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Results: 1-13 |
Results: 13
Heterozygous mutations in ANKH, the human ortholog of the mouse progressive ankylosis gene, result in craniometaphyseal dysplasia
Authors: Nurnberg, P Thiele, H Chandler, D Hohne, W Cunningham, ML Ritter, H Leschik, G Uhlmann, K Mischung, C Harrop, K Goldblatt, J Borochowitz, ZU Kotzot, D Westermann, F Mundlos, S Braun, HS Laing, N Tinschert, S
Citation: P. Nurnberg et al., Heterozygous mutations in ANKH, the human ortholog of the mouse progressive ankylosis gene, result in craniometaphyseal dysplasia, NAT GENET, 28(1), 2001, pp. 37-41
New series of vectors for phage display and prokaryotic expression of proteins
Authors: Paschke, M Zahn, G Warsinke, A Hohne, W
Citation: M. Paschke et al., New series of vectors for phage display and prokaryotic expression of proteins, BIOTECHNIQU, 30(4), 2001, pp. 720
Structure of jack bean chitinase
Authors: Hahn, M Hennig, M Schlesier, B Hohne, W
Citation: M. Hahn et al., Structure of jack bean chitinase, ACT CRYST D, 56, 2000, pp. 1096-1099
Atomic resolution structure of native porcine pancreatic elastase at 1.1 angstrom
Authors: Wurtele, M Hahn, M Hilpert, K Hohne, W
Citation: M. Wurtele et al., Atomic resolution structure of native porcine pancreatic elastase at 1.1 angstrom, ACT CRYST D, 56, 2000, pp. 520-523
Evolutionary transition pathways for changing peptide ligand specificity and structure
Authors: Hoffmuller, U Knaute, T Hahn, M Hohne, W Schneider-Mergener, J Kramer, A
Citation: U. Hoffmuller et al., Evolutionary transition pathways for changing peptide ligand specificity and structure, EMBO J, 19(18), 2000, pp. 4866-4874
Crystal structure of a phage library-derived single-chain Fv fragment complexed with turkey egg-white lysozyme at 2.0 angstrom resolution
Authors: Ay, J Keitel, T Kuttner, G Wessner, H Scholz, C Hahn, M Hohne, W
Citation: J. Ay et al., Crystal structure of a phage library-derived single-chain Fv fragment complexed with turkey egg-white lysozyme at 2.0 angstrom resolution, J MOL BIOL, 301(2), 2000, pp. 239-246
X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonasaeruginosa: Basis of substrate specificity
Authors: Keitel, T Diehl, A Knaute, T Stezowski, JJ Hohne, W Gorisch, H
Citation: T. Keitel et al., X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonasaeruginosa: Basis of substrate specificity, J MOL BIOL, 297(4), 2000, pp. 961-974
Changing the antigen binding specificity by single point mutations of an anti-p24 (HIV-1) antibody
Authors: Winkler, K Kramer, A Kuttner, G Seifert, M Scholz, C Wessner, H Schneider-Mergener, J Hohne, W
Citation: K. Winkler et al., Changing the antigen binding specificity by single point mutations of an anti-p24 (HIV-1) antibody, J IMMUNOL, 165(8), 2000, pp. 4505-4514
Characterizing and optimizing protease/peptide inhibitor interactions, a new application for spot synthesis
Authors: Hilpert, K Hansen, G Wessner, H Schneider-Mergener, J Hohne, W
Citation: K. Hilpert et al., Characterizing and optimizing protease/peptide inhibitor interactions, a new application for spot synthesis, J BIOCHEM, 128(6), 2000, pp. 1051-1057
Investigation of a tetracycline-regulated phage display system
Authors: Zahn, G Skerra, A Hohne, W
Citation: G. Zahn et al., Investigation of a tetracycline-regulated phage display system, PROTEIN ENG, 12(12), 1999, pp. 1031-1034
Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments
Authors: Welfle, K Misselwitz, R Hausdorf, G Hohne, W Welfle, H
Citation: K. Welfle et al., Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments, BBA-PROT ST, 1431(1), 1999, pp. 120-131
Characterization of neutralizing anti-pre-S1 and anti-pre-S2 (HBV) monoclonal antibodies and their fragments
Authors: Kuttner, G Kramer, A Schmidtke, G Giessmann, E Dong, L Roggenbuck, D Scholz, C Seifert, M Stigler, RD Schneider-Mergener, J Porstmann, T Hohne, W
Citation: G. Kuttner et al., Characterization of neutralizing anti-pre-S1 and anti-pre-S2 (HBV) monoclonal antibodies and their fragments, MOL IMMUNOL, 36(10), 1999, pp. 669-683
Interaction of the capsid protein p24 (HIV-1) with sequence-derived peptides: Influence on p24 dimerization
Authors: Hilpert, K Behlke, J Scholz, C Misselwitz, R Schneider-Mergener, J Hohne, W
Citation: K. Hilpert et al., Interaction of the capsid protein p24 (HIV-1) with sequence-derived peptides: Influence on p24 dimerization, VIROLOGY, 254(1), 1999, pp. 6-10
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