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Wenschuh H., Volkmer-Engert R., Schmidt M., Schulz M., Schneider-Mergener J., Reineke U. Coherent membrane supports for parallel microsynthesis and screening of bioactive peptides. Biopolymers. 55:2000;188-206.
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Cross-reactive binding of cyclic peptides to an anti-TGFα antibody Fab fragment: An X-ray structural and thermodynamic analysis
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Hahn R., Welfle H., Wessner H., Zahn G., Scholz C., Seifert M., Harkins R., Schneider-Mergener J., Höhne W. Cross-reactive binding of cyclic peptides to an anti-TGFα antibody Fab fragment: an X-ray structural and thermodynamic analysis. J Mol Biol. 314:2001;293-309. This publication describes the conformational stabilization of a peptidic antibody epitope by cyclic analogues including disulfide and N terminus to sidechain cyclisation methods.
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11
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A modular approach to the spot synthesis of 1,2,5-trisubstituted hydantoins on cellulose membranes
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Heine N., Germeroth L., Schneider-Mergener J., Wenschuh H. A modular approach to the spot synthesis of 1,2,5-trisubstituted hydantoins on cellulose membranes. Tetrahedron Lett. 42:2001;227-230.
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Combining SPOT synthesis and native chemical ligation to generate large arrays of small protein domains
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Toepert F., Knaute T., Guffler S., Schneider-Mergener J. Combining SPOT synthesis and native chemical ligation to generate large arrays of small protein domains. Lebl M., Houghten R.A., Peptides, The Wave of the Future. Proceedings of the 2nd International and the 17th American Peptide Symposium. 2001;212-213 Kluwer Academic Publishers, Dordrecht. The combination of SPOT synthesis and native chemical ligation enables the rapid synthesis of large arrays of small proteins or protein modules.
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Peptides, The Wave of the Future. Proceedings of the 2nd International and the 17th American Peptide Symposium
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Toepert, F.1
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Identification of distinct antibody epitopes and mimotopes from a peptide array of 5520 randomly generated sequences
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Reineke U, Ivascu C, Schlief M, Landgraf C, Gericke S, Zahn G, Herzel H, Volkmer-Engert R, Schneider-Mergener J: Identification of distinct antibody epitopes and mimotopes from a peptide array of 5520 randomly generated sequences. J Immunol Methods 2002, in press.
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J Immunol Methods
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0035852860
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Dekker N., Cox R.C., Kramer A., Egmond M.R. Substrate specificity of the integral membrane protease OmpT determined by spatially addressed peptide libraries. Biochemistry. 40:2001;1694-1701. This paper is noteworthy as arrays of internally quenched peptides are used for the first time to characterise the subsite specificity of a large integral membrane enzyme.
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Biochemistry
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Akadémiai Kiadó: Budapest
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Reineke U, Bhargava S, Schutkowski M, Landgraf C, Germeroth L, Fischer G, Schneider-Mergener J: Spatial addressable fluorescence-quenched peptide libraries for the identification and characterization of protease substrates. In Peptides 1998 Proceedings of the 25th European Peptide Symposium. Akadémiai Kiadó: Budapest, 562-563.
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Peptides 1998 Proceedings of the 25th European Peptide Symposium
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19
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0035807963
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Binding specificity of Escherichia coli trigger factor
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Patzelt H., Rüdiger S., Brehmer D., Kramer G., Vorderwülbecke S., Schaffitzel E., Waitz A., Hesterkamp T., Dong L., Schneider-Mergener J., et al. Binding specificity of Escherichia coli trigger factor. Proc Natl Acad Sci USA. 98:2001;14244-14249.
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Application of the SPOT method to the identification of peptides and amino acids from the antibody paratope that contributes to antibody binding
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Laune D, Molina F, Ferrières G, Villard S, Bès C, Rieunier F, Chardès T, Granier C: Application of the SPOT method to the identification of peptides and amino acids from the antibody paratope that contributes to antibody binding. J Immunol Methods 2002: in press.
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Molecular basis for the substrate specificity of NEK6: Evidence that it does not phosphorylate the hydrophobic motif of S6K and SGK in vivo
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J Biol Chem
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Lizcano, J.M.1
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Bioconj Chem
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Melnyk, O.1
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