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Hamilton Andrew
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http://hub.abes.fr/acs/periodical/jacsat/1991/volume_113/issue_20/101021ja00020a027/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_1/101021ja037614z/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/1991/volume_113/issue_1/101021ja00001a068/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/1992/volume_114/issue_1/101021ja00027a059/authorship/3
http://hub.abes.fr/acs/periodical/jmcmar/2008/volume_51/issue_17/101021jm800113p/authorship/11
http://hub.abes.fr/acs/periodical/jacsat/2006/volume_128/issue_7/101021ja056833c/authorship/5
http://hub.abes.fr/acs/periodical/jmcmar/2002/volume_45/issue_1/101021jm0103099/authorship/7
http://hub.abes.fr/acs/periodical/jmcmar/2004/volume_47/issue_2/101021jm030236o/authorship/13
http://hub.abes.fr/acs/periodical/jacsat/2006/volume_128/issue_48/101021ja066472g/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/2003/volume_125/issue_15/101021ja028574m/authorship/5
http://hub.abes.fr/acs/periodical/joceah/2001/volume_66/issue_22/101021jo010413y/authorship/5
http://hub.abes.fr/acs/periodical/jmcmar/2005/volume_48/issue_11/101021jm0491039/authorship/11
http://hub.abes.fr/acs/periodical/jacsat/2003/volume_125/issue_34/101021ja034563x/authorship/2
http://hub.abes.fr/acs/periodical/jmcmar/2006/volume_49/issue_19/101021jm060081v/authorship/15
http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_18/101021ja039562j/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_15/101021ja0446404/authorship/7
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_29/101021ja050122x/authorship/10
http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_40/101021ja0317731/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/2007/volume_129/issue_10/101021ja076881s/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/1988/volume_110/issue_19/101021ja00227a045/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/1992/volume_114/issue_3/101021ja00029a068/authorship/3
http://hub.abes.fr/acs/periodical/jacsat/1993/volume_115/issue_1/101021ja00054a066/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/1991/volume_113/issue_19/101021ja00019a067/authorship/2
http://hub.abes.fr/acs/periodical/jacsat/1988/volume_110/issue_6/101021ja00214a075/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1995/volume_34/issue_38/101021bi00038a037/authorship/5
http://hub.abes.fr/acs/periodical/jacsat/1987/volume_109/issue_16/101021ja00250a052/authorship/1
http://hub.abes.fr/acs/periodical/jacsat/1991/volume_113/issue_14/101021ja00014a055/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/1995/volume_117/issue_32/101021ja00137a021/authorship/2
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Conformational selectivity in molecular recognition: the influence of artificial receptors on the cis-trans isomerization of acylprolines
Molecular recognition: bis-acylguanidiniums provide a simple family of receptors for phosphodiesters
Self-Assembling, Chromogenic Receptors for the Recognition of Dicarboxylic Acids
Molecular recognition and catalysis. Acceleration of phosphodiester cleavage by a simple hydrogen-bonding receptor
Molecular recognition: hydrogen-bonding receptors that function in highly competitive solvents
Burkitt Lymphoma Daudi Cells Contain Two Distinct Farnesyltransferases with Different Divalent Cation Requirements
Aromatic-aromatic interactions in molecular recognition: a family of artificial receptors for thymine that shows both face-to-face and edge-to-face orientations
Carboxylic acid complexation by a synthetic analog of the "carboxylate-binding pocket" of vancomycin
Induced fit in synthetic receptors: nucleotide base recognition by a molecular hinge
FEP-Guided Selection of Bicyclic Heterocycles in Lead Optimization forNon-Nucleoside Inhibitors of HIV-1 Reverse Transcriptase
Catalytic Unfolding and Proteolysis of Cytochrome c Inducedby Synthetic Binding Agents
FEP-Guided Selection of Bicyclic Heterocycles in LeadOptimization for Non-Nucleoside Inhibitors of HIV-1Reverse Transcriptase [J. Am. Chem. Soc.2006, 128,15372−15373].
Pattern Recognition of Proteins Based on an Array ofFunctionalized Porphyrins
Directed Denaturation: Room Temperature and Stoichiometric Unfolding ofCytochrome c by a Metalloporphyrin Dimer
Terphenyl-Based Bak BH3 α-Helical Proteomimetics asLow-Molecular-Weight Antagonists of Bcl-xL
Design of a Synthetic Foldamer that Modifies the Growth of Calcite Crystals
Pattern-Based Detection of Different Proteins Using an Array of FluorescentProtein Surface Receptors
Structurally Simple, Potent, Plasmodium Selective Farnesyltransferase Inhibitors That Arrestthe Growth of Malaria Parasites
Design and Synthesis of Potent Nonpeptidic Farnesyltransferase InhibitorsBased on a Terphenyl Scaffold
Terephthalamide Derivatives as Mimetics of Helical Peptides: Disruption of the Bcl-xL/Bak Interaction
Rigid Macrocyclic Triamides as Anion Receptors: Anion-Dependent Binding Stoichiometries and 1H ChemicalShift Changes
Thermodynamic Aspects of Dicarboxylate Recognition by SimpleArtificial Receptors
Protein Farnesyltransferase Inhibitors Exhibit Potent Antimalarial Activity
Potent, Plasmodium-Selective Farnesyltransferase Inhibitors That Arrest the Growth of Malaria Parasites: Structure−Activity Relationships of Ethylenediamine-Analogue Scaffolds and Homology Model Validation
Design and Synthesis of Peptidomimetic Protein Farnesyltransferase Inhibitorsas Anti-Trypanosoma brucei Agents
Complexation control of pericyclic reactions: supramolecular effects on the intramolecular Diels-Alder reaction [Erratum to document cited in CA114(3):23229t]
Complexation control of pericyclic reactions: supramolecular effects on the intramolecular Diels-Alder reaction
Hydrogen bonding and molecular recognition: synthetic, complexation, and structural studies on barbiturate binding to an artificial receptor
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