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Lectins: Carbohydrate-specific proteins that mediate cellular recognition
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Lis H, Sharon N Lectins: carbohydrate-specific proteins that mediate cellular recognition. Chem Rev. 98:1998;637-674.
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Lis, H.1
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Selectin-carbohydrate interactions: From natural ligands to designed mimics
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Simanek EE, McGarvey GJ, Jablonowski JA, Wong CH Selectin-carbohydrate interactions: from natural ligands to designed mimics. Chem Rev. 98:1998;833-862.
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Simanek, E.E.1
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0032985340
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Structure and conformation of complex carbohydrates of glycoproteins, glycolipids and bacterial polysaccharides
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Bush CA, Martin-Pastor M, Imberty A Structure and conformation of complex carbohydrates of glycoproteins, glycolipids and bacterial polysaccharides. Annu Rev Biophys Biomol Struct. 28:1999;269-293.
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Bush, C.A.1
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0031856212
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The second decade- Into the third millennium
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New perspectives for NMR spectroscopy are described.
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Wüthrich K The second decade- into the third millennium. Nat Struct Biol. 5:1998;492-496. New perspectives for NMR spectroscopy are described.
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Wüthrich, K.1
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0031851289
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New techniques in structural NMR-anisotropic interactions
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Modern NMR techniques that permit the determination of structures using methods other than nuclear Overhauser enhancements are clearly revealed.
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Prestegard JH New techniques in structural NMR-anisotropic interactions. Nat Struct Biol. 5:1998;517-522. Modern NMR techniques that permit the determination of structures using methods other than nuclear Overhauser enhancements are clearly revealed.
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Prestegard, J.H.1
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0032370218
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NMR investigations of carbohydrate protein interactions in solution
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An up-to-date review of the applications of NMR spectroscopy to studying sugar-protein molecular recognition processes.
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Poveda A, Jiménez-Barbero J NMR investigations of carbohydrate protein interactions in solution. Chem Soc Rev. 27:1998;133-143. An up-to-date review of the applications of NMR spectroscopy to studying sugar-protein molecular recognition processes.
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Poveda, A.1
Jiménez-Barbero, J.2
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0033577284
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Calculation of the Ramachandran potential of mean force for a disaccharide in aqueous solution
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Naidoo KJ, Brady JW Calculation of the Ramachandran potential of mean force for a disaccharide in aqueous solution. J Am Chem Soc. 121:1999;2244-2252.
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Naidoo, K.J.1
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8
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0032439584
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A comparison and chemometric analysis of several molecular mechanics force fields and parameters sets applied to carbohydrates
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Perez S, Imberty A, Engelsen SB, Gruza J, Mazeau K, Jimenez-Barbero J, Poveda A, Espinosa JF, van Eick BP, Johnson Get al. A comparison and chemometric analysis of several molecular mechanics force fields and parameters sets applied to carbohydrates. Carbohydr Res. 314:1999;141-155.
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Perez, S.1
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Mazeau, K.5
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Poveda, A.7
Espinosa, J.F.8
Van Eick, B.P.9
Johnson, G.10
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9
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0032483725
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Three bond C-O-C-C spin coupling constants in carbohydrates: Development of a Karplus relationship
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Bose B, Zhao S, Stenutz R, Cloran F, Bondo PB, Bondo G, Hertz B, Carmichael I, Serianni AS Three bond C-O-C-C spin coupling constants in carbohydrates: development of a Karplus relationship. J Am Chem Soc. 120:1998;11158-11173.
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Bose, B.1
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Bondo, P.B.5
Bondo, G.6
Hertz, B.7
Carmichael, I.8
Serianni, A.S.9
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10
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0000944192
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Long range proton-carbon coupling constants in conformational analysis of oligosaccharides
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Rundlof T, Kjellberg A, Damberg C, Nishida T, Widmalm G Long range proton-carbon coupling constants in conformational analysis of oligosaccharides. Magn Reson Chem. 36:1998;839-847.
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Rundlof, T.1
Kjellberg, A.2
Damberg, C.3
Nishida, T.4
Widmalm, G.5
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11
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0032211753
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Conformational changes due to vicinal glycosylation: The branched α-L-Rhap(1-2)[β-D-Galp(1-3)]β-D-Glc1-OMe trisaccharide compared with its parent disaccharides
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Kozar T, Nifant'ev EN, Grosskurth H, Dabrowski U, Dabrowski J Conformational changes due to vicinal glycosylation: the branched α-L-Rhap(1-2)[β-D-Galp(1-3)]β-D-Glc1-OMe trisaccharide compared with its parent disaccharides. Biopolymers. 46:1998;417-432.
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Kozar, T.1
Nifant'Ev, E.N.2
Grosskurth, H.3
Dabrowski, U.4
Dabrowski, J.5
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12
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0000271518
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Secondary H/D isotope effect on hydrogen bonded hydroxyl groups as a tool for recognizing distance constraints in conformational analysis of oligosaccharides
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Dabrowski J, Grosskurth H, Baust C, Nifant'ev EN Secondary H/D isotope effect on hydrogen bonded hydroxyl groups as a tool for recognizing distance constraints in conformational analysis of oligosaccharides. J Biomol NMR. 12:1998;161-172.
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J Biomol NMR
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, pp. 161-172
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Dabrowski, J.1
Grosskurth, H.2
Baust, C.3
Nifant'Ev, E.N.4
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13
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0348227872
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The use of chemical shifts of hydroxy protons of oligosaccharides as conformational probes for NMR studies in aqueous solution
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Evidence for persistent hydrogen bond interaction in branched trisaccharides
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Sandström C, Baumann H, Kenne L: The use of chemical shifts of hydroxy protons of oligosaccharides as conformational probes for NMR studies in aqueous solution. Evidence for persistent hydrogen bond interaction in branched trisaccharides. J Chem Soc Perkin Trans II 1998:2385-2393.
