ARTICLE;
CARBON NUCLEAR MAGNETIC RESONANCE;
CYCLOADDITION;
DRUG STRUCTURE;
DRUG SYNTHESIS;
PROTON NUCLEAR MAGNETIC RESONANCE;
CHEMICAL STRUCTURE;
CHEMISTRY;
DRUG ANTAGONISM;
DRUG DESIGN;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
SYNTHESIS;
AMINO ACYL-TRNA SYNTHETASES;
DEOXYADENOSINES;
DRUG DESIGN;
ENZYME INHIBITORS;
MAGNETIC RESONANCE SPECTROSCOPY;
MOLECULAR STRUCTURE;
TRIAZOLES;
VIDARABINE;
Marcel Dekker, New York, Nucleoside Analogues in Cancer Therapy
Cheson, B.D.; Keating, M.J.; William Plunkett, W. Nucleoside Analogues in Cancer Therapy; Marcel Dekker, New York, 1997, vol. Nucleoside Analogues in Cancer Therapy.
The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: The mechanism of discrimination between asparagine and aspartic acid
a) Berthert-Colominas, C., Seignovert, L., Ḧartlein, M., Grøtli, M., Cusack, S., Lebermann, R. The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid. EMBO J. 1998, 17, 2947-2960;
Crystal structure of a eukaryote/archaeon-like prolyl-tRNA synthetase and its complex with tRNAPro(CGG)
b) Yaremchuk, A.; Cusack, S.; Tukalo, M. Crystal structure of a eukaryote/archaeon-like prolyl-tRNA synthetase and its complex with tRNAPro(CGG). EMBO J.. 2000, 19, 4745-4758;
Succession of substrate induced conformational changes ensures the amino acid specificity of thermus thermophilus prolyltrna synthetase: Comparison with histidyl-tRNA synthetase
c) Yaremchuk, A., Tukalo, M., Grøtli, M., Cusack, S.A Succession of substrate induced conformational changes ensures the amino acid specificity of thermus thermophilus prolyltrna synthetase: Comparison with histidyl-tRNA synthetase. J. Mol. Biol., 2001, 309, 989-1002.
Structural and mechanistic basis of pre- and posttransfer editing by leucyl-tRNA synthetase
a) Lincecum, T.L., Tukalo, M., Yaremchuk, A., Mursinna, R.S., Williams, A.M., Sproat, B.S., Van Den Eynde, W. Link, A., Van Calenbergh S., Grøtli, M., Martinis S.A., Cusack, S., Structural and mechanistic basis of pre- and posttransfer editing by leucyl-tRNA synthetase. Mol. Cell 2003, 11, 951-963;
The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation
b) Tukalo, M.; Yaremchuk, A.; Fukunaga, R.; Yokoyama, S.; Cusack, S. The crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation. Nature Struct. Mol. Biol. 2005, 12, 923-930;
Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase
c) Fukunaga, R.; Yokoyama, S. Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase. J. Mol. Biol. 2006, 359, 901-912.
Synthesis and conformational analysis of 2′-deoxy-2′-(3- methoxybenzamido)adenosine, a rational-designed inhibitor of trypanosomal glyceraldehyde phosphate dehydrogenase (GAPDH)
a) Van Calenbergh, S.; Van Den Eeckhout, E.; Herdewijn, P.; De Bruyn, A.; Verlinde, C.L. M. J.; Hol, W.G. J.; Callens, M.; Van Aerschot, A.; Rozenski, J. Synthesis and conformational analysis of 2′-deoxy-2′-(3- methoxybenzamido)adenosine, a rational-designed inhibitor of trypanosomal glyceraldehyde phosphate dehydrogenase (GAPDH). Helv. Chim. Acta 1994, 77, 631-644;
Selective inhibition of trypanosomal glyceraldehyde-3-phosphate dehydrogenase by protein structure-based design: Toward new drugs for the treatment of sleeping sickness
b) Verlinde, C.L.M.J.; Callens, M.; Van Calenbergh, S.; Van Aerschot, A.; Herdewijn, P.; Hannaert, V.; Michels, P.A.; Opperdoes, F.R.; Hol, W.G.J. Selective inhibition of trypanosomal glyceraldehyde-3-phosphate dehydrogenase by protein structure-based design: toward new drugs for the treatment of sleeping sickness. J. Med. Chem. 1994, 37, 3605-3613;
Synthesis and structure-activity relationships of analogs of 2′-deoxy-2′-(3-methoxybenzamido)adenosine, a selective inhibitor of trypanosomal glycosomal glyceraldehyde-3-phosphate dehydrogenase
c) Van Calenbergh, S.; Verlinde, C.L.M.J.; Soenens, J.; De Bruyn, A.; Callens, M.; Blaton, N.M.; Peeters, O.M.; Rozenski, J.; Hol, W.G.J.; Herdewijn, P. Synthesis and structure-activity relationships of analogs of 2′-deoxy-2′-(3-methoxybenzamido)adenosine, a selective inhibitor of trypanosomal glycosomal glyceraldehyde-3-phosphate dehydrogenase. J. Med. Chem. 1995, 38, 3838-3849;
For reviews on the subject, see:, Marcel Dekker, New York
a) For reviews on the subject, see: Spatola, A.F. Chemistry and Biochemistry of Amino Acids, Peptides, and Proteins, Marcel Dekker, New York, 1983, pp. 267-357;
Tornoe, C.W.; Christensen, C.; Meldal, M. Peptidotriazoles on Solid Phase: [1,2,3]-Triazoles by Regiospecific Copper(I)-Catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides. J. Org. Chem. 2002, 67, 3057-3064.
b) Tornoe, C.W.; Christensen, C.; Meldal, M. Peptidotriazoles on Solid Phase: [1,2,3]-Triazoles by Regiospecific Copper(I)-Catalyzed 1,3-dipolar cycloadditions of terminal alkynes to azides. J. Org. Chem. 2002, 67, 3057-3064.
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Synthesis and incorporation of 2′-amino acid conjugated nucleotides into ribozymes
Matulic-Adamic, J.; Beigelman, L.; Dudycz, L.W.; Gonzalez, C.; Usman, N. Synthesis and incorporation of 2′-amino acid conjugated nucleotides into ribozymes. Bioorg. Med. Chem. Lett. 1995, 5, 2721-2724.
Synthesis of adenosine-based fluorosides containing a novel heterocyclic ring system
O'Mahony, G.; Ehrman, E.; Grøtli, M. Synthesis of adenosine-based fluorosides containing a novel heterocyclic ring system. Tetrahedron Lett. 2005, 46, 6745-6748.
Nucleic acid related compounds. 72. Removal of silyl protecting groups from hydroxyl functions with ammonium fluoride in methanol
Zhang, W.J.; Robins, M.J. Nucleic acid related compounds. 72. Removal of silyl protecting groups from hydroxyl functions with ammonium fluoride in methanol. Tetrahedron Lett. 1992, 33, 1177-1180.