About: Tonge Peter J.

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Attributs	Valeurs
type	Person
name	Tonge Peter J. Tonge P. J.
familyName	Tonge
Given name	P. J. Peter Peter J.
is relates of	http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_38/101021bi00153a002/authorship/1 http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_42/101021bi020382g/authorship/4 http://hub.abes.fr/acs/periodical/bichaw/2003/volume_42/issue_15/101021bi0300229/authorship/5 http://hub.abes.fr/acs/periodical/jacsat/1992/volume_114/issue_22/101021ja00048a078/authorship/1 http://hub.abes.fr/acs/periodical/jacsat/1993/volume_115/issue_19/101021ja00072a031/authorship/1 http://hub.abes.fr/acs/periodical/achre4/1995/volume_28/issue_1/101021ar00049a002/authorship/2 http://hub.abes.fr/acs/periodical/jpchax/1994/volume_98/issue_14/101021j100065a010/authorship/4 http://hub.abes.fr/acs/periodical/bichaw/1991/volume_30/issue_19/101021bi00233a021/authorship/1 http://hub.abes.fr/acs/periodical/bichaw/1994/volume_33/issue_49/101021bi00253a011/authorship/3 http://hub.abes.fr/acs/periodical/jacsat/1991/volume_113/issue_11/101021ja00011a037/authorship/1 http://hub.abes.fr/oup/periodical/jac/2009/volume_64/issue_5/101093jacdkp307/authorship/9 http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_1/101021bi9915364/authorship/3 http://hub.abes.fr/acs/periodical/bichaw/1997/volume_36/issue_33/101021bi970941x/authorship/2 http://hub.abes.fr/acs/periodical/bichaw/1999/volume_38/issue_29/101021bi990506y/authorship/4 http://hub.abes.fr/acs/periodical/jpcbfk/2002/volume_106/issue_23/101021jp0145560/authorship/3 http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_9/101021ja042466d/authorship/6 http://hub.abes.fr/acs/periodical/jmcmar/2004/volume_47/issue_3/101021jm030182i/authorship/7 http://hub.abes.fr/acs/periodical/bichaw/1997/volume_36/issue_8/101021bi962549/authorship/4 http://hub.abes.fr/acs/periodical/jmcmar/2006/volume_49/issue_2/101021jm050920y/authorship/8 http://hub.abes.fr/acs/periodical/jacsat/2003/volume_125/issue_23/101021ja034588w/authorship/4 http://hub.abes.fr/acs/periodical/bichaw/2003/volume_42/issue_40/101021bi0344578/authorship/6 http://hub.abes.fr/acs/periodical/bichaw/2007/volume_46/issue_4/101021bi0608515/authorship/5 http://hub.abes.fr/acs/periodical/jacsat/2000/volume_122/issue_47/101021ja001891d/authorship/5 http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_15/101021bi992675o/authorship/4 http://hub.abes.fr/acs/periodical/achre4/2008/volume_41/issue_1/101021ar700156e/authorship/2 http://hub.abes.fr/acs/periodical/bichaw/1999/volume_38/issue_41/101021bi990529c/authorship/4 http://hub.abes.fr/acs/periodical/jpcafh/2004/volume_108/issue_21/101021jp037902h/authorship/5 http://hub.abes.fr/acs/periodical/jpcbfk/2006/volume_110/issue_41/101021jp0650735/authorship/5 http://hub.abes.fr/acs/periodical/jacsat/2000/volume_122/issue_17/101021ja992286h/authorship/6 http://hub.abes.fr/acs/periodical/jacsat/2001/volume_123/issue_3/101021ja003406k/authorship/3 http://hub.abes.fr/acs/periodical/jpcbfk/2006/volume_110/issue_43/101021jp065326u/authorship/5 http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_6/101021bi001733z/authorship/4 http://hub.abes.fr/acs/periodical/jmcmar/2006/volume_49/issue_15/101021jm060222t/authorship/5 http://hub.abes.fr/acs/periodical/bichaw/1996/volume_35/issue_38/101021bi960648h/authorship/2 http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_26/101021bi0008940/authorship/3 http://hub.abes.fr/acs/periodical/jacsat/2007/volume_129/issue_50/101021ja074074n/authorship/4 http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_2/101021bi002065k/authorship/6 http://hub.abes.fr/acs/periodical/bichaw/2008/volume_47/issue_14/101021bi800023a/authorship/12 http://hub.abes.fr/acs/periodical/bichaw/2007/volume_46/issue_4/101021bi060852x/authorship/5 http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_23/101021ja050083p/authorship/4 http://hub.abes.fr/acs/periodical/jacsat/2007/volume_129/issue_20/101021ja068219m/authorship/9 http://hub.abes.fr/acs/periodical/bichaw/2000/volume_39/issue_45/101021bi0006464/authorship/6 http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_4/101021ja0754507/authorship/6 http://hub.abes.fr/acs/periodical/bichaw/2005/volume_44/issue_34/101021bi0507837/authorship/4 http://hub.abes.fr/acs/periodical/jacsat/1998/volume_120/issue_39/101021ja982243l/authorship/2 http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_42/101021bi00042a020/authorship/6 http://hub.abes.fr/acs/periodical/bichaw/1989/volume_28/issue_16/101021bi00442a025/authorship/1 http://hub.abes.fr/acs/periodical/bichaw/1990/volume_29/issue_48/101021bi00500a002/authorship/1 http://hub.abes.fr/acs/periodical/bichaw/1994/volume_33/issue_42/101021bi00208a014/authorship/2 http://hub.abes.fr/acs/periodical/jacsat/1989/volume_111/issue_4/101021ja00186a055/authorship/1 http://hub.abes.fr/springer/periodical/10542/1996/volume_10/issue_7/B917415E86E06016E053120B220A5885/authorship/4
is Author of	Enoyl-Coenzyme A Hydratase-Catalyzed Exchange of the .alpha.-Protons of Coenzyme A Thiol Esters: A Model for an Enolized Intermediate in the Enzyme-Catalyzed Elimination? Unlocking the Secrets of Enzyme Power Using Raman Spectroscopy Markedly different acyl papain structures deacylate at similar rates: resonance Raman spectroscopic and kinetic evidence Evidence for electrophilic catalysis in the 4-chlorobenzoyl-CoA dehalogenase reaction: UV, Raman, and 13C-NMR spectral studies of dehalogenase complexes of benzoyl-CoA adducts Forces, bond lengths, and reactivity: fundamental insight into the mechanism of enzyme catalysis Electronic Rearrangement Induced by Substrate Analog Binding to the Enoyl-CoA Hydratase Active Site: Evidence for Substrate Activation Characterization of trans- and cis-5-methylthienylacryloyl chymotrypsin using Raman difference spectroscopy, NMR, and kinetics: carbonyl environment and reactivity Evidence from Raman Spectroscopy That InhA, theMycobacterial Enoyl Reductase, Modulates the Conformationof the NADH Cofactor to Promote Catalysis Ultrafast Structural Dynamics in BLUF Domains: TransientInfrared Spectroscopy of AppA and Its Mutants Procatalytic Ligand Strain. Ionization and Perturbation of 8-Nitroxanthine at theUrate Oxidase Active Site Ultrafast Excited and Ground-State Dynamics of the Green Fluorescent ProteinChromophore in Solution Stereospecific 1H and 13C NMR Assignments of Crotonyl CoA andHexadienoyl CoA: Conformational Analysis and Comparison withProtein−CoA Complexes Stereospecificity of the Reaction Catalyzed by Enoyl-CoA Hydratase Role of Glutamate 144 and Glutamate 164 in the Catalytic Mechanism ofEnoyl-CoA Hydratase H-Bonding in Alcohols Is Reflected in the Cα−H Bond Strength: Variation of C−D Vibrational Frequency and Fractionation Factor Light-Driven Decarboxylation of Wild-Type Green FluorescentProtein An Alternate Proton Acceptor for Excited-State ProtonTransfer in Green Fluorescent Protein: Rewiring GFP Deacylation and Reacylation for a Series of Acyl Cysteine Proteases, IncludingAcyl Groups Derived from Novel Chromophoric Substrates Substituted diphenyl ethers as a broad-spectrum platform for the development of chemotherapeutics for the treatment of tularaemia Raman Study of the Polarizing Forces Promoting Catalysis in4-Chlorobenzoate-CoA Dehalogenase Active Site Heterogeneity in Dimethyl Sulfoxide Reductase from Rhodobactercapsulatus Revealed by Raman Spectroscopy Probing the Ground State Structure of the Green Fluorescent Protein ChromophoreUsing Raman Spectroscopy Effect of Mutagenesis on the Stereochemistry of Enoyl-CoA Hydratase Structure and Mechanism of MbtI, the Salicylate Synthase fromMycobacterium tuberculosis Structure−Activity Studies of the Inhibition of FabI, the Enoyl Reductase fromEscherichia coli, by Triclosan: Kinetic Analysis of Mutant FabIs Probing Hydrogen-Bonding Interactions in the Active Site of Medium-ChainAcyl-CoA Dehydrogenase Using Raman Spectroscopy 4-Hydroxycinnamoyl-CoA: An Ionizable Probe of the Active Site of the MediumChain Acyl-CoA Dehydrogenase Medium-Chain Acyl-Coenzyme A Dehydrogenase Bound to a Product Analogue,Hexadienoyl-Coenzyme A: Effects on Reduction Potential, pKa, and Polarization Involvement of Glycine 141 in Substrate Activation by Enoyl-CoA Hydratase Mechanism and Inhibition of saFabI, the Enoyl Reductase from Staphylococcus aureus Ultrafast Vibrational Spectroscopy of the Flavin Chromophore Inhibitors of FabI, an Enzyme Drug Target in the Bacterial Fatty Acid Biosynthesis Pathway Ring Current Effects in the Active Site of Medium-ChainAcyl-CoA Dehydrogenase Revealed by NMR Spectroscopy Observation of Excited-State Proton Transfer in Green Fluorescent Proteinusing Ultrafast Vibrational Spectroscopy Lysine 190 Is the Catalytic Base in MenF, the Menaquinone-Specific IsochorismateSynthase from Escherichia coli: Implications for an Enzyme Family Structure of Hexadienoyl-CoA Bound to Enoyl-CoA Hydratase Determined byTransferred Nuclear Overhauser Effect Measurements: Mechanistic PredictionsBased on the X-ray Structure of 4-(Chlorobenzoyl)-CoA Dehalogenase Inhibition of InhA, the Enoyl Reductase from Mycobacterium tuberculosis, byTriclosan and Isoniazid Isotopic Labeling and Normal-Mode Analysis of a Model Green Fluorescent ProteinChromophore Inhibition of the Bacterial Enoyl Reductase FabI by Triclosan: AStructure−Reactivity Analysis of FabI Inhibition by Triclosan Analogues Targeting FtsZ for Antituberculosis DrugDiscovery: Noncytotoxic Taxanes as NovelAntituberculosis Agents Synthesis of Crotonyl-OxyCoA: A Mechanistic Probeof the Reaction Catalyzed by Enoyl-CoA Hydratase Roles of Tyrosine 158 and Lysine 165 in the Catalytic Mechanism of InhA, theEnoyl-ACP Reductase from Mycobacterium tuberculosis

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