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J Chem Soc Perkin Trans
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Sandström, C.1
Baumann, H.2
Kenne, L.3
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14
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0032576191
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Effect of solvation on the rotation of the hydroxymethyl groups in carbohydrates
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Rockwell GC, Grindley TB Effect of solvation on the rotation of the hydroxymethyl groups in carbohydrates. J Am Chem Soc. 120:1998;10953-10963.
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J Am Chem Soc
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Rockwell, G.C.1
Grindley, T.B.2
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15
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0345588730
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Dynamic exchange between stabilized conformations predicted for hyaluronan tetrasaccharides: Comparison of molecular dynamic simulations with available NMR data
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Almond A, Brass A, Sheehan JK Dynamic exchange between stabilized conformations predicted for hyaluronan tetrasaccharides: comparison of molecular dynamic simulations with available NMR data. Glycobiology. 6:1998;1433-1444.
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Glycobiology
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Almond, A.1
Brass, A.2
Sheehan, J.K.3
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16
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0032932522
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Glycosyl inositol derivatives related to inositolphosphoglycan mediators: Synthesis, structure and biological activity
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Dietrich HJ, Chiara JL, Espinosa JF, Jimenez-Barbero J, Leon Y, Varela-Nieto I, Mato JM, Cano FH, Foces-Foces C, Martin-Lomas M Glycosyl inositol derivatives related to inositolphosphoglycan mediators: synthesis, structure and biological activity. Chem Eur J. 5:1999;320-336.
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Chem Eur J
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Dietrich, H.J.1
Chiara, J.L.2
Espinosa, J.F.3
Jimenez-Barbero, J.4
Leon, Y.5
Varela-Nieto, I.6
Mato, J.M.7
Cano, F.H.8
Foces-Foces, C.9
Martin-Lomas, M.10
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17
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0032174883
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Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules
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Ottiger M, Bax A Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules. J Biomol NMR. 12:1998;361-372.
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J Biomol NMR
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, pp. 361-372
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Ottiger, M.1
Bax, A.2
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18
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0000486350
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NMR investigation of oligosaccharide conformation using dipolar couplings in an aqueous dilute liquid crystalline medium
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The authors show how it is possible to deduce the average conformation of a tetrasaccharide in solution using residual dipolar C-H couplings, without using nuclear Overhauser enhancement information.
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Rundlof T, Landersjo C, Lycknert K, Maliniak A, Widmalm G NMR investigation of oligosaccharide conformation using dipolar couplings in an aqueous dilute liquid crystalline medium. Magn Reson Chem. 36:1998;773-776. The authors show how it is possible to deduce the average conformation of a tetrasaccharide in solution using residual dipolar C-H couplings, without using nuclear Overhauser enhancement information.
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Magn Reson Chem
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, pp. 773-776
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-
Rundlof, T.1
Landersjo, C.2
Lycknert, K.3
Maliniak, A.4
Widmalm, G.5
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19
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0032566781
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Residual dipolar couplings as new conformational restraints in isotopically 13C-enriched oligosaccharides
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C-H residual dipolar couplings within a simulated annealing protocol were used to deduce the solution conformation of sialyl lactose. No nuclear Overhauser enhancement information is necessary to deduce the major conformation in solution.
-
Kiddle GR, Homans SW Residual dipolar couplings as new conformational restraints in isotopically 13C-enriched oligosaccharides. FEBS Lett. 436:1998;128-130. C-H residual dipolar couplings within a simulated annealing protocol were used to deduce the solution conformation of sialyl lactose. No nuclear Overhauser enhancement information is necessary to deduce the major conformation in solution.
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(1998)
FEBS Lett
, vol.436
, pp. 128-130
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Kiddle, G.R.1
Homans, S.W.2
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20
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0032538016
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1H dipolar couplings in NMR spectra of field oriented oligosaccharides
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3, were estimated using easy experimental NMR methods. The potential use of this method to relatively position remote rings is described.
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3, were estimated using easy experimental NMR methods. The potential use of this method to relatively position remote rings is described.
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(1998)
J Am Chem Soc
, vol.120
, pp. 9366-9367
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Bolon, P.J.1
Prestegard, J.H.2
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21
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0033597639
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Derivation of the bound state conformation of a ligand in a weakly aligned ligand-protein complex
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As the alignment of a protein-ligand complex is substantially larger than that of the free ligand, residual dipolar couplings were used to deduce the toxin-bound conformation of a trisaccharide, without using TR-NOE experiments.
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Shimizu H, Donohue-Rolfe A, Homans SW Derivation of the bound state conformation of a ligand in a weakly aligned ligand-protein complex. J Am Chem Soc. 121:1999;5815-5816. As the alignment of a protein-ligand complex is substantially larger than that of the free ligand, residual dipolar couplings were used to deduce the toxin-bound conformation of a trisaccharide, without using TR-NOE experiments.
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(1999)
J Am Chem Soc
, vol.121
, pp. 5815-5816
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Shimizu, H.1
Donohue-Rolfe, A.2
Homans, S.W.3
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22
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0033525658
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Carbohydrate binding, quaternary structure, and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus
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Hamelryck TA, Loris R, Bouckaert J, Dao-Thi M, Strecker G, Imberty A, Fernandez E, Wyns L, Etzler ME Carbohydrate binding, quaternary structure, and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus. J Mol Biol. 286:1999;1161-1177.
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J Mol Biol
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Hamelryck, T.A.1
Loris, R.2
Bouckaert, J.3
Dao-Thi, M.4
Strecker, G.5
Imberty, A.6
Fernandez, E.7
Wyns, L.8
Etzler, M.E.9
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23
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0032491184
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Structural basis for the recognition of carbohydrates by human galectin 7
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A comparison of the structural features of galectin-7 with other galectins explains their different selectivity for natural ligands.
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Leonidas DD, Vatzaki EH, Vorum H, Celis JE, Madsen P, Acharya KR Structural basis for the recognition of carbohydrates by human galectin 7. Biochemistry. 37:1998;13930-13940. A comparison of the structural features of galectin-7 with other galectins explains their different selectivity for natural ligands.
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(1998)
Biochemistry
, vol.37
, pp. 13930-13940
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Leonidas, D.D.1
Vatzaki, E.H.2
Vorum, H.3
Celis, J.E.4
Madsen, P.5
Acharya, K.R.6
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24
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2642683194
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NMR investigations of carbohydrate-protein interactions: Refined three dimensional structure of the complex between hevein and methyl chitobioside
-
One of the few examples of a detailed three-dimensional structural analysis of a protein-carbohydrate complex in solution is described. Van der Waals interactions between the two GlcNAc chairs and tryptophan and tyrosine rings, as well as two protein-sugar hydrogen bonds, are responsible for the specific association.
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Asensio JL, Cañada FJ, Bruix M, Gonzalez C, Khiar N, Rodriguez Romero A, Jimenez-Barbero J NMR investigations of carbohydrate-protein interactions: refined three dimensional structure of the complex between hevein and methyl chitobioside. Glycobiology. 8:1998;569-577. One of the few examples of a detailed three-dimensional structural analysis of a protein-carbohydrate complex in solution is described. Van der Waals interactions between the two GlcNAc chairs and tryptophan and tyrosine rings, as well as two protein-sugar hydrogen bonds, are responsible for the specific association.
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(1998)
Glycobiology
, vol.8
, pp. 569-577
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-
Asensio, J.L.1
Cañada, F.J.2
Bruix, M.3
Gonzalez, C.4
Khiar, N.5
Rodriguez Romero, A.6
Jimenez-Barbero, J.7
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25
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0000178351
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A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity
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Simpson PJ, Bolam DN, Cooper A, Ciruela A, Hazlewood GP, Gilbert HJ, Williamson MP A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity. Structure. 7:1999;853-864.
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Structure
, vol.7
, pp. 853-864
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Simpson, P.J.1
Bolam, D.N.2
Cooper, A.3
Ciruela, A.4
Hazlewood, G.P.5
Gilbert, H.J.6
Williamson, M.P.7
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26
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0031768107
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Weak substrate binding to transport proteins studied by NMR
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Spooner PJ, O'Reilly WJ, Homans SW, Rutherford NG, Henderson PJ, Watts A Weak substrate binding to transport proteins studied by NMR. Biophys J. 75:1998;2794-2800.
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Biophys J
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Spooner, P.J.1
O'Reilly, W.J.2
Homans, S.W.3
Rutherford, N.G.4
Henderson, P.J.5
Watts, A.6
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27
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0033599567
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TROSY triple resonance four dimensional spectroscopy of a 46 ns tumbling protein
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Modern NMR techniques expand the range of application of NMR spectroscopy to the study large complexes in the near future.
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Yang D, Kay LE TROSY triple resonance four dimensional spectroscopy of a 46 ns tumbling protein. J Am Chem Soc. 121:1999;2571-2575. Modern NMR techniques expand the range of application of NMR spectroscopy to the study large complexes in the near future.
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(1999)
J Am Chem Soc
, vol.121
, pp. 2571-2575
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Yang, D.1
Kay, L.E.2
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28
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0032110303
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Conformational analysis of Chlamydia-specific disaccharide Kdo-(2->8)-Kdp-(2->O)-allyl in aqueous solution and bound to a monoclonal antibody: Observation of intermolecular transfer NOEs
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Sokolowski T, Haselhorst T, Scheffer K, Weisemann R, Kosma P, Brade H, Brade L, Peters T Conformational analysis of Chlamydia-specific disaccharide Kdo-(2->8)-Kdp-(2->O)-allyl in aqueous solution and bound to a monoclonal antibody: observation of intermolecular transfer NOEs. J Biomol NMR. 12:1998;123-133.
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J Biomol NMR
, vol.12
, pp. 123-133
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-
Sokolowski, T.1
Haselhorst, T.2
Scheffer, K.3
Weisemann, R.4
Kosma, P.5
Brade, H.6
Brade, L.7
Peters, T.8
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29
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0033580680
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NMR experiments reveal distinct antibody-bound conformations of a synthetic disaccharide representing a general structural element of bacterial lipopolysaccharide epitopes
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Haselhorst T, Espinosa JF, Jimenez-Barbero J, Sokolowski T, Kosma P, Brade H, Brade L, Peters T NMR experiments reveal distinct antibody-bound conformations of a synthetic disaccharide representing a general structural element of bacterial lipopolysaccharide epitopes. Biochemistry. 38:1999;6449-6459.
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Biochemistry
, vol.38
, pp. 6449-6459
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Haselhorst, T.1
Espinosa, J.F.2
Jimenez-Barbero, J.3
Sokolowski, T.4
Kosma, P.5
Brade, H.6
Brade, L.7
Peters, T.8
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30
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0032483135
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Solution structure of the complex between the B-subunit homopentamer of verotoxin VT-1 from Escherichia coli and the trisaccharide moiety of globotriaosylceramide
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Shimizu H, Field RA, Homans SW, Donohue-Rolfe A Solution structure of the complex between the B-subunit homopentamer of verotoxin VT-1 from Escherichia coli and the trisaccharide moiety of globotriaosylceramide. Biochemistry. 37:1998;11078-11082.
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Biochemistry
, vol.37
, pp. 11078-11082
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Shimizu, H.1
Field, R.A.2
Homans, S.W.3
Donohue-Rolfe, A.4
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31
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0033555207
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Bioaffinity NMR spectroscopy: Identification of an E-selectin antagonist in a substance mixture by transfer NOE
-
Transferred nuclear Overhauser enhancement methods can discriminate an E-selectin antagonist from a complex mixture of similar compounds. Perspectives on the application and drawbacks of the method are discussed.
-
Henrichsen D, Ernst B, Magnani JL, Wang WT, Meyer B, Peters T Bioaffinity NMR spectroscopy: identification of an E-selectin antagonist in a substance mixture by transfer NOE. Angew Chem Int Ed. 38:1999;98-102. Transferred nuclear Overhauser enhancement methods can discriminate an E-selectin antagonist from a complex mixture of similar compounds. Perspectives on the application and drawbacks of the method are discussed.
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(1999)
Angew Chem Int Ed
, vol.38
, pp. 98-102
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-
Henrichsen, D.1
Ernst, B.2
Magnani, J.L.3
Wang, W.T.4
Meyer, B.5
Peters, T.6
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32
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0033553844
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Characterization of ligand binding by saturation transfer difference NMR spectroscopy
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Mayer M, Meyer B Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew Chem Int Ed. 38:1999;1784-1788.
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(1999)
Angew Chem Int Ed
, vol.38
, pp. 1784-1788
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Mayer, M.1
Meyer, B.2
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33
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0033599483
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Stable isotope assisted NMR studies on 13C-enriched sialyl LewisX in solution and bound to E-selectin
-
13C-labeled sialyl LewisX was used to explore its conformation while bound to E-selectin. Quantitative nuclear Overhauser enhancement (NOE)-derived distances and vicinal scalar C-H couplings were used as input for time-averaged molecular dynamics simulations to derive the free and bound conformations of the tetrasaccharide. The reported conformations significantly differs from those deduced in previous studies.
-
13C-labeled sialyl LewisX was used to explore its conformation while bound to E-selectin. Quantitative nuclear Overhauser enhancement (NOE)-derived distances and vicinal scalar C-H couplings were used as input for time-averaged molecular dynamics simulations to derive the free and bound conformations of the tetrasaccharide. The reported conformations significantly differs from those deduced in previous studies.
-
(1999)
J Am Chem Soc
, vol.121
, pp. 2546-2551
-
-
Harris, R.1
Kiddle, G.R.2
Field, R.A.3
Milton, M.J.4
Ernst, B.5
Magnani, J.L.6
Homans, S.W.7
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34
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0032517379
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Observation of the anti-conformation of a glycosidic linkage in an antibody bound oligosaccharide
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Milton MJ, Bundle DR Observation of the anti-conformation of a glycosidic linkage in an antibody bound oligosaccharide. J Am Chem Soc. 120:1998;10547-10548.
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(1998)
J Am Chem Soc
, vol.120
, pp. 10547-10548
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-
Milton, M.J.1
Bundle, D.R.2
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35
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7144254472
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Conformer selection and differential restriction of ligand mobility by a plant lectin. Conformational behaviour of Galβ1-3GlcNAcβ1-R, Galβ1-3GalNAcβ1-R and Galβ1-2Galβ1-R' in the free state and complexed with galactoside-specific mistletoe lectin as revealed by random walk and conformational clustering molecular mechanics calculations, molecular dynamics simulations
-
and nuclear Overhauser experiments
-
Gilleron M, Siebert HC, Kaltner H, von der Lieth CW, Kozár T, Halkes KM, Korchagina EY, Bovin NV, Gabius HJ, Vliegenthart JFG Conformer selection and differential restriction of ligand mobility by a plant lectin. Conformational behaviour of Galβ1-3GlcNAcβ1-R, Galβ1-3GalNAcβ1-R and Galβ1-2Galβ1-R' in the free state and complexed with galactoside-specific mistletoe lectin as revealed by random walk and conformational clustering molecular mechanics calculations, molecular dynamics simulations and nuclear Overhauser experiments. Eur J Biochem. 252:1998;416-427.
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(1998)
Eur J Biochem
, vol.252
, pp. 416-427
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-
Gilleron, M.1
Siebert, H.C.2
Kaltner, H.3
Von Der Lieth, C.W.4
Kozár, T.5
Halkes, K.M.6
Korchagina, E.Y.7
Bovin, N.V.8
Gabius, H.J.9
Vliegenthart, J.F.G.10
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36
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0033135544
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Structure of heparin-derived tetrasaccharide complexed to the plasma protein antithrombin derived from NOEs, J-couplings and chemical shifts
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Hricovini M, Guerrini M, Bisio A Structure of heparin-derived tetrasaccharide complexed to the plasma protein antithrombin derived from NOEs, J-couplings and chemical shifts. Eur J Biochem. 261:1998;789-801.
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Eur J Biochem
, vol.261
, pp. 789-801
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Hricovini, M.1
Guerrini, M.2
Bisio, A.3
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37
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0032479020
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Thermodynamic and conformational implications of glycosidic rotamers preorganized for binding
-
Significant reduction of torsional flexibility failed to produce important entropic gains with the interaction of tethered ligands with a monoclonal antibody. Changes in the water structure around the tethers may contribute to the observed thermodynamic parameters.
-
Bundle DR, Alibes R, Nilar S, Otter A, Warwas M, Zhang P Thermodynamic and conformational implications of glycosidic rotamers preorganized for binding. J Am Chem Soc. 120:1998;5317-5318. Significant reduction of torsional flexibility failed to produce important entropic gains with the interaction of tethered ligands with a monoclonal antibody. Changes in the water structure around the tethers may contribute to the observed thermodynamic parameters.
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(1998)
J Am Chem Soc
, vol.120
, pp. 5317-5318
-
-
Bundle, D.R.1
Alibes, R.2
Nilar, S.3
Otter, A.4
Warwas, M.5
Zhang, P.6
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38
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0032838399
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Synthesis and conformational analysis of a conformationally constrained trisaccharide and complexation properties with concanavalin A
-
•], an important entropy gain is observed with the binding of a synthetically rigidified trisaccharide to the lectin concanavalin A. The entropy gain is offset by a significant lost of enthalpy.
-
•], an important entropy gain is observed with the binding of a synthetically rigidified trisaccharide to the lectin concanavalin A. The entropy gain is offset by a significant lost of enthalpy.
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(1999)
Chem Eur J
, vol.5
, pp. 2281-2294
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Navarre, N.1
Amiot, N.2
Van Oijen, A.3
Imberty, A.4
Poveda, A.5
Jimenez Barbero, J.6
Cooper, A.7
Nutley, M.A.8
Boons, G.-J.9
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39
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0032479045
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Role of water in the specific binding of mannose and mannooligosaccharides to concanavalin A
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Swaminathan CP, Surolia N, Surolia A Role of water in the specific binding of mannose and mannooligosaccharides to concanavalin A. J Am Chem Soc. 120:1998;5153-5159.
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(1998)
J Am Chem Soc
, vol.120
, pp. 5153-5159
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Swaminathan, C.P.1
Surolia, N.2
Surolia, A.3
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40
-
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0032484122
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Thermodynamics of binding of the core trimannoside of asparagine-linked carbohydrates and deoxy analogs to Dioclea grandiflora lectin
-
The binding of monodeoxy derivatives of the typical trimannoside core of glycoproteins to Dioclea grandiflora lectin was studied by microcalorimetry. The role of every hydroxyl group was deduced from the thermodynamic binding parameters.
-
Dam TK, Oscarson S, Brewer CF Thermodynamics of binding of the core trimannoside of asparagine-linked carbohydrates and deoxy analogs to Dioclea grandiflora lectin. J Biol Chem. 273:1998;32812-32817. The binding of monodeoxy derivatives of the typical trimannoside core of glycoproteins to Dioclea grandiflora lectin was studied by microcalorimetry. The role of every hydroxyl group was deduced from the thermodynamic binding parameters.
-
(1998)
J Biol Chem
, vol.273
, pp. 32812-32817
-
-
Dam, T.K.1
Oscarson, S.2
Brewer, C.F.3
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41
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0032484210
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Crystal structure of the lectin from Dioclea grandiflora complexed with core trimannoside of asparagine-linked carbohydrates
-
The analysis of the crystal structure of the Dioclea grandiflora lectin-trimannoside complex permits the interpretation of the thermodynamic data in structural terms. The role of water molecules is also explained.
-
Rozwarski DA, Swami BM, Brewer CF, Sacchettini JC Crystal structure of the lectin from Dioclea grandiflora complexed with core trimannoside of asparagine-linked carbohydrates. J Biol Chem. 273:1998;32818-32825. The analysis of the crystal structure of the Dioclea grandiflora lectin-trimannoside complex permits the interpretation of the thermodynamic data in structural terms. The role of water molecules is also explained.
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(1998)
J Biol Chem
, vol.273
, pp. 32818-32825
-
-
Rozwarski, D.A.1
Swami, B.M.2
Brewer, C.F.3
Sacchettini, J.C.4
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42
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0032484018
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Differential solvation of "core" trimannoside complexes of the Dioclea grandiflora lectin and concanavalin A detected by primary solvent isotope effects in isothermal titration microcalorimetry
-
The complete picture of the binding process between Dioclea grandiflora lectin and the core trimannoside is described and compared with that for concanavalin A. Although most of the binding features are explained, the fine details of the differential binding selectivity remain unclear.
-
Dam TK, Oscarson S, Sacchettini JC, Brewer CF Differential solvation of "core" trimannoside complexes of the Dioclea grandiflora lectin and concanavalin A detected by primary solvent isotope effects in isothermal titration microcalorimetry. J Biol Chem. 273:1998;32826-32832. The complete picture of the binding process between Dioclea grandiflora lectin and the core trimannoside is described and compared with that for concanavalin A. Although most of the binding features are explained, the fine details of the differential binding selectivity remain unclear.
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(1998)
J Biol Chem
, vol.273
, pp. 32826-32832
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-
Dam, T.K.1
Oscarson, S.2
Sacchettini, J.C.3
Brewer, C.F.4
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43
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0032134217
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Hydrogen bonding geometry of a protein-bound carbohydrate from water exchange-mediated cross relaxation
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Sayers EW, Weaver JL, Prestegard JH Hydrogen bonding geometry of a protein-bound carbohydrate from water exchange-mediated cross relaxation. J Biomol NMR. 12:1998;209-222.
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(1998)
J Biomol NMR
, vol.12
, pp. 209-222
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Sayers, E.W.1
Weaver, J.L.2
Prestegard, J.H.3
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44
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0033541092
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Transferred cross correlated relaxation: Application to the determination of sugar pucker in an aminoacylated tRNA-mimetic weakly bound to EF-Tu
-
The puckering of a protein-bound sugar within a RNA mimetic was determined using new NMR experiments. The information gained depends on the correlation time of the molecule and, therefore, the collected data are dominated by the complexed state.
