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0028946013
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Glycobiology: Towards understanding the function of sugars
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of special interest. A concise review addressing many relevant issues regarding the function and properties of sugars in glycoproteins.
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Dwek RA. Glycobiology: towards understanding the function of sugars. of special interest Biochem Soc Trans. 23:1995;1-25 A concise review addressing many relevant issues regarding the function and properties of sugars in glycoproteins.
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Biochem Soc Trans
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Dwek, R.A.1
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Biological roles of oligosaccharides: All of the theories are correct
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Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology. 3:1993;97-130.
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Glycobiology
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Varki, A.1
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0027519943
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Protein glycosylation. Structural and functional aspects
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Lis H, Sharon N. Protein glycosylation. Structural and functional aspects. Eur J Biochem. 218:1993;1-27.
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Eur J Biochem
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Lis, H.1
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Structures and function of the sugar chains of glycoproteins
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Kobata A. Structures and function of the sugar chains of glycoproteins. Eur J Biochem. 209:1992;483-501.
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Eur J Biochem
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Kobata, A.1
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0029016696
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Structure and epitope characterization of the O-specific polysaccharide of Proteus mirabilis O28 containing amides of D-galacturonic acid with L-serine and L-lysine
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Radziejewska-Lebrecht J, Shaskov AS, Vinogradov EV, Grosskurth H, Bartodziejska B, Rozalski A, Kaca W, Kononov LO, Chernyak AY, Mayer H, et al. Structure and epitope characterization of the O-specific polysaccharide of Proteus mirabilis O28 containing amides of D-galacturonic acid with L-serine and L-lysine. Eur J Biochem. 230:1995;705-712.
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Eur J Biochem
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Radziejewska-Lebrecht, J.1
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Grosskurth, H.4
Bartodziejska, B.5
Rozalski, A.6
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London: Academic Press
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Barclay AN, Birkeland ML, Brown MH, Beyers AD, Davis SJ, Somoza C, Williams AF. The Leukocyte Antigen Facts Book. 1993;Academic Press, London.
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The Leukocyte Antigen Facts Book
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Barclay, A.N.1
Birkeland, M.L.2
Brown, M.H.3
Beyers, A.D.4
Davis, S.J.5
Somoza, C.6
Williams, A.F.7
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10
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0028938503
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Composition and sequence specific resonance assignments of the heterogeneous N-linked glycan in the 13.6 kDa adhesion domain of human CD2 as determined by NMR on the intact glycoprotein
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13C NMR experiments at natural abundance. Similar approaches may be used for assigning NMR resonances of other moderately glycosylated glycoproteins that may lead to the structural study of additional glycoproteins by NMR. Such structural studies are still sparse and are urgently needed to learn more about the structural role of glycans in glycoproteins.
-
13C NMR experiments at natural abundance. Similar approaches may be used for assigning NMR resonances of other moderately glycosylated glycoproteins that may lead to the structural study of additional glycoproteins by NMR. Such structural studies are still sparse and are urgently needed to learn more about the structural role of glycans in glycoproteins.
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Biochemistry
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Wyss, D.F.1
Choi, J.S.2
Wagner, G.3
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11
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0029133626
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Conformation and function of the N-linked glycan in the adhesion domain of human CD2
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of outstanding interest. This paper describes the first three-dimensional NMR solution structure of an intact glycoprotein and the mobility of individual glycoforms of the single heterogeneous high-mannose N-glycan relative to the polypeptide by measuring the line widths of C-H groups throughout the glycoprotein. Detailed studies of the enzymatically treated human CD2 adhesion domain and a series of full-length human CD2 mutants reveal the importance of the glycan for the stability of the glycoprotein and hence the binding activity of this CD2 fragment.
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Wyss DF, Choi JS, Li J, Knoppers MH, Willis KJ, Arulanandam ARN, Smolyar A, Reinherz EL, Wagner G. Conformation and function of the N-linked glycan in the adhesion domain of human CD2. of outstanding interest Science. 269:1995;1273-1278 This paper describes the first three-dimensional NMR solution structure of an intact glycoprotein and the mobility of individual glycoforms of the single heterogeneous high-mannose N-glycan relative to the polypeptide by measuring the line widths of C-H groups throughout the glycoprotein. Detailed studies of the enzymatically treated human CD2 adhesion domain and a series of full-length human CD2 mutants reveal the importance of the glycan for the stability of the glycoprotein and hence the binding activity of this CD2 fragment.
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Science
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Wyss, D.F.1
Choi, J.S.2
Li, J.3
Knoppers, M.H.4
Willis, K.J.5
Arulanandam, A.R.N.6
Smolyar, A.7
Reinherz, E.L.8
Wagner, G.9
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12
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0028962403
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Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
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of special interest. The authors derived a model on the basis of X-ray and NMR data in combination with molecular modeling, explaining how oligosaccharides in the IgG from patients with rheumatoid arthritis, which are deficient in two terminal galactoses, can interact with complement through binding the lectin mannose-binding protein. This is a striking example of the fact that different glycoforms of a glycoprotein may display their sugar chains in quite different orientations with respect to the polypeptide and that this may give the attached oligosaccharides quite different functions.
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Malhotra R, Wormald MR, Rudd PM, Fischer PB, Dwek RA, Sim RB. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. of special interest Nat Med. 1:1995;237-243 The authors derived a model on the basis of X-ray and NMR data in combination with molecular modeling, explaining how oligosaccharides in the IgG from patients with rheumatoid arthritis, which are deficient in two terminal galactoses, can interact with complement through binding the lectin mannose-binding protein. This is a striking example of the fact that different glycoforms of a glycoprotein may display their sugar chains in quite different orientations with respect to the polypeptide and that this may give the attached oligosaccharides quite different functions.
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(1995)
Nat Med
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Malhotra, R.1
Wormald, M.R.2
Rudd, P.M.3
Fischer, P.B.4
Dwek, R.A.5
Sim, R.B.6
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14
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0028773130
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Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
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Fletcher CM, Harrison RA, Lachmann PJ, Neuhaus D. Structure of a soluble, glycosylated form of the human complement regulatory protein CD59. Structure. 2:1994;185-199.
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Structure
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Fletcher, C.M.1
Harrison, R.A.2
Lachmann, P.J.3
Neuhaus, D.4
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0027456631
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Protocol: Expression of soluble recombinant glycoproteins with predefined glycosylation: Application to the crystallization of the T-cell glycoprotein CD2
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Davis SJ, Puklavec MJ, Ashford DA, Harlos K, Jones EY, Stuart DI, Williams AF. Protocol: expression of soluble recombinant glycoproteins with predefined glycosylation: application to the crystallization of the T-cell glycoprotein CD2. Protein Eng. 6:1993;229-232.
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Davis, S.J.1
Puklavec, M.J.2
Ashford, D.A.3
Harlos, K.4
Jones, E.Y.5
Stuart, D.I.6
Williams, A.F.7
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0028774038
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Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5Å resolution
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Bodian DL, Jones EY, Harlos K, Stuart DI, Davis SJ. Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5Å resolution. Structure. 2:1994;755-766.
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Structure
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Bodian, D.L.1
Jones, E.Y.2
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Davis, S.J.5
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Virtual and solution conformations of oligosaccharides
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Cumming DA, Carver JP. Virtual and solution conformations of oligosaccharides. Biochemistry. 26:1987;6664-6676.
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Rutherford TJ, Partridge J, Weller CT, Homans SW. Characterization of the extent of internal motions in oligosaccharides. Biochemistry. 32:1993;12715-12724.
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Conformational analysis of the xylose-containing N-glycan of pineapple stem bromelain as part of the intact glycoprotein
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of special interest. A comparison between the conformational behaviour of the N-glycan of pineapple stem bromelain as part of the intact glycoprotein and a bromelain-derived glycopeptide (see [34]) shows interesting differences, suggesting that, in the intact glycoprotein, glycan - polypeptide interactions alter the conformation and dynamical behaviour of the N-glycan.
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Lommerse JPM, Kroon-Batenburg LMJ, Kamerling JP, Vliegenthart JFG. Conformational analysis of the xylose-containing N-glycan of pineapple stem bromelain as part of the intact glycoprotein. of special interest Biochemistry. 34:1995;8196-8206 A comparison between the conformational behaviour of the N-glycan of pineapple stem bromelain as part of the intact glycoprotein and a bromelain-derived glycopeptide (see [34]) shows interesting differences, suggesting that, in the intact glycoprotein, glycan - polypeptide interactions alter the conformation and dynamical behaviour of the N-glycan.
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Biochemistry
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Lommerse, J.P.M.1
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Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose
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Shaanan B, Lis H, Sharon N. Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose. Science. 254:1991;862-866.
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Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 Å resolution
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Varghese JN, Colman PM. Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 Å resolution. J Mol Biol. 221:1991;473-486.
