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Charles Craik, PhD

TitleProfessor
SchoolUCSF School of Pharmacy
DepartmentPharmaceutical Chemistry
Address600 16th St
San Francisco CA 94158
Phone415-476-8146
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    Collapse Biography 
    Collapse Awards and Honors
    National Honor Society1972  - 1975Alden Scholar
    Phi Beta Kappa1974  - 1975Doane Distinguished Scholar
    1975  - 1975Richard Edwin Lee Scholar
    The Amer. Assoc. for the Advan. of Science1978  - 1978Member, The Amer. Chem. Soc
    American Cancer Society 1982  - 1983Postdoctoral Fellow
    American Society of Biological Chemists1983  - 1983Member
    National Institutes of Health1983  - 1984Postdoctoral Fellow
    Science Digest1985  - 1986Top 100 Innovators
    BioTechniques1987  - 1997Editorial Board Member
    DNA1988  - 1988Editorial Board Member
    Protein Engineering1988  - 1988Associate Editor
    Applied Biocatalysis1989  - 1989Editorial Board Member
    Member, The Protein Society1989  - 1990Nominating Committee
    Sigma Xi1991  - 1994Distinguished Lecturer
    National Science Foundation Molecular Biochemistry1993  - 1996Advisory Panel
    Gordon Conference on Proteolytic Enzymes and Inhibitors1996  - 1996Vice Chair
    Gordon Conference on Proteolytic Enzymes and Inhibitors1998  - 1998Chair
    Cold Spring Harbor Meeting on the Biology of Proteolysis1997  - 1997Co-organizer
    Cold Spring Harbor Meeting on the Biology of Proteolysis1999  - 1999Co-organizer
    Cold Spring Harbor Meeting on the Biology of Proteolysis2001  - 2001Co-organizer
    Immunex Corporation (Seattle, WA)2000  - 2000POSH Lecturer
    United States Pharmacopeia2009Council of Experts
    Allegheney College (Meadville, PA)2010  - 2010Lord Lecturer
    American Association for the Advancement of Science2011  - 2011Fellow
    Institute of Organic Chemistry and Biochemistry, Academy of Sciences, Prague, Czech Republic2013  - 2013Institute Medal Lecture and Award

    Collapse Overview 
    Collapse Overview
    My research focuses on structure-function analysis of proteases and their inhibitors. In my lab we use a combination of genetic, biochemical, and biophysical methods, with particular emphasis on identifying the roles and regulating the activity of proteases associated with infectious diseases, cancer, and development.

    Proteases are directly or indirectly involved in virtually every biological function or dysfunction. The omnipresence of proteases and their natural inhibitors has placed them among the most studied proteins in biochemistry. The research efforts of the lab focus primarily on the structure-function analysis of proteases and their inhibitors using a combination of genetic, biochemical and biophysical methods. Chemical biological approaches are used or are being developed to study the substrate specificity, catalytic mechanism and biological role of proteases and their macromolecular inhibitors. The genes for serine (trypsin, serine collagenase, easter, prostate specific antigen, T-cell specific granzymes, MT-SP1 and 2, KSHV protease), cysteine (cruzain and falcipain) and aspartyl (HIV1 & HIV2 & SIV) proteases and macromolecular inhibitors such as ecotin and single chain antibodies are manipulated and expressed in heterologous expression systems. Targeted, region specific or random substitutions are introduced recombinantly to create variants that provide insight into the structure and activity of the target protein. A particular emphasis of our work is on identifying the roles and regulating the activity of proteases associated with infectious diseases, cancer and development. These studies are providing a better understanding of both the chemical make-up and the biological importance of these critical proteins. This in turn is leading to the development of strategies for regulating proteolytic activity as a means of therapeutic intervention. Further study of these proteins holds promise for better understanding, rapid detection and eventual control of infectious diseases and cancer.


    Collapse Research 
    Collapse Research Activities and Funding
    Mapping the conformational cycle of transmembrane transporters
    NIH/NIGMS P01GM111126Aug 1, 2015 - Jul 31, 2020
    Role: Co-Investigator
    Non-invasive Differentiation of Benign Lesions from Aggressive Pancreatic Cancer
    NIH/NCI R21CA185689Jan 1, 2015 - Dec 31, 2016
    Role: Principal Investigator
    Antibody Research Technology Center
    NIH/NCI P41CA196276Sep 24, 2014 - Aug 31, 2019
    Role: Co-Investigator
    Extracellular Proteolysis as a Molecular Stratification Tool for Cancer
    NIH/NCI R21CA186077Apr 1, 2014 - Mar 31, 2016
    Role: Principal Investigator
    Allosteric Inhibition of a Family of Proteolytic Enzymes
    NIH/NIGMS R01GM104659Jul 10, 2013 - Mar 31, 2017
    Role: Principal Investigator
    A Technological Platform for the Identification of Serine Proteases in Cancer
    NIH/NCI R01CA128765Jul 17, 2009 - Jun 30, 2014
    Role: Principal Investigator
    HARC Center: HIV Accessory and Regulatory Complexes
    NIH/NIGMS P50GM082250Aug 27, 2007 - Aug 31, 2017
    Role: Co-Investigator
    Targeting Allosteric Studies to Modulate Protein Interactions and Function
    NIH/NIAID R01AI067423Apr 17, 2007 - Mar 31, 2012
    Role: Principal Investigator
    Research Training in Chemistry and Chemical Biology
    NIH/NIGMS T32GM064337Jul 1, 2002 - Jun 30, 2017
    Role: Principal Investigator
    SFSU/UCSF Comprehensive Cancer Partnership Program
    NIH/NCI U56CA096216Jul 1, 2002 - Jun 30, 2010
    Role: Co-Investigator
    Structure Biology and Targeted Drug Design for AIDS
    NIH/NIGMS P01GM056531Sep 1, 1997 - Aug 31, 2007
    Role: Co-Investigator
    Proteases in Cancer Biology and Drug Development
    NIH/NCI P01CA072006Jun 10, 1997 - Jun 30, 2010
    Role: Co-Principal Investigator
    Targeting Cysteine Proteases: Antiparasitic Chemotherapy
    NIH P01AI035707May 1, 1995 - May 31, 2010
    Role: Co-Investigator
    STRUCTURAL BIOLOGY AND TARGETED DRUG DESIGN FOR AIDS
    NIH/NIGMS P01GM039552Sep 1, 1987 - Aug 31, 1997
    Role: Principal Investigator
    Bio-Organic Biomedical Mass Spectrometry Resource
    NIH P41RR001614Mar 1, 1982 - May 31, 2015
    Role: Co-Investigator
    Resource for Biocomputing, Visualization, and Informatics
    NIH/NCRR P41RR001081Jun 1, 1976 - Sep 14, 2012
    Role: Co-Investigator

    Collapse ORNG Applications 
    Collapse Websites
    Collapse In The News
    Collapse Global Health

    Collapse Bibliographic 
    Collapse Publications
    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Researchers can login to make corrections and additions, or contact us for help.
    List All   |   Timeline
    1. Meyer NO, O'Donoghue AJ, Schulze-Gahmen U, Ravalin M, Moss SM, Winter MB, Knudsen GM, Craik C. Multiplex Substrate Profiling by Mass Spectrometry for Kinases Reveals Quantitative Substrate Motifs. Anal Chem. 2017 Mar 21. PMID: 28322550.
      View in: PubMed
    2. Guo CJ, Chang FY, Wyche TP, Backus KM, Acker TM, Funabashi M, Taketani M, Donia MS, Nayfach S, Pollard KS, Craik C, Cravatt BF, Clardy J, Voigt CA, Fischbach MA. Discovery of Reactive Microbiota-Derived Metabolites that Inhibit Host Proteases. Cell. 2017 Jan 26; 168(3):517-526.e18. PMID: 28111075.
      View in: PubMed
    3. Clarke SC, Dumesic PA, Homer CM, O'Donoghue AJ, La Greca F, Pallova L, Majer P, Madhani HD, Craik CS. Integrated Activity and Genetic Profiling of Secreted Peptidases in Cryptococcus neoformans Reveals an Aspartyl Peptidase Required for Low pH Survival and Virulence. PLoS Pathog. 2016 Dec; 12(12):e1006051. PMID: 27977806.
      View in: PubMed
    4. Winter MB, Salcedo EC, Lohse MB, Hartooni N, Gulati M, Sanchez H, Takagi J, Hube B, Andes DR, Johnson AD, Craik C, Nobile CJ. Global Identification of Biofilm-Specific Proteolysis in Candida albicans. MBio. 2016; 7(5). PMID: 27624133.
      View in: PubMed
    5. O'Donoghue AJ, Ivry SL, Chaudhury C, Hostetter DR, Hanahan D, Craik CS. Procathepsin E is highly abundant but minimally active in pancreatic ductal adenocarcinoma tumors. Biol Chem. 2016 Sep 1; 397(9):871-81. PMID: 27149201.
      View in: PubMed
    6. Goupil LS, Ivry SL, Hsieh I, Suzuki BM, Craik CS, O'Donoghue AJ, McKerrow JH. Cysteine and Aspartyl Proteases Contribute to Protein Digestion in the Gut of Freshwater Planaria. PLoS Negl Trop Dis. 2016 Aug; 10(8):e0004893. PMID: 27501047.
      View in: PubMed
    7. Duan C, Alibakhshi MA, Kim DK, Brown CM, Craik CS, Majumdar A. Label-Free Electrical Detection of Enzymatic Reactions in Nanochannels. ACS Nano. 2016 Aug 23; 10(8):7476-84. PMID: 27472431.
      View in: PubMed
    8. Lentz CS, Ordonez AA, Kasperkiewicz P, La Greca F, O'Donoghue AJ, Schulze CJ, Powers JC, Craik CS, Drag M, Jain SK, Bogyo M. Design of Selective Substrates and Activity-Based Probes for Hydrolase Important for Pathogenesis 1 (HIP1) from Mycobacterium tuberculosis. ACS Infect Dis. 2016 Nov 11; 2(11):807-815. PMID: 27739665.
      View in: PubMed
    9. Homer CM, Summers DK, Goranov AI, Clarke SC, Wiesner DL, Diedrich JK, Moresco JJ, Toffaletti D, Upadhya R, Caradonna I, Petnic S, Pessino V, Cuomo CA, Lodge JK, Perfect J, Yates JR, Nielsen K, Craik CS, Madhani HD. Intracellular Action of a Secreted Peptide Required for Fungal Virulence. Cell Host Microbe. 2016 Jun 8; 19(6):849-64. PMID: 27212659.
      View in: PubMed
    10. Le Gall SM, Szabo R, Lee M, Kirchhofer D, Craik CS, Bugge TH, Camerer E. Matriptase activation connects tissue factor-dependent coagulation initiation to epithelial proteolysis and signaling. Blood. 2016 Jun 23; 127(25):3260-9. PMID: 27114461.
      View in: PubMed
    11. Drake CR, Sevillano N, Truillet C, Craik C, VanBrocklin HF, Evans MJ. Site-Specific Radiofluorination of Biomolecules with 8-[(18)F]-Fluorooctanoic Acid Catalyzed by Lipoic Acid Ligase. ACS Chem Biol. 2016 Jun 17; 11(6):1587-94. PMID: 27008570.
      View in: PubMed
    12. Julien O, Zhuang M, Wiita AP, O'Donoghue AJ, Knudsen GM, Craik C, Wells JA. Quantitative MS-based enzymology of caspases reveals distinct protein substrate specificities, hierarchies, and cellular roles. Proc Natl Acad Sci U S A. 2016 Apr 5; 113(14):E2001-10. PMID: 27006500.
      View in: PubMed
    13. Li H, O'Donoghue AJ, van der Linden WA, Xie SC, Yoo E, Foe IT, Tilley L, Craik CS, da Fonseca PC, Bogyo M. Structure- and function-based design of Plasmodium-selective proteasome inhibitors. Nature. 2016 Feb 10; 530(7589):233-6. PMID: 26863983.
      View in: PubMed
    14. Gable JE, Lee GM, Acker TM, Hulce KR, Gonzalez ER, Schweigler P, Melkko S, Farady CJ, Craik C. Fragment-Based Protein-Protein Interaction Antagonists of a Viral Dimeric Protease. ChemMedChem. 2016 Apr 19; 11(8):862-9. PMID: 26822284.
      View in: PubMed
    15. Bibo-Verdugo B, O'Donoghue AJ, Rojo-Arreola L, Craik CS, García-Carreño F. Complementary Proteomic and Biochemical Analysis of Peptidases in Lobster Gastric Juice Uncovers the Functional Role of Individual Enzymes in Food Digestion. Mar Biotechnol (NY). 2016 Apr; 18(2):201-14. PMID: 26613762.
      View in: PubMed
    16. Jones SK, Clarke SC, Craik CS, Bennett RJ. Evolutionary Selection on Barrier Activity: Bar1 Is an Aspartyl Protease with Novel Substrate Specificity. MBio. 2015; 6(6). PMID: 26604258.
      View in: PubMed
    17. Wong KR, Menendez E, Craik CS, Kavanaugh WM, Vasiljeva O. In vivo imaging of protease activity by Probody therapeutic activation. Biochimie. 2016 Mar; 122:62-7. PMID: 26546838.
      View in: PubMed
    18. Page MJ, Lourenço AL, David T, LeBeau AM, Cattaruzza F, Castro HC, VanBrocklin HF, Coughlin SR, Craik CS. Non-invasive imaging and cellular tracking of pulmonary emboli by near-infrared fluorescence and positron-emission tomography. Nat Commun. 2015; 6:8448. PMID: 26423607; PMCID: PMC4593073.
    19. Dvorák J, Fajtová P, Ulrychová L, Leontovyc A, Rojo-Arreola L, Suzuki BM, Horn M, Mareš M, Craik CS, Caffrey CR, O'Donoghue AJ. Excretion/secretion products from Schistosoma mansoni adults, eggs and schistosomula have unique peptidase specificity profiles. Biochimie. 2016 Mar; 122:99-109. PMID: 26409899.
      View in: PubMed
    20. O'Donoghue AJ, Knudsen GM, Beekman C, Perry JA, Johnson AD, DeRisi JL, Craik CS, Bennett RJ. Destructin-1 is a collagen-degrading endopeptidase secreted by Pseudogymnoascus destructans, the causative agent of white-nose syndrome. Proc Natl Acad Sci U S A. 2015 Jun 16; 112(24):7478-83. PMID: 25944934; PMCID: PMC4475985 [Available on 12/16/15].
    21. Wermelinger LS, Frattani FS, Carneiro-Lobo TC, Craik CS, Castro HC, Zingali RB. Ecotin: Exploring a feasible antithrombotic profile. Int J Biol Macromol. 2015 Jul; 78:296-303. PMID: 25881959.
      View in: PubMed
    22. LeBeau AM, Sevillano N, Markham K, Winter MB, Murphy ST, Hostetter DR, West J, Lowman H, Craik CS, VanBrocklin HF. Imaging active urokinase plasminogen activator in prostate cancer. Cancer Res. 2015 Apr 1; 75(7):1225-35. PMID: 25672980; PMCID: PMC4383704 [Available on 04/01/16].
    23. Sharma V, Panwar P, O'Donoghue AJ, Cui H, Guido RV, Craik CS, Brömme D. Structural requirements for the collagenase and elastase activity of cathepsin K and its selective inhibition by an exosite inhibitor. Biochem J. 2015 Jan 1; 465(1):163-73. PMID: 25279554.
      View in: PubMed
    24. Kim J, Wu S, Tomasiak TM, Mergel C, Winter MB, Stiller SB, Robles-Colmanares Y, Stroud RM, Tampé R, Craik CS, Cheng Y. Subnanometre-resolution electron cryomicroscopy structure of a heterodimeric ABC exporter. Nature. 2015 Jan 15; 517(7534):396-400. PMID: 25363761; PMCID: PMC4372080.
    25. Skala W, Utzschneider DT, Magdolen V, Debela M, Guo S, Craik CS, Brandstetter H, Goettig P. Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity. J Biol Chem. 2014 Dec 5; 289(49):34267-83. PMID: 25326387; PMCID: PMC4256358.
    26. Mahon C, Krogan NJ, Craik CS, Pick E. Cullin E3 ligases and their rewiring by viral factors. Biomolecules. 2014; 4(4):897-930. PMID: 25314029; PMCID: PMC4279162.
    27. Gable JE, Acker TM, Craik CS. Current and Potential Treatments for Ubiquitous but Neglected Herpesvirus Infections. Chem Rev. 2014 Nov 26; 114(22):11382-412. PMID: 25275644; PMCID: PMC4254030.
    28. Tajon CA, Seo D, Asmussen J, Shah N, Jun YW, Craik CS. Sensitive and selective plasmon ruler nanosensors for monitoring the apoptotic drug response in leukemia. ACS Nano. 2014 Sep 23; 8(9):9199-208. PMID: 25166742; PMCID: PMC4174091.
    29. Lucas JM, Heinlein C, Kim T, Hernandez SA, Malik MS, True LD, Morrissey C, Corey E, Montgomery B, Mostaghel E, Clegg N, Coleman I, Brown CM, Schneider EL, Craik C, Simon JA, Bedalov A, Nelson PS. The androgen-regulated protease TMPRSS2 activates a proteolytic cascade involving components of the tumor microenvironment and promotes prostate cancer metastasis. Cancer Discov. 2014 Nov; 4(11):1310-25. PMID: 25122198; PMCID: PMC4409786.
    30. Gable JE, Lee GM, Jaishankar P, Hearn BR, Waddling CA, Renslo AR, Craik CS. Broad-spectrum allosteric inhibition of herpesvirus proteases. Biochemistry. 2014 Jul 22; 53(28):4648-60. PMID: 24977643; PMCID: PMC4108181.
    31. Grove LM, Southern BD, Jin TH, White KE, Paruchuri S, Harel E, Wei Y, Rahaman SO, Gladson CL, Ding Q, Craik CS, Chapman HA, Olman MA. Urokinase-type plasminogen activator receptor (uPAR) ligation induces a raft-localized integrin signaling switch that mediates the hypermotile phenotype of fibrotic fibroblasts. J Biol Chem. 2014 May 2; 289(18):12791-804. PMID: 24644284; PMCID: PMC4007467.
    32. LeBeau AM, Sevillano N, King ML, Duriseti S, Murphy ST, Craik CS, Murphy LL, VanBrocklin HF. Imaging the urokinase plasminongen activator receptor in preclinical breast cancer models of acquired drug resistance. Theranostics. 2014; 4(3):267-79. PMID: 24505235; PMCID: PMC3915090.
    33. Tajon C, Jun YW, Craik CS. Single-molecule sensing of caspase activation in live cells via plasmon coupling nanotechnology. Methods Enzymol. 2014; 544:271-97. PMID: 24974294.
      View in: PubMed
    34. Asmussen J, Lasater EA, Tajon C, Oses-Prieto J, Jun YW, Taylor BS, Burlingame A, Craik CS, Shah NP. MEK-dependent negative feedback underlies BCR-ABL-mediated oncogene addiction. Cancer Discov. 2014 Feb; 4(2):200-15. PMID: 24362263; PMCID: PMC4248023.
    35. Du X, Chen NL, Wong A, Craik CS, Brömme D. Elastin degradation by cathepsin V requires two exosites. J Biol Chem. 2013 Nov 29; 288(48):34871-81. PMID: 24121514; PMCID: PMC3843099.
    36. O'Donoghue AJ, Jin Y, Knudsen GM, Perera NC, Jenne DE, Murphy JE, Craik CS, Hermiston TW. Global substrate profiling of proteases in human neutrophil extracellular traps reveals consensus motif predominantly contributed by elastase. PLoS One. 2013; 8(9):e75141. PMID: 24073241; PMCID: PMC3779220.
    37. Corvo I, O'Donoghue AJ, Pastro L, Pi-Denis N, Eroy-Reveles A, Roche L, McKerrow JH, Dalton JP, Craik CS, Caffrey CR, Tort JF. Dissecting the active site of the collagenolytic cathepsin L3 protease of the invasive stage of Fasciola hepatica. PLoS Negl Trop Dis. 2013; 7(7):e2269. PMID: 23875031; PMCID: PMC3708847.
    38. Small JL, O'Donoghue AJ, Boritsch EC, Tsodikov OV, Knudsen GM, Vandal O, Craik CS, Ehrt S. Substrate specificity of MarP, a periplasmic protease required for resistance to acid and oxidative stress in Mycobacterium tuberculosis. J Biol Chem. 2013 May 3; 288(18):12489-99. PMID: 23504313; PMCID: PMC3642297.
    39. Raman K, Trivedi NN, Raymond WW, Ganesan R, Kirchhofer D, Verghese GM, Craik CS, Schneider EL, Nimishakavi S, Caughey GH. Mutational tail loss is an evolutionary mechanism for liberating marapsins and other type I serine proteases from transmembrane anchors. J Biol Chem. 2013 Apr 12; 288(15):10588-98. PMID: 23447538; PMCID: PMC3624440.
    40. LeBeau AM, Duriseti S, Murphy ST, Pepin F, Hann B, Gray JW, VanBrocklin HF, Craik CS. Targeting uPAR with antagonistic recombinant human antibodies in aggressive breast cancer. Cancer Res. 2013 Apr 1; 73(7):2070-81. PMID: 23400595; PMCID: PMC3618559.
    41. LeBeau AM, Lee M, Murphy ST, Hann BC, Warren RS, Delos Santos R, Kurhanewicz J, Hanash SM, VanBrocklin HF, Craik CS. Imaging a functional tumorigenic biomarker in the transformed epithelium. Proc Natl Acad Sci U S A. 2013 Jan 2; 110(1):93-8. PMID: 23248318; PMCID: PMC3538269.
    42. Lee GM, Balouch E, Goetz DH, Lazic A, McKerrow JH, Craik CS. Mapping inhibitor binding modes on an active cysteine protease via nuclear magnetic resonance spectroscopy. Biochemistry. 2012 Dec 18; 51(50):10087-98. PMID: 23181936; PMCID: PMC3566641.
    43. O'Donoghue AJ, Eroy-Reveles AA, Knudsen GM, Ingram J, Zhou M, Statnekov JB, Greninger AL, Hostetter DR, Qu G, Maltby DA, Anderson MO, Derisi JL, McKerrow JH, Burlingame AL, Craik CS. Global identification of peptidase specificity by multiplex substrate profiling. Nat Methods. 2012 Nov; 9(11):1095-100. PMID: 23023596; PMCID: PMC3707110.
    44. Nimishakavi S, Besprozvannaya M, Raymond WW, Craik CS, Gruenert DC, Caughey GH. Activity and inhibition of prostasin and matriptase on apical and basolateral surfaces of human airway epithelial cells. Am J Physiol Lung Cell Mol Physiol. 2012 Jul; 303(2):L97-106. PMID: 22582115; PMCID: PMC3404626.
    45. Sojka D, Franta Z, Frantová H, Bartosová P, Horn M, Váchová J, O'Donoghue AJ, Eroy-Reveles AA, Craik CS, Knudsen GM, Caffrey CR, McKerrow JH, Mares M, Kopácek P. Characterization of gut-associated cathepsin D hemoglobinase from tick Ixodes ricinus (IrCD1). J Biol Chem. 2012 Jun 15; 287(25):21152-63. PMID: 22539347; PMCID: PMC3375538.
    46. Ingram JR, Rafi SB, Eroy-Reveles AA, Ray M, Lambeth L, Hsieh I, Ruelas D, Lim KC, Sakanari J, Craik CS, Jacobson MP, McKerrow JH. Investigation of the proteolytic functions of an expanded cercarial elastase gene family in Schistosoma mansoni. PLoS Negl Trop Dis. 2012; 6(4):e1589. PMID: 22509414; PMCID: PMC3317910.
    47. Wu S, Avila-Sakar A, Kim J, Booth DS, Greenberg CH, Rossi A, Liao M, Li X, Alian A, Griner SL, Juge N, Yu Y, Mergel CM, Chaparro-Riggers J, Strop P, Tampé R, Edwards RH, Stroud RM, Craik CS, Cheng Y. Fabs enable single particle cryoEM studies of small proteins. Structure. 2012 Apr 4; 20(4):582-92. PMID: 22483106; PMCID: PMC3322386.
    48. Norbury LJ, Hung A, Beckham S, Pike RN, Spithill TW, Craik CS, Choe Y, Fecondo JV, Smooker PM. Analysis of Fasciola cathepsin L5 by S2 subsite substitutions and determination of the P1-P4 specificity reveals an unusual preference. Biochimie. 2012 May; 94(5):1119-27. PMID: 22285967.
      View in: PubMed
    49. Craik CS, Shahian T. A screening strategy for trapping the inactive conformer of a dimeric enzyme with a small molecule inhibitor. Methods Mol Biol. 2012; 928:119-31. PMID: 22956137; PMCID: PMC3739972.
