Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Freiburg

1989

Sustmann, R., Sicking, W. & Schulz, G.E. (1989). Das aktive Zentrum der Glutathionreduktase, ein Beispiel für Nahezu-Übergangsstrukturen. Angew. Chem. 101, 1056-1058. The active site of glutathione reductase: An example of near-transition state structures. Angew. Chem. Int. Ed. Engl. 28, 1023-1025.

Berger, A., Schiltz, E. & Schulz, G.E. (1989). Guanylate kinase from Saccharomyces cerevisiae: Isolation and characterization, crystallization and preliminary X-ray analysis, amino acid sequence and comparison with adenylate kinases. Eur. J. Biochem. 184, 433-443.

Karplus, P.A., Pai, E.F. & Schulz, G.E. (1989). A crystallographic study of the glutathione binding site of glutathione reductase at 0.3 nm resolution. Eur. J. Biochem. 178, 693-703.

Erdmann, V.A., Lippmann, C., Betzel, C., Dauter, Z., Wilson, K., Hilgenfeld, R., Hoven, J., Liesum, A., Saenger, W., Müller-Fahrnow, A., Hinrichs, W., Düvel, M., Schulz, G.E., Müller, C.W., Wittmann, H.G., Yonath, A., Weber, G., Stegen, K. & Plaas-Link, A. (1989). Crystallization of proteins under microgravity. FEBS Lett. 259, 194-198.

Weiss, M.S., Nestel, U., Wacker, T., Weckesser, J., Kreutz, W., Welte, W. & Schulz, G.E. (1989). The crystal structure of porin from Rhodobacter capsulatus at 6 Å resolution. FEBS Lett. 256, 143-146.

Karplus, P.A. & Schulz, G.E. (1989). Substrate binding and catalysis by glutathione reductase as derived from refined enzyme:substrate crystal structures at 2 Å resolution. J. Mol. Biol. 210, 163-180.

Hofmann, B.E., Bender, H. & Schulz, G.E. (1989). The three-dimensional structure of cyclodextrin glycosyltransferase from Bacillus circulans at 3.4 Å resolution. J. Mol. Biol. 209, 793-800.

Schirmer, R.H., Krauth-Siegel, R.L. & Schulz, G.E. (1989). Glutathione Reductase. In: Glutathione (eds. D. Dolphin, R. Poulson & O. Avramovic) John Wiley & Sons, New York, pp.553-596.

1988

Schulz, G.E. (1988). A critical evaluation of methods for prediction of protein secondary structures. In: Annual Reviews of Biophysics and Biophysical Chemistry (ed. D.M. Engelman), Annu.Rev.Inc., Palo Alto, vol.17, pp. 1-21.

Schulz, G.E. & Karplus, P.A. (1988). High-resolution structure and catalytic action of human glutathione reductase. Biochem. Soc. Transact. (London) 16, 81-84.

Pai, E.F., Karplus, P.A. & Schulz, G.E. (1988). Binding of NADPH and NADPH-analogs to glutathione reductase. Biochemistry 27, 4465-4474.

Karplus, P.A., Krauth-Siegel, R.L., Schirmer, R.H. & Schulz, G.E. (1988). Inhibition of human glutathione reductase by the nitrosourea drugs BCNU and HeCNU: a crystallographic analysis. Eur. J. Biochem. 171, 193-198.

Dreusicke, D. & Schulz, G.E. (1988). The switch between two conformations of adenylate kinase. J. Mol. Biol. 203, 1021-1028.

Müller, C.W. & Schulz, G.E. (1988). Structure of the complex of adenylate kinase from Escherichia coli with the inhibitor P,P-di(adenosine-5'-) pentaphosphate. J. Mol. Biol. 202, 909-912.

Dreusicke, D., Karplus, P.A. & Schulz, G.E. (1988). Refined structure of porcine cytosolic adenylate kinase at 2.1 Å resolution. J. Mol. Biol. 199, 359-371.

Reuner, C., Hable, M., Wilmanns, M., Kiefer, E., Schiltz, E. & Schulz, G.E. (1988). Amino acid sequence and three-dimensional structure of cytosolic adenylate kinase from carp muscle. Protein Sequences & Data Analysis 1, 335-343.

1987

Schulz, G.E. (1987). Structural and functional relationships in the adenylate kinase family. Cold Spring Harbor Symposia on Quantitative Biology, 52, 428-439.

Egner, U., Tomasselli, A.G. & Schulz, G.E. (1987). Structure of the complex of yeast adenylate kinase with the inhibitor P,P-di(adenosine-5'-)pentaphosphate at 2.6 Å resolution. J. Mol. Biol. 195, 649-658.

Karplus, P.A. & Schulz, G.E. (1987). The refined structure of glutathione reductase at 1.54 Å resolution. J. Mol. Biol. 195, 701-729.

Proba, K., Tomasselli, A.G., Nielsen, P. & Schulz, G.E. (1987). The cDNA sequence encoding cytosolic adenylate kