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Craik Charles S.
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http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_14/101021bi011781z/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_5/101021bi011753g/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1987/volume_26/issue_9/101021bi00383a031/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1993/volume_32/issue_46/101021bi00097a030/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_12/101021bi00127a005/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1989/volume_28/issue_24/101021bi00450a005/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1994/volume_33/issue_11/101021bi00177a016/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1987/volume_26/issue_11/101021bi00385a020/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1989/volume_28/issue_10/101021bi00436a004/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_8/101021bi011762p/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/2006/volume_128/issue_32/101021ja0614159/authorship/3
http://hub.abes.fr/oup/periodical/bioinformatics/2010/volume_26/issue_14/101093bioinformaticsbtq267/authorship/6
http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_22/101021ja049977k/authorship/6
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http://hub.abes.fr/acs/periodical/bichaw/2003/volume_42/issue_30/101021bi0344679/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/2006/volume_45/issue_11/101021bi0523658/authorship/5
http://hub.abes.fr/acs/periodical/joceah/2002/volume_67/issue_3/101021jo016140o/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_42/101021bi001019h/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/2000/volume_122/issue_30/101021ja0002262/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_26/101021bi025638x/authorship/5
http://hub.abes.fr/acs/periodical/jacsat/2003/volume_125/issue_9/101021ja027973e/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/1992/volume_114/issue_12/101021ja00038a067/authorship/5
http://hub.abes.fr/acs/periodical/bichaw/1990/volume_29/issue_37/101021bi00489a012/authorship/5
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http://hub.abes.fr/acs/periodical/jacsat/1992/volume_114/issue_5/101021ja00031a037/authorship/2
http://hub.abes.fr/acs/periodical/jmcmar/1994/volume_37/issue_5/101021jm00031a017/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/1989/volume_28/issue_24/101021bi00450a004/authorship/3
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http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_7/101021bi00007a010/authorship/5
http://hub.abes.fr/acs/periodical/joceah/1994/volume_59/issue_21/101021jo00100a021/authorship/4
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Molecular cloning of dog mast cell tryptase and a related protease: structural evidence of a unique mode of serine protease activation
Exogenous Acetate Reconstitutes the Enzymic Activity of Trypsin Asp189Ser
Engineered Metal Regulation of Trypsin Specificity
Specific inhibition of HIV-1 protease by boronated porphyrins
Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin
An investigation into the minimum requirements for peptide hydrolysis by mutation of the catalytic triad of trypsin
Haloperidol-Based Irreversible Inhibitors of the HIV-1 and HIV-2 Proteases
Regulation of serine protease activity by an engineered metal switch
Isolation and characterization of a cDNA encoding rat cationic trypsinogen
Structure of the protease from simian immunodeficiency virus: Complex with an irreversible nonpeptide inhibitor
Nonpeptide HIV Protease Inhibitors. Differential Introduction of Alkylamino Groups into the Two Aryl Rings of Haloperidol
Crystal structures of two engineered thiol trypsins
Prediction of protease substrates using sequence and structure features
Isotope-Coded and Affinity-Tagged Cross-Linking (ICATXL): An EfficientStrategy to Probe Protein Interaction Surfaces
Expedient Solid-Phase Synthesis of Fluorogenic ProteaseSubstrates Using the 7-Amino-4-carbamoylmethylcoumarin (ACC)Fluorophore
Chemically Mediated Site-Specific Cleavage ofProteins
Elimination of 13Cα Splitting in Protein NMR Spectra by Deconvolution withMaximum Entropy Reconstruction
Selective Inhibition of the Collagenolytic Activity of Human Cathepsin K byAltering Its S2 Subsite Specificity
Anisotropic Dynamics of the JE-2147−HIV Protease Complex: Drug Resistanceand Thermodynamic Binding Mode Examined in a 1.09 Å Structure,
Functional Consequences of the Kaposi's Sarcoma-Associated Herpesvirus ProteaseStructure: Regulation of Activity and Dimerization by Conserved StructuralElements,
Conformational Change Coupling the Dimerization and Activation of KSHVProtease
Methyl Groups as Probes for Proteins and Complexes inIn-Cell NMR Experiments
Quantitative Identification of the Protonation State of Histidines in Vitro and inVivo
Potent and Selective Inhibition of Membrane-Type Serine Protease 1 by HumanSingle-Chain Antibodies
Chemically Mediated Site-Specific Proteolysis. Alteration of Protein−ProteinInteraction
One Functional Switch Mediates Reversible and Irreversible Inactivation of aHerpesvirus Protease
Inhibition of HIV protease activity by heterodimer formation
Structure of an engineered, metal-actuated switch in trypsin
Introduction of a cysteine protease active site into trypsin
Perturbing the polar environment of Asp102 in trypsin: consequences of replacing conserved Ser214
An alternate geometry for the catalytic triad of serine proteases
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