    50. Jäger S, Kim DY, Hultquist JF, Shindo K, LaRue RS, Kwon E, Li M, Anderson BD, Yen L, Stanley D, Mahon C, Kane J, Franks-Skiba K, Cimermancic P, Burlingame A, Sali A, Craik CS, Harris RS, Gross JD, Krogan NJ. Vif hijacks CBF-ß to degrade APOBEC3G and promote HIV-1 infection. Nature. 2012 Jan 19; 481(7381):371-5. PMID: 22190037; PMCID: PMC3310910.
    51. Jäger S, Cimermancic P, Gulbahce N, Johnson JR, McGovern KE, Clarke SC, Shales M, Mercenne G, Pache L, Li K, Hernandez H, Jang GM, Roth SL, Akiva E, Marlett J, Stephens M, D'Orso I, Fernandes J, Fahey M, Mahon C, O'Donoghue AJ, Todorovic A, Morris JH, Maltby DA, Alber T, Cagney G, Bushman FD, Young JA, Chanda SK, Sundquist WI, Kortemme T, Hernandez RD, Craik CS, Burlingame A, Sali A, Frankel AD, Krogan NJ. Global landscape of HIV-human protein complexes. Nature. 2012 Jan 19; 481(7381):365-70. PMID: 22190034; PMCID: PMC3310911.
    52. Schneider EL, Lee MS, Baharuddin A, Goetz DH, Farady CJ, Ward M, Wang CI, Craik CS. A reverse binding motif that contributes to specific protease inhibition by antibodies. J Mol Biol. 2012 Jan 27; 415(4):699-715. PMID: 22154938; PMCID: PMC3268006.
    53. Kim J, Stroud RM, Craik CS. Rapid identification of recombinant Fabs that bind to membrane proteins. Methods. 2011 Dec; 55(4):303-9. PMID: 21958987; PMCID: PMC3264787.
      
    54. 
       Ray M, Hostetter DR, Loeb CR, Simko J, . Ifhibition of Grafzyme B by PI-9 protects prostate cancer cells from apoptosis. Prostate. 2012 Juf 1; 72(8):846-55. PMID: 21919020; PMCID: PMC3401211. 
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  • 4a href='https:/'connects.catalyst.harvard.edu/Profiles/profile/30360153' target5'_blank'>de Poot SA, Westgeest M, Hostetter DR, Van Damme P$ Plasman K, Demeyer K, Broekhuiren R, Gevaert K$ Craik CS
    
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     Zhou Y, Agudelo J, Lu K, Goetz DH, Hanseld E, Chen YT, Roush WR, McKerrow J, Craik CS, Amberg SM, Simmons G. Inhibitors of SARS-CoV eftry--identification using an internally-controlded dual envelope pseudovirion assay. Antiviral Res. 2011 Nov; 92(2):187-94. PMID: 21820471; PMCAD: PMC3205982.<'span>
     View in: PubMed, PubMed Central
  • 
  •  Franta Z, Sojka D, Fraftova H, Dvorak B, Horn M, Srba B, Talacko P, Mares M, Schneider E, Craik CS<'b>, EcKerrow JH, Caffrey CR$ Kopacek P. IrCD1 - the haemoglgbinolytic cathepsin L of the hard tick, Ixodes ricinus. Int J Parasitol. 2011 Oct; 41(12):1253-62. PMID: 21819909. 
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  • 4div> Benfett MJ, Mahgn C, Jäger S, Pache L, Kumar D, Shapiro A, Rao K, Chanda SC, Craik CS, Frankel AD, Krogan NJ 
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     Lee GM$ Shahian T, Baharuddin A, Gable JE, Craik CS4/b>. Enzyme inhabition by allosteric capture of an inactive conformation. J Mol Biol. 2011 Sep 2; 411(5):999-1016. PMID: 21723875; PMCID: PMC3157250. 
     
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  • 4div> Craik CS$ Page MJ, Madisgn EL. Proteases as therapeutics& Biochem J. 2011 Apr 1; 435(1):1-16. PMID: 21406063; PMCID: PMC4503466. 
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    Brown CM, Ray M, Eroy-Reveles AA, Egea P, Tajgn C, Craik CS. Peptide length and leaving-group sterics anfluence potencq of peptide phosphonate protease inhibitors. Chem Biol. 2011 Jaf 28; 18 1):48-57. PMID: 21276938; PMCID2 PMC3074588.  View in: PubMed, PubMed Centrad
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     Farady CB, Craik CS. Mechanisms of macromolecular protease inhibitors. Chembiochee. 2010 Nov 22; 11(17):2341-6. PEID: 21053238; PECID: PMC4150018& <'div>
     View in: PubMed, PubMed Ceftral 4/div>
     Swenerton RK, Zhang S, Sajid M, Medzihradszcy KF, Craik CS, Kellq BL, McKerrow JH. The olagopeptidase B of Leishmania regulates parasite enolase and immufe evasion. J Bigl Chem. 2011 Jaf 7; 286 1):429-40. PMID2 20961853; PMCID: PMC3013002.
     View in: PubMed, PubMed Central
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  •  Na BK, Bae YA, Zo YG, C`oe Y, Kim SH, Desai PV, Avery MA, Craik CS, Kim TS, Rosenthal PJ, Kong Y. Bioc`emical properties of a novel cysteine protease gf Plasmodium vivax, vivapain-4. PLoS Negl Trop Dis. 2010; 4(10)2e849. PMID: 20967286; PMCID: PMC2953480.
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    View in: PubMed4/a>, PubMed Central  
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    Liz MA, Fleeing CE, Nunes AF, Almeida MR, Mar FM, Choe Y, Craik CS, Powers JC, Bogyo M$ Sousa MM. Substrate specificitq of transthyretan: identificatign of natural substrates in the fervous system. Biochem J. 2009 Apr 15; 419(2):467-74. PMID: 19138167; PMCID: PMC4153561.
    
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    4span id="ctl01_rpPublication_ctd85_lblPublicatign">Lee GM, Craik CS. Trapping moving targets with smadl molecules. Scaence. 2009 Apr 10; 324(5924):213-5. PMID: 19359579; PMCID: PMC2181433. 
    
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  • Wilke ME, Higaki JN, Craik C, Fletterick RJ. Crystallographic analysis of trypsin-G226A. A specificity pocket mutant of rat trypsin with altered binding and catalysis. J Mol Biol. 1991 Jun 5; 219(3):525-32. PMID: 2051486.
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  • Wilke ME, Higaki JN, Craik C, Fletterick RJ. Crystal structure of rat trypsin-S195C at -150 degrees C. Analysis of low activity of recombinant and semisynthetic thiol proteases. J Mol Biol. 1991 Jun 5; 219(3):511-23. PMID: 1904942.
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  • McGrath ME, Hines WM, Sakanari JA, Fletterick RJ, Craik C. The sequence and reactive site of ecotin. A general inhibitor of pancreatic serine proteases from Escherichia coli. J Biol Chem. 1991 Apr 5; 266(10):6620-5. PMID: 2007606.
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  • Babé LM, Pichuantes S, Craik C. Inhibition of HIV protease activity by heterodimer formation. Biochemistry. 1991 Jan 8; 30(1):106-11. PMID: 1988010.
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  • D.L. Sloane, R. Leung, C.S. Craik & E. Sigal. A Primary Determinant for Lipoxygenase Postional Specificity. Nature 354, 149-152. 1991.
  • C.S.Craik. Modus Operandi. Nature . 1991; 353, 469 .
  • Tomasselli AG, Howe WJ, Hui JO, Sawyer TK, Reardon IM, DeCamp DL, Craik C, Heinrikson RL. Calcium-free calmodulin is a substrate of proteases from human immunodeficiency viruses 1 and 2. Proteins. 1991; 10(1):1-9. PMID: 2062825.
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  • Babé LM, Craik C. Time dependent heterodimer formation leads to inhibition of HIV protease activity. Adv Exp Med Biol. 1991; 306:543-7. PMID: 1812756.
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  • DeCamp DL, Babé LM, Furth P, Ortiz de Montellano P, Kuntz ID, Craik C. Structure-based inhibition of HIV-1 protease activity and viral infectivity. Adv Exp Med Biol. 1991; 306:489-92. PMID: 1812747.
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  • Earnest T, Fauman E, Craik C, Stroud R. 1.59 A structure of trypsin at 120 K: comparison of low temperature and room temperature structures. Proteins. 1991; 10(3):171-87. PMID: 1881877.
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  • 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 .
  • Sloane DL, Dixon RA, Craik C, Sigal E. Expression of cloned human 15-lipoxygenase in eukaryotic and prokaryotic systems. Adv Prostaglandin Thromboxane Leukot Res. 1991; 21A:25-8. PMID: 1825549.
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  • Higaki JN, Haymore BL, Chen S, Fletterick RJ, Craik C. Regulation of serine protease activity by an engineered metal switch. Biochemistry. 1990 Sep 18; 29(37):8582-6. PMID: 2125468.
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  • Bathurst IC, Moen LK, Lujan MA, Gibson HL, Feucht PH, Pichuantes S, Craik C, Santi DV, Barr PJ. Characterization of the human immunodeficiency virus type-1 reverse transcriptase enzyme produced in yeast. Biochem Biophys Res Commun. 1990 Sep 14; 171(2):589-95. PMID: 1698361.
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  • DesJarlais RL, Seibel GL, Kuntz ID, Furth PS, Alvarez JC, Ortiz de Montellano PR, DeCamp DL, Babé LM, Craik C. Structure-based design of nonpeptide inhibitors specific for the human immunodeficiency virus 1 protease. Proc Natl Acad Sci U S A. 1990 Sep; 87(17):6644-8. PMID: 2204060; PMCID: PMC54593.
  • Hall MN, Craik C, Hiraoka Y. Homeodomain of yeast repressor alpha 2 contains a nuclear localization signal. Proc Natl Acad Sci U S A. 1990 Sep; 87(18):6954-8. PMID: 1976249; PMCID: PMC54660.
  • Pichuantes S, Babé LM, Barr PJ, DeCamp DL, Craik C. Recombinant HIV2 protease processes HIV1 Pr53gag and analogous junction peptides in vitro. J Biol Chem. 1990 Aug 15; 265(23):13890-8. PMID: 2199446.
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  • Vanderslice P, Ballinger SM, Tam EK, Goldstein SM, Craik C, Caughey GH. Human mast cell tryptase: multiple cDNAs and genes reveal a multigene serine protease family. Proc Natl Acad Sci U S A. 1990 May; 87(10):3811-5. PMID: 2187193; PMCID: PMC53993.
  • Stewart EA, Craik C, Hake L, Bowcock AM. Human carboxypeptidase A identifies a BglII RFLP and maps to 7q31-qter. Am J Hum Genet. 1990 Apr; 46(4):795-800. PMID: 1969228; PMCID: PMC1683655.
  • Sigal E, Grunberger D, Highland E, Gross C, Dixon RA, Craik CS. Expression of cloned human reticulocyte 15-lipoxygenase and immunological evidence that 15-lipoxygenases of different cell types are related. J Biol Chem. 1990 Mar 25; 265(9):5113-20. PMID: 2318885.
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  • Eakin AE, Bouvier J, Sakanari JA, Craik C, McKerrow JH. Amplification and sequencing of genomic DNA fragments encoding cysteine proteases from protozoan parasites. Mol Biochem Parasitol. 1990 Feb; 39(1):1-8. PMID: 2406590.
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  • L. Evnin, J. Vasquez & C.S. Craik. Proc. Substrate Specificity of Trypsin Investigated Using a Genetic Selection. Natl. Acad. Sci. USA 87 . 1990; 6659-6663.
  • Sloane DL, Craik C, Sigal E. The expression of active human reticulocyte 15-lipoxygenase in bacteria. Biomed Biochim Acta. 1990; 49(2-3):S11-6. PMID: 1696810.
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  • M. Obukowicz, M. Gustafson, K. Junger, R. Leimgruber, A. Wittwer, T-C. Wun, T. Warren, B. Bishop, K. Mathis, D. McPherson, N. Siegel, M. Jennings, B. Brightwell, J. Diaz-Collier, L. Bell, C.S. Craik & W. Tacon. Secretion of Active Kringle 2-Serine Protease in E. coli. J. Bio. Chem. 29, 9737-9745 . 1990.
  • E. Stewart, C.S. Craik, L. Hake & A. Bowcock. Human CPA Identifies a BglII RFLP and Maps to 7q31-qter. Amer. J. Hum. Gen. 46, 795 -800 . 1990.
  • S. Pichuantes, L. Babé, P. Barr, D. DeCamp & C.S. Craik. Recombinant HIV 2 Protease Processes HIV 1 Pr53gag and Analogous Junction Peptides In Vitro. J. Bio. Chem. 265, 13890-13898 . 1990.
  • A.L. Ferris, A. Hizi, S.D. Showalter, S. Pichuantes, L. Babé & C.S. Craik. Immunologic and Proteolytic Analysis of HIV-2 Reverse Transcriptase Structure. Virology 175. 1990; 456-464 .
  • McGrath ME, Wilke ME, Higaki JN, Craik C, Fletterick RJ. Crystal structures of two engineered thiol trypsins. Biochemistry. 1989 Nov 28; 28(24):9264-70. PMID: 2611228.
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  • Sakanari JA, Staunton CE, Eakin AE, Craik C, McKerrow JH. Serine proteases from nematode and protozoan parasites: isolation of sequence homologs using generic molecular probes. Proc Natl Acad Sci U S A. 1989 Jul; 86(13):4863-7. PMID: 2662185; PMCID: PMC297515.
  • Vanderslice P, Craik CS, Nadel JA, Caughey GH. Molecular cloning of dog mast cell tryptase and a related protease: structural evidence of a unique mode of serine protease activation. Biochemistry. 1989 May 16; 28(10):4148-55. PMID: 2504277.
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  • Shimada K, Koh CS, Hashimoto T, Shoji S, Yanagisawa N. [A case of aseptic meningoencephalitis with recurrent abnormal behavior, status epilepticus and aphthous stomatitis, improved by acyclovir]. Rinsho Shinkeigaku. 1989 Mar; 29(3):367-70. PMID: 2752665.
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  • McGrath ME, Fletterick RJ, Craik C. Rapid preparation of proteins for crystallization trials. Biotechniques. 1989 Mar; 7(3):246-7. PMID: 2631770.
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  • Vasquez JR, Evnin LB, Higaki JN, Craik C. An expression system for trypsin. J Cell Biochem. 1989 Mar; 39(3):265-76. PMID: 2651464.
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  • Pichuantes S, Babé LM, Barr PJ, Craik C. Recombinant HIV1 protease secreted by Saccharomyces cerevisiae correctly processes myristylated gag polyprotein. Proteins. 1989; 6(3):324-37. PMID: 2695931.
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  • A. Eakin, J.N. Higaki, J.H. McKerrow & C.S. Craik. Cysteine or Serine Proteinase. Nature 342,132. 1989.
  • Sigal E, Craik C, Dixon RA, Nadel JA. Cloning and expression of human arachidonate 15-lipoxygenase. Trans Assoc Am Physicians. 1989; 102:176-84. PMID: 2638524.
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  • Sigal E, Grunberger D, Craik C, Caughey GH, Nadel JA. Arachidonate 15-lipoxygenase from human leukocytes: purification and structural homology to other mammalian lipoxygenases. Adv Prostaglandin Thromboxane Leukot Res. 1989; 19:156-9. PMID: 2526462.
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  • J. Higaki L.B. Evnin & C.S. Craik. Introduction of a Cysteine Protease Active Site into Trypsin. Biochem. 28, 9256-9263 . 1989.
  • Sigal E, Craik C, Highland E, Grunberger D, Costello LL, Dixon RA, Nadel JA. Molecular cloning and primary structure of human 15-lipoxygenase. Biochem Biophys Res Commun. 1988 Dec 15; 157(2):457-64. PMID: 3202857.
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  • Gráf L, Hegyi G, Likó I, Hepp J, Medzihradszky K, Craik CS, Rutter WJ. Structural and functional integrity of specificity and catalytic sites of trypsin. Int J Pept Protein Res. 1988 Dec; 32(6):512-8. PMID: 2907752.
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  • Gardell SJ, Craik C, Clauser E, Goldsmith EJ, Stewart CB, Graf M, Rutter WJ. A novel rat carboxypeptidase, CPA2: characterization, molecular cloning, and evolutionary implications on substrate specificity in the carboxypeptidase gene family. J Biol Chem. 1988 Nov 25; 263(33):17828-36. PMID: 3182871.
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  • Clauser E, Gardell SJ, Craik C, MacDonald RJ, Rutter WJ. Structural characterization of the rat carboxypeptidase A1 and B genes. Comparative analysis of the rat carboxypeptidase gene family. J Biol Chem. 1988 Nov 25; 263(33):17837-45. PMID: 3182872.
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  • Powell SK, Orci L, Craik C, Moore HP. Efficient targeting to storage granules of human proinsulins with altered propeptide domain. J Cell Biol. 1988 Jun; 106(6):1843-51. PMID: 2838491; PMCID: PMC2115124.
  • Sigal E, Grunberger D, Craik CS, Caughey GH, Nadel JA. Arachidonate 15-lipoxygenase (omega-6 lipoxygenase) from human leukocytes. Purification and structural homology to other mammalian lipoxygenases. J Biol Chem. 1988 Apr 15; 263(11):5328-32. PMID: 3356688.
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  • Sigal E, Grunberger D, Cashman JR, Craik CS, Caughey GH, Nadel JA. Arachidonate 15-lipoxygenase from human eosinophil-enriched leukocytes: partial purification and properties. Biochem Biophys Res Commun. 1988 Jan 15; 150(1):376-83. PMID: 3337718.
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  • Sprang SR, Fletterick RJ, Gráf L, Rutter WJ, Craik C. Studies of specificity and catalysis in trypsin by structural analysis of site-directed mutants. Crit Rev Biotechnol. 1988; 8(3):225-36. PMID: 3063392.
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  • Evnin LB, Craik C. Development of an efficient method for generating and screening active trypsin and trypsin variants. Ann N Y Acad Sci. 1988; 542:61-74. PMID: 3228244.
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  • Sprang S, Standing T, Fletterick RJ, Stroud RM, Finer-Moore J, Xuong NH, Hamlin R, Rutter WJ, Craik C. The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis. Science. 1987 Aug 21; 237(4817):905-9. PMID: 3112942.
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  • Craik CS, Roczniak S, Largman C, Rutter WJ. The catalytic role of the active site aspartic acid in serine proteases. Science. 1987 Aug 21; 237(4817):909-13. PMID: 3303334.
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  • Fletcher TS, Alhadeff M, Craik CS, Largman C. Isolation and characterization of a cDNA encoding rat cationic trypsinogen. Biochemistry. 1987 Jun 2; 26(11):3081-6. PMID: 3607011.
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  • Graf L, Craik C, Patthy A, Roczniak S, Fletterick RJ, Rutter WJ. Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin. Biochemistry. 1987 May 5; 26(9):2616-23. PMID: 3111531.