-
Carlomagno T, Felli IC, Czech M, Fischer R, Sprinzl M, Griesinger C Transferred cross correlated relaxation: application to the determination of sugar pucker in an aminoacylated tRNA-mimetic weakly bound to EF-Tu. J Am Chem Soc. 121:1999;1945-1948. The puckering of a protein-bound sugar within a RNA mimetic was determined using new NMR experiments. The information gained depends on the correlation time of the molecule and, therefore, the collected data are dominated by the complexed state.
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(1999)
J Am Chem Soc
, vol.121
, pp. 1945-1948
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-
Carlomagno, T.1
Felli, I.C.2
Czech, M.3
Fischer, R.4
Sprinzl, M.5
Griesinger, C.6
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45
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0033541040
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Transferred cross correlated relaxation complements TR-NOE. Structure of an IL-4R derived peptide bound to STAT-6
-
•] was used to examine the conformational changes of a peptide when bound by a protein. Although isotope labeling is necessary, this methodology permits the expansion of knowledge concerning bound conformations of biomolecules.
-
•] was used to examine the conformational changes of a peptide when bound by a protein. Although isotope labeling is necessary, this methodology permits the expansion of knowledge concerning bound conformations of biomolecules.
-
(1999)
J Am Chem Soc
, vol.121
, pp. 1949-1953
-
-
Blommers, M.J.J.1
Stark, W.2
Jones, C.E.3
Head, D.4
Owen, C.E.5
Jahnke, W.6
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46
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0033577261
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Sugar mimics: An artificial receptor for cholera toxin
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Bernardi A, Checchia A, Brocca P, Sonnino S, Zuccotto F Sugar mimics: an artificial receptor for cholera toxin. J Am Chem Soc. 121:1999;2032-2036.
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(1999)
J Am Chem Soc
, vol.121
, pp. 2032-2036
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-
Bernardi, A.1
Checchia, A.2
Brocca, P.3
Sonnino, S.4
Zuccotto, F.5
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47
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0033582454
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Molten globule-like state of peanut lectin monomer retains its carbohydrate specificity
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Reddy GB, Srinivas VR, Ahmad N, Surolia A Molten globule-like state of peanut lectin monomer retains its carbohydrate specificity. J Biol Chem. 274:1999;4500-4503.
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(1999)
J Biol Chem
, vol.274
, pp. 4500-4503
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-
Reddy, G.B.1
Srinivas, V.R.2
Ahmad, N.3
Surolia, A.4
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48
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0033559148
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Recent insights into inhibition, structure, and mechanism of configuration-retaining glycosidases
-
A detailed revision of the current view of the structure/mechanism relationship for retaining glycosidase enzymes.
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Heightman TD, Vasella AT Recent insights into inhibition, structure, and mechanism of configuration-retaining glycosidases. Angew Chem Int Ed. 38:1999;750-770. A detailed revision of the current view of the structure/mechanism relationship for retaining glycosidase enzymes.
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(1999)
Angew Chem Int Ed
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, pp. 750-770
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-
Heightman, T.D.1
Vasella, A.T.2
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49
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0032566284
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Snapshots along an enzymatic reaction coordinate: Analysis of a retaining beta-glycoside hydrolase
-
A complete structural view of the pathway of the hydrolysis of a fluorosugar by a retaining glycosidase is provided by X-ray crystallography.
-
Davies GJ, Mackenzie L, Varrot A, Dauter M, Brzozowski AM, Schulein M, Withers SG Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase. Biochemistry. 37:1998;11707-11713. A complete structural view of the pathway of the hydrolysis of a fluorosugar by a retaining glycosidase is provided by X-ray crystallography.
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(1998)
Biochemistry
, vol.37
, pp. 11707-11713
-
-
Davies, G.J.1
MacKenzie, L.2
Varrot, A.3
Dauter, M.4
Brzozowski, A.M.5
Schulein, M.6
Withers, S.G.7
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50
-
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0033551103
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The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 Å resolution
-
Sulzenbacher G, Mackenzie LF, Wilson KS, Withers SG, Dupont C, Davies GJ The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 Å resolution. Biochemistry. 38:1999;4826-4833.
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(1999)
Biochemistry
, vol.38
, pp. 4826-4833
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-
Sulzenbacher, G.1
MacKenzie, L.F.2
Wilson, K.S.3
Withers, S.G.4
Dupont, C.5
Davies, G.J.6
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51
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0031715607
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Insights into transition state stabilization of the β-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants
-
Notenboom V, Birsan C, Nitz M, Rose DR, Warren RA, Withers SG Insights into transition state stabilization of the β-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants. Nat Struct Biol. 5:1998;812-818.
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(1998)
Nat Struct Biol
, vol.5
, pp. 812-818
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Notenboom, V.1
Birsan, C.2
Nitz, M.3
Rose, D.R.4
Warren, R.A.5
Withers, S.G.6
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52
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0040441605
-
Xylan binding subsite mapping in the xylanase from Penicillium simplicissimum using xylooligosaccharides as cryo-protectant
-
Schmidt A, Gbitz GM, Kratky C Xylan binding subsite mapping in the xylanase from Penicillium simplicissimum using xylooligosaccharides as cryo-protectant. Biochemistry. 38:1999;2403-2412.
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(1999)
Biochemistry
, vol.38
, pp. 2403-2412
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-
Schmidt, A.1
Gbitz, G.M.2
Kratky, C.3
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53
-
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0032578420
-
Thermophilic xylanase from Thermomyces lanuginosus: High-resolution X-ray structure and modeling studies
-
Gruber K, Klintschar G, Hayn M, Schlacher A, Steiner W, Kratky C Thermophilic xylanase from Thermomyces lanuginosus: high-resolution X-ray structure and modeling studies. Biochemistry. 37:1998;13475-13485.
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(1998)
Biochemistry
, vol.37
, pp. 13475-13485
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-
Gruber, K.1
Klintschar, G.2
Hayn, M.3
Schlacher, A.4
Steiner, W.5
Kratky, C.6
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54
-
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0033547747
-
Dual affinity labeling of the active site of human lysozyme with an N-acetyllactosamine derivative: First ligand assisted recognition of the second ligand
-
Muraki M, Harata K, Sugita N, Sato K Dual affinity labeling of the active site of human lysozyme with an N-acetyllactosamine derivative: first ligand assisted recognition of the second ligand. Biochemistry. 38:1999;540-548.
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(1999)
Biochemistry
, vol.38
, pp. 540-548
-
-
Muraki, M.1
Harata, K.2
Sugita, N.3
Sato, K.4
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55
-
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0032533450
-
High-resolution native and complex structures of thermostable beta-mannanase from Thermonospora fusca-substrate specificity in glycosyl hydrolase family 5
-
Hilge M, Gloor SM, Rypniewski W, Sauer O, Heightman TD, Zimmermann W, Winterhalter K, Piontek K High-resolution native and complex structures of thermostable beta-mannanase from Thermonospora fusca-substrate specificity in glycosyl hydrolase family 5. Structure. 6:1998;1433-1444.
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(1998)
Structure
, vol.6
, pp. 1433-1444
-
-
Hilge, M.1
Gloor, S.M.2
Rypniewski, W.3
Sauer, O.4
Heightman, T.D.5
Zimmermann, W.6
Winterhalter, K.7
Piontek, K.8
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56
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0032029412
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Conformational differences between Fuc(1-3)GlcNAc and its thioglycoside analogue
-
Aguilera B, Jimenez-Barbero J, Fernandez-Mayoralas A Conformational differences between Fuc(1-3)GlcNAc and its thioglycoside analogue. Carbohydr Res. 308:1998;19-27.
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(1998)
Carbohydr Res
, vol.308
, pp. 19-27
-
-
Aguilera, B.1
Jimenez-Barbero, J.2
Fernandez-Mayoralas, A.3
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57
-
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0033006065
-
Conformational differences between C- And O-glycosides: The C-mannobiose/O-mannobiose case
-
C-mannobiose presents a high population of conformers with a nonexoanomeric orientation of the α angle, demonstrating that, in general, C-and O-glycoside conformations are different.
-
Espinosa JF, Bruix M, Jarreton O, Skrydstrup T, Beau JM, Jiménez Barbero J Conformational differences between C- and O-glycosides: the C-mannobiose/O-mannobiose case. Chem Eur J. 4:1999;442-448. C-mannobiose presents a high population of conformers with a nonexoanomeric orientation of the α angle, demonstrating that, in general, C-and O-glycoside conformations are different.
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(1999)
Chem Eur J
, vol.4
, pp. 442-448
-
-
Espinosa, J.F.1
Bruix, M.2
Jarreton, O.3
Skrydstrup, T.4
Beau, J.M.5
Jiménez Barbero, J.6
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58
-
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0032508934
-
Preferred conformation of C-lactose at the free and peanut lectin bound states
-
C-lactose is bound by peanut lectin in the same conformation as O-lactose. Key hydrogen bonds between the protein and a glucose residue in the syn conformation provide the required interactions for the exclusive recognition of this conformer.
-
Ravishankar R, Surolia A, Vijayan M, Lim S, Kishi Y Preferred conformation of C-lactose at the free and peanut lectin bound states. J Am Chem Soc. 120:1998;11297-11303. C-lactose is bound by peanut lectin in the same conformation as O-lactose. Key hydrogen bonds between the protein and a glucose residue in the syn conformation provide the required interactions for the exclusive recognition of this conformer.
-
(1998)
J Am Chem Soc
, vol.120
, pp. 11297-11303
-
-
Ravishankar, R.1
Surolia, A.2
Vijayan, M.3
Lim, S.4
Kishi, Y.5
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59
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0032542581
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E. coli galactoside recognizes a high energy conformation of C-lactose, a non hydrolyzable substrate analogue. NMR investigations of the molecular complex
-
NMR spectroscopy and molecular modeling were used to demonstrate the exclusive recognition of a local minimum conformation of C-lactose by a glycosidase enzyme. This fact indirectly reveals the intrinsic flexibility of C-lactose and provides experimental proof for conformational distortion at an enzyme-binding and/or catalytic site.
-
Espinosa JF, Montero E, Vian A, Garcia JL, Dietrich H, Schmidt RR, Martin-Lomas M, Imberty A, Cañada J, Jimenez-Barbero J E. coli galactoside recognizes a high energy conformation of C-lactose, a non hydrolyzable substrate analogue. NMR investigations of the molecular complex. J Am Chem Soc. 120:1998;1309-1316. NMR spectroscopy and molecular modeling were used to demonstrate the exclusive recognition of a local minimum conformation of C-lactose by a glycosidase enzyme. This fact indirectly reveals the intrinsic flexibility of C-lactose and provides experimental proof for conformational distortion at an enzyme-binding and/or catalytic site.
-
(1998)
J Am Chem Soc
, vol.120
, pp. 1309-1316
-
-
Espinosa, J.F.1
Montero, E.2
Vian, A.3
Garcia, J.L.4
Dietrich, H.5
Schmidt, R.R.6
Martin-Lomas, M.7
Imberty, A.8
Cañada, J.9
Jimenez-Barbero, J.10
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60
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0032830561
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Bovine heart galectin-1 selects an unique (syn) conformation of C-lactose, a flexible lactose analogue
-
•] provide the required interactions for the exclusive recognition of the syn-Φψ conformer by bovine heart galectin-1
-
•] provide the required interactions for the exclusive recognition of the syn-Φψ conformer by bovine heart galectin-1.
-
(1999)
J Am Chem Soc
-
-
Asensio, J.L.1
Espinosa, J.F.2
Dietrich, H.3
Cañada, F.J.4
Schmidt, R.R.5
Martín Lomas, M.6
André, S.7
Gabius, H.J.8
Jiménez-Barbero, J.9
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61
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0033541043
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Synthesis, conformational analysis and phase characterization of a versatile self-assembling monoglucosyl diacylglycerol analogue
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Song J, Hollingsworth IR Synthesis, conformational analysis and phase characterization of a versatile self-assembling monoglucosyl diacylglycerol analogue. J Am Chem Soc. 121:1999;1851-1861.
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(1999)
J Am Chem Soc
, vol.121
, pp. 1851-1861
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Song, J.1
Hollingsworth, I.R.2
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62
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0033599579
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Structural study on O-glycopeptides: Glycosylation induced conformational changes of O-GlcNac, O-LacNAc, O-sialyl-LacNAc, and O-sialyl-Lewis X peptides of the mucin domain of MAdCAM-1
-
Wu W, Pasternack L, Hwanh DH, Koeller KM, Lin CC, Seitz O, Wong C-H Structural study on O-glycopeptides: glycosylation induced conformational changes of O-GlcNac, O-LacNAc, O-sialyl-LacNAc, and O-sialyl-Lewis X peptides of the mucin domain of MAdCAM-1. J Am Chem Soc. 121:1999;2409-2417.
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(1999)
J Am Chem Soc
, vol.121
, pp. 2409-2417
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-
Wu, W.1
Pasternack, L.2
Hwanh, D.H.3
Koeller, K.M.4
Lin, C.C.5
Seitz, O.6
Wong, C.-H.7
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63
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0032176417
-
13C labeling of the glycans
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13C labeling of the glycans. J Biomol NMR. 12:1998;385-394.
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(1998)
J Biomol NMR
, vol.12
, pp. 385-394
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-
Yamaguchi, Y.1
Kato, K.2
Shindo, M.3
Aoki, S.4
Furusho, K.5
Koga, K.6
Takahashi, N.7
Arata, Y.8
Shimada, I.9
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64
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0033616690
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Probing cell-surface architecture through synthesis: An NMR-determined structural motif for tumor-associated mucins
-
Glycopeptide synthesis, coupled with detailed NMR analysis, provides insights into the design of a basic sequence that is able to mimic an elongated mucin motif.
-
Live DH, Williams LJ, Kuduk SD, Schwarz JB, Glunz PW, Chen XT, Sames D, Kumar RA, Danishefsky SJ Probing cell-surface architecture through synthesis: an NMR-determined structural motif for tumor-associated mucins. Proc Natl Acad Sci USA. 96:1999;3489-3493. Glycopeptide synthesis, coupled with detailed NMR analysis, provides insights into the design of a basic sequence that is able to mimic an elongated mucin motif.
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(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 3489-3493
-
-
Live, D.H.1
Williams, L.J.2
Kuduk, S.D.3
Schwarz, J.B.4
Glunz, P.W.5
Chen, X.T.6
Sames, D.7
Kumar, R.A.8
Danishefsky, S.J.9
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65
-
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0032403790
-
The high degree of internal flexibility observed for an oligomannose oligosaccharide does not alter the overall topology of the molecule
-
Woods RJ, Pathiaseril A, Wormald MR, Edge CJ, Dwek EA The high degree of internal flexibility observed for an oligomannose oligosaccharide does not alter the overall topology of the molecule. Eur J Biochem. 258:1998;372-386.
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(1998)
Eur J Biochem
, vol.258
, pp. 372-386
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-
Woods, R.J.1
Pathiaseril, A.2
Wormald, M.R.3
Edge, C.J.4
Dwek, E.A.5
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66
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0033547753
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Conformational studies by NMR of the antimicrobial peptide, drosocin, and its non-glycosylated derivative: Effects of glycosylation on solution conformation
-
McManus AM, Otvos L.Jr., Hoffmann R, Craik DJ Conformational studies by NMR of the antimicrobial peptide, drosocin, and its non-glycosylated derivative: effects of glycosylation on solution conformation. Biochemistry. 38:1999;705-714.
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(1999)
Biochemistry
, vol.38
, pp. 705-714
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-
McManus, A.M.1
Otvos, L.jr.2
Hoffmann, R.3
Craik, D.J.4
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67
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0032146060
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A molecular basis for glycosylation induced conformational switching
-
The conformation and dynamics of different glycopeptides with natural and modified chitobioses was analyzed by NMR spectroscopy. The authors state that the N-acetyl groups on the sugars have a key influence on the glycopeptide conformation.
-
O'Connor SE, Imperiali B A molecular basis for glycosylation induced conformational switching. Chem Biol. 5:1998;427-437. The conformation and dynamics of different glycopeptides with natural and modified chitobioses was analyzed by NMR spectroscopy. The authors state that the N-acetyl groups on the sugars have a key influence on the glycopeptide conformation.
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(1998)
Chem Biol
, vol.5
, pp. 427-437
-
-
O'Connor, S.E.1
Imperiali, B.2
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68
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0031758846
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A structural role for glycosylation: Lessons from the hp model
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Hoffmann D, Florcke H A structural role for glycosylation: lessons from the hp model. Fold Des. 3:1998;337-343.
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(1998)
Fold des
, vol.3
, pp. 337-343
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-
Hoffmann, D.1
Florcke, H.2
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