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Charles Craik
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Professor, School of Pharmacy
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Email: charles.craik@ucsf.edu
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Biography
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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Displaying 226 - 250 of 391
- Selvarajan S, Lund LR, Takeuchi T, Craik CS, Werb Z. A plasma kallikrein-dependent plasminogen cascade required for adipocyte differentiation. Nat Cell Biol. 2001 Mar; 3(3):267-75.
- Nealon K, Newcomb WW, Pray TR, Craik CS, Brown JC, Kedes DH. Lytic replication of Kaposi's sarcoma-associated herpesvirus results in the formation of multiple capsid species: isolation and molecular characterization of A, B, and C capsids from a gammaherpesvirus. J Virol. 2001 Mar; 75(6):2866-78.
- Reiling KK, Pray TR, Craik CS, Stroud RM. Functional consequences of the Kaposi's sarcoma-associated herpesvirus protease structure: regulation of activity and dimerization by conserved structural elements. Biochemistry. 2000 Oct 24; 39(42):12796-803.
- Waugh SM, Harris JL, Fletterick R, Craik CS. The structure of the pro-apoptotic protease granzyme B reveals the molecular determinants of its specificity. Nat Struct Biol. 2000 Sep; 7(9):762-5.
- Takeuchi T, Harris JL, Huang W, Yan KW, Coughlin SR, Craik CS. Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates. J Biol Chem. 2000 Aug 25; 275(34):26333-42.
- Harris JL, Backes BJ, Leonetti F, Mahrus S, Ellman JA, Craik CS. Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries. Proc Natl Acad Sci U S A. 2000 Jul 05; 97(14):7754-9.
- Gillmor SA, Takeuchi T, Yang SQ, Craik CS, Fletterick RJ. Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor of serine proteases. J Mol Biol. 2000 Jun 16; 299(4):993-1003.
- Sambrano GR, Huang W, Faruqi T, Mahrus S, Craik C, Coughlin SR. Cathepsin G activates protease-activated receptor-4 in human platelets. J Biol Chem. 2000 Mar 10; 275(10):6819-23.
- Rozzelle JE, Dauber DS, Todd S, Kelley R, Craik CS. Macromolecular inhibitors of HIV-1 protease. Characterization of designed heterodimers. J Biol Chem. 2000 Mar 10; 275(10):7080-6.
- Todd S, Anderson C, Jolly DJ, Craik CS. HIV protease as a target for retrovirus vector-mediated gene therapy. Biochim Biophys Acta. 2000 Mar 07; 1477(1-2):168-88.
- B. Wang, M. Lodder, J. Zhou, T.T. Baird, Jr., K.C. Brown, C.S. Craik, S.M. Hecht. J. Am. Chem. Soc. Chemically Mediated Site-Specific Cleavage of Proteins. 2000; 122:7402-7403.
- K.K. Reiling, T.R. Pray, C.S. Craik, R.M. Stroud. Structure: Regulation of Activity and Dimerization by Conserved Structural Elements. Biochemistry. 2000; 24:12796-803 .
- T.T. Baird Jr., B. Wang, M. Lodder, S.M. Hecht and C.S. Craik. Generation of Active Trypsin by Chemical Cleavage. Tetrahedron Letters. 2000; 556:9477-9485 .
- Brachyurins. Tsu, C., and Craik, C.S. Handbook of Proteolytic Enzymes . 2004; 2nd Ed.
- Shimba, N. Nomura, A.M., Marnett, A.B. and Craik, C.S. Herpesvirus Protease Inhibition by Dimer Disruption. J. Virol. 2004; 12(78):6657-65 .
- Stoop AA, Craik CS. Engineering of a macromolecular scaffold to develop specific protease inhibitors. Nat Biotechnol. 2003 Sep; 21(9):1063-8.
- Bell JK, Goetz DH, Mahrus S, Harris JL, Fletterick RJ, Craik CS. The oligomeric structure of human granzyme A is a determinant of its extended substrate specificity. Nat Struct Biol. 2003 Jul; 10(7):527-34.
- Shimba N, Serber Z, Ledwidge R, Miller SM, Craik CS, Dötsch V. Quantitative identification of the protonation state of histidines in vitro and in vivo. Biochemistry. 2003 Aug 05; 42(30):9227-34.
- Raymond WW, Ruggles SW, Craik CS, Caughey GH. Albumin is a substrate of human chymase. Prediction by combinatorial peptide screening and development of a selective inhibitor based on the albumin cleavage site. J Biol Chem. 2003 Sep 05; 278(36):34517-24.
- Leiting B, Pryor KD, Wu JK, Marsilio F, Patel RA, Craik CS, Ellman JA, Cummings RT, Thornberry NA. Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII. Biochem J. 2003 Apr 15; 371(Pt 2):525-32.
- Mackewicz CE, Craik CS, Levy JA. The CD8+ cell noncytotoxic anti-HIV response can be blocked by protease inhibitors. Proc Natl Acad Sci U S A. 2003 Mar 18; 100(6):3433-8.
- Sun J, Pons J, Craik CS. Potent and selective inhibition of membrane-type serine protease 1 by human single-chain antibodies. Biochemistry. 2003 Feb 04; 42(4):892-900.
- Shimba N, Stern AS, Craik CS, Hoch JC, Dötsch V. Elimination of 13Calpha splitting in protein NMR spectra by deconvolution with maximum entropy reconstruction. J Am Chem Soc. 2003 Mar 05; 125(9):2382-3.
- Bhatt AS, Takeuchi T, Ylstra B, Ginzinger D, Albertson D, Shuman MA, Craik CS. Quantitation of membrane type serine protease 1 (MT-SP1) in transformed and normal cells. Biol Chem. 2003 Feb; 384(2):257-66.
- Barrios AM, Craik CS. Scanning the prime-site substrate specificity of proteolytic enzymes: a novel assay based on ligand-enhanced lanthanide ion fluorescence. Bioorg Med Chem Lett. 2002 Dec 16; 12(24):3619-23.