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  • Craik CS, Roczniak S, Sprang S, Fletterick R, Rutter W. Redesigning trypsin via genetic engineering. J Cell Biochem. 1987 Mar; 33(3):199-211. PMID: 3553217.
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  • Ebina Y, Araki E, Taira M, Shimada F, Mori M, Craik C, Siddle K, Pierce SB, Roth RA, Rutter WJ. Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity. Proc Natl Acad Sci U S A. 1987 Feb; 84(3):704-8. PMID: 3101064; PMCID: PMC304284.
  • W.J. Rutter, S.J. Gardell, S. Roczniak, D. Hilvert, S. Sprang, R.J. Fletterick & C.S. Craik. Edited by D. Oxender and C.F. Fox. New York: Alan R. Liss, Inc. Redesigning Proteins via Genetic Engineering. In: Protein Modification and Design, pp. 257-267. 1987.
  • T.L. Burgess, C.S. Craik, L. Matsuuchi & R.B. Kelly. In Vitro Mutagenesis of Trypsinogen: The Role of the N-Terminus in Intracellular Protein Targeting to Secretory Granules. J. Cell Bio. 105, 659-668 . 1987.
  • C.S. Craik. Edited by D. Oxender. New York: Alan R. Liss, Inc. Expression and Overproduction of Proteins. In: Protein Structure, Folding and Design 2, pp. 467-476. . 1987.
  • C.S. Craik, S. Roczniak, S. Sprang, R.J. Fletterick & W.J. Rutter. Edited by D. Cunningham and G. Long. New York: Alan R Liss, Inc. Redesigning Trypsin via Genetic Engineering. In: Proteases in Biological Control and Biotechnology. 1987; 183-195.
  • Higaki JN, Gibson BW, Craik CS. Evolution of catalysis in the serine proteases. Cold Spring Harb Symp Quant Biol. 1987; 52:615-21. PMID: 3331347.
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  • Bowcock AM, Crandall J, Daneshvar L, Lee GM, Young B, Zunzunegui V, Craik C, Cavalli-Sforza LL, King MC. Genetic analysis of cystic fibrosis: linkage of DNA and classical markers in multiplex families. Am J Hum Genet. 1986 Dec; 39(6):699-706. PMID: 3026172; PMCID: PMC1684114.
  • S. Gardell, C.S. Craik, D. Hilvert, M. Urdea & W. Rutter. Edited by I. Bertini, C. Luchinat, W. Maret, and M. Zeppezauer. Boston, Massachusetts: Birkhäuser. Probing the Role of Tyrosine 248 in Carboxypeptidase A with Site-Directed Mutagenesis. In: Comparative Analysis of Catalytic Mechanisms of Zinc Enzymes. . 1986.
  • Gardell SJ, Craik CS, Hilvert D, Urdea MS, Rutter WJ. Site-directed mutagenesis shows that tyrosine 248 of carboxypeptidase A does not play a crucial role in catalysis. Nature. 1985 Oct 10-16; 317(6037):551-5. PMID: 3840231.
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  • Burgess TL, Craik C, Kelly RB. The exocrine protein trypsinogen is targeted into the secretory granules of an endocrine cell line: studies by gene transfer. J Cell Biol. 1985 Aug; 101(2):639-45. PMID: 2991303; PMCID: PMC2113688.
  • Craik CS, Largman C, Fletcher T, Roczniak S, Barr PJ, Fletterick R, Rutter WJ. Redesigning trypsin: alteration of substrate specificity. Science. 1985 Apr 19; 228(4697):291-7. PMID: 3838593.
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  • C.S. Craik. Biotechniques. Use of Oligonucleotides for Site-Specific Mutagenesis. 1985; 3:12-19.
  • Craik CS, Choo QL, Swift GH, Quinto C, MacDonald RJ, Rutter WJ. Structure of two related rat pancreatic trypsin genes. J Biol Chem. 1984 Nov 25; 259(22):14255-64. PMID: 6094547.
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  • Bell GI, Quinto C, Quiroga M, Valenzuela P, Craik CS, Rutter WJ. Isolation and sequence of a rat chymotrypsin B gene. J Biol Chem. 1984 Nov 25; 259(22):14265-70. PMID: 6209274.
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  • Swift GH, Craik CS, Stary SJ, Quinto C, Lahaie RG, Rutter WJ, MacDonald RJ. Structure of the two related elastase genes expressed in the rat pancreas. J Biol Chem. 1984 Nov 25; 259(22):14271-8. PMID: 6094548.
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  • Honey NK, Sakaguchi AY, Quinto C, MacDonald RJ, Bell GI, Craik C, Rutter WJ, Naylor SL. Chromosomal assignments of human genes for serine proteases trypsin, chymotrypsin B, and elastase. Somat Cell Mol Genet. 1984 Jul; 10(4):369-76. PMID: 6589790.
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  • Honey NK, Sakaguchi AY, Lalley PA, Quinto C, MacDonald RJ, Craik C, Bell GI, Rutter WJ, Naylor SL. Chromosomal assignments of genes for trypsin, chymotrypsin B, and elastase in mouse. Somat Cell Mol Genet. 1984 Jul; 10(4):377-83. PMID: 6589791.
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  • Craik CS, Rutter WJ, Fletterick R. Splice junctions: association with variation in protein structure. Science. 1983 Jun 10; 220(4602):1125-9. PMID: 6344214.
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  • Craik CS, Sprang S, Fletterick R, Rutter WJ. Intron-exon splice junctions map at protein surfaces. Nature. 1982 Sep 9; 299(5879):180-2. PMID: 7110339.
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  • C.S. Craik & S. Beychok. Edited by C. Ho. In: Interaction Between Iron Proteins in Oxygen and Electron Transport, Elsevier North Holland Biomedical Press . 1982; 192-197.
  • Craik CS, Buchman SR, Beychok S. O2 binding properties of the product of the central exon of beta-globin gene. Nature. 1981 May 7; 291(5810):87-90. PMID: 7231528.
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  • Craik CS, Vallette I, Beychok S, Waks M. Refolding defects in hemoglobin Rothschild. J Biol Chem. 1980 Jul 10; 255(13):6219-23. PMID: 7391018.
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  • Craik CS, Buchman SR, Beychok S. Characterization of globin domains: heme binding to the central exon product. Proc Natl Acad Sci U S A. 1980 Mar; 77(3):1384-8. PMID: 6929492; PMCID: PMC348499.
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