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0028773158
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Structure of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: Role of the fucose moiety
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Bourne Y, Mazurier J, Legrand D, Rougé P, Montreuil J, Spik G, Cambillau C. Structure of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety. Structure. 2:1994;209-219.
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Stereochemistry of the N-glycosylation sites in glycoproteins
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of outstanding interest. This paper provides a survey of crystal structures of N-glycosylated proteins determined up to early 1995. It compares the conformation of the first Glc-NAc residue and the neighboring polypeptide sequence in terms of dihedral angles. It shows statistics of hydrogen bonds and hydrophobic interactions at such sites.
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Imberty A, Pérez S. Stereochemistry of the N-glycosylation sites in glycoproteins. of outstanding interest Protein Eng. 8:1995;699-709 This paper provides a survey of crystal structures of N-glycosylated proteins determined up to early 1995. It compares the conformation of the first Glc-NAc residue and the neighboring polypeptide sequence in terms of dihedral angles. It shows statistics of hydrogen bonds and hydrophobic interactions at such sites.
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Protein Eng
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Pérez, S.2
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0028361114
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Structure of phaseolin at 2.2 Å resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins
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Lawrence MC, Izard T, Beauchat M, Blagrove RJ, Colman PM. Structure of phaseolin at 2.2 Å resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. J Mol Biol. 238:1994;748-776.
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Lawrence, M.C.1
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Colman, P.M.5
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Abbadi, A.1
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Imperiali B, Shannon KL, Rickert KW. Role of peptide conformation in asparagine-linked glycosylation. J Am Chem Soc. 114:1992;7942-7944.
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Imperiali, B.1
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Conformations and internal mobility of a glycopeptide derived from bromelain using molecular dynamics simulations and NOESY analysis
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of special interest. The conformational and internal flexibility of a small glycopeptide from pineapple stem bromelain is described using a combination of MD simulations in water and NOE data. For the oligosaccharide part, a model was developed to estimate characteristic times for large reorientational motions around the glycosidic linkages associated with conformational transitions and two saccharide residues of the hexasaccharide showed such a flexibility. In contrast to the polypeptide, which was very mobile during the MD simulations, the rest of the glycan appears to be relatively rigid.
-
Lommerse JPM, Kroon-Batenburg LMJ, Kroon J, Kamerling JP, Vliegenthart JFG. Conformations and internal mobility of a glycopeptide derived from bromelain using molecular dynamics simulations and NOESY analysis. of special interest J Biomol NMR. 5:1995;79-94 The conformational and internal flexibility of a small glycopeptide from pineapple stem bromelain is described using a combination of MD simulations in water and NOE data. For the oligosaccharide part, a model was developed to estimate characteristic times for large reorientational motions around the glycosidic linkages associated with conformational transitions and two saccharide residues of the hexasaccharide showed such a flexibility. In contrast to the polypeptide, which was very mobile during the MD simulations, the rest of the glycan appears to be relatively rigid.
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J Biomol NMR
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Lommerse, J.P.M.1
Kroon-Batenburg, L.M.J.2
Kroon, J.3
Kamerling, J.P.4
Vliegenthart, J.F.G.5
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35
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0028819608
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Ligand binding by the immunoglobulin superfamily recognition molecule CD2 is glycosylation-independent
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Davis SJ, Davies EA, Barclay AN, Daenke S, Bodian DL, Jones EY, Stuart DI, Butters TD, Dwek RA, Van der Merwe PA. Ligand binding by the immunoglobulin superfamily recognition molecule CD2 is glycosylation-independent. J Biol Chem. 270:1995;369-375.
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Barclay, A.N.3
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Bodian, D.L.5
Jones, E.Y.6
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Butters, T.D.8
Dwek, R.A.9
Van der Merwe, P.A.10
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Joao HC, Dwek RA. Effects of glycosylation on protein structure and dynamics in ribonuclease B and some of its individual glycoforms. Eur J Biochem. 218:1993;239-244.
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Stabilization of proteins by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor
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of special interest. A detailed comparison of glycosylated with nonglycosylated PMP-C by NMR reveals that fucosylation decreases globally the dynamic fluctuations of the molecule and thus increases the stability of the glycopeptide.
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Crystal sturctures of native and inhibited forms of human cathepsin D: Implications for lysosomal targeting and drug design
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A structural motif in the variant surface glycoproteins of Trypanosoma brucei
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