik CS. In vitro characterization of nonpeptide irreversible inhibitors of HIV proteases. J Biol Chem. 1994 Apr 08; 269(14):10691-8.
    http://www.ncbi.nlm.nih.gov/pubmed/2051486
  19. Perona JJ, Hedstrom L, Wagner RL, Rutter WJ, Craik CS, Fletterick RJ. Exogenous acetate reconstitutes the enzymatic activity of trypsin Asp189Ser. Biochemistry. 1994 Mar 22; 33(11):3252-9.
    http://www.ncbi.nlm.nih.gov/pubmed/2007606
  20. De Voss JJ, Sui Z, DeCamp DL, Salto R, Babé LM, Craik CS, Ortiz de Montellano PR. Haloperidol-based irreversible inhibitors of the HIV-1 and HIV-2 proteases. J Med Chem. 1994 Mar 04; 37(5):665-73.
    http://www.ncbi.nlm.nih.gov/pubmed/1988010
  21. Gudmundsdóttir A, Gudmundsdóttir E, Oskarsson S, Bjarnason JB, Eakin AK, Craik CS. Isolation and characterization of cDNAs from Atlantic cod encoding two different forms of trypsinogen. Eur J Biochem. 1993 Nov 01; 217(3):1091-7.
    http://www.ncbi.nlm.nih.gov/pubmed/1881877
  22. D.L. Sloane, R. Leung, C.S. Craik & E. Sigal. A Primary Determinant for Lipoxygenase Postional Specificity. Nature 354, 149-152. 1991.
  23. D.L. DeCamp, L.M. Babé, P. Furth, P. Ortiz de Montellano, I.D. Kuntz & C.S. Craik. Adv. Exptl. Med. Bio. Structure-based inhibition of HIV-1 protease activity and viral infectivity. 1991; 306:489-492 .
  24. Perona JJ, Tsu CA, Craik CS, Fletterick RJ. Crystal structures of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI. J Mol Biol. 1993 Apr 05; 230(3):919-33.
    http://www.ncbi.nlm.nih.gov/pubmed/2062825
  25. Perona JJ, Evnin LB, Craik CS. A genetic selection elucidates structural determinants of arginine versus lysine specificity in trypsin. Gene. 1993 Dec 27; 137(1):121-6.
    http://www.ncbi.nlm.nih.gov/pubmed/1825549