Alexander Vinitsky - Academia.edu (original) (raw)
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Università degli Studi di Firenze (University of Florence)
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Papers by Alexander Vinitsky
Organic Letters, 2001
2-Aryl-2,2-difluoroacetamido-proline and pipecolate esters are high affinity FKBP12 ligands whose... more 2-Aryl-2,2-difluoroacetamido-proline and pipecolate esters are high affinity FKBP12 ligands whose rotamase inhibitory activity is comparable to that seen for the corresponding ketoamides. X-ray structural studies suggest that the fluorine atoms participate in discrete interactions with the Phe36 phenyl ring and the Tyr26 hydroxyl group, with the latter resembling a moderate-to-weak hydrogen bond.
Bioorganic & Medicinal Chemistry Letters, 2000
FKBP12 ligands have been prepared for a high-throughput¯uorescence polarization assay. K i s for ... more FKBP12 ligands have been prepared for a high-throughput¯uorescence polarization assay. K i s for FKBP12 rotamase inhibition by these ligands range from 1.3 mM to 32 nM, and their design is based on X-ray crystal structures of FKBP12 complexed with known immunophilin ligands.
Journal of Biological Chemistry, 1994
Organic Letters, 2001
2-Aryl-2,2-difluoroacetamido-proline and pipecolate esters are high affinity FKBP12 ligands whose... more 2-Aryl-2,2-difluoroacetamido-proline and pipecolate esters are high affinity FKBP12 ligands whose rotamase inhibitory activity is comparable to that seen for the corresponding ketoamides. X-ray structural studies suggest that the fluorine atoms participate in discrete interactions with the Phe36 phenyl ring and the Tyr26 hydroxyl group, with the latter resembling a moderate-to-weak hydrogen bond.
Bioorganic & Medicinal Chemistry Letters, 2000
FKBP12 ligands have been prepared for a high-throughput¯uorescence polarization assay. K i s for ... more FKBP12 ligands have been prepared for a high-throughput¯uorescence polarization assay. K i s for FKBP12 rotamase inhibition by these ligands range from 1.3 mM to 32 nM, and their design is based on X-ray crystal structures of FKBP12 complexed with known immunophilin ligands.
Journal of Biological Chemistry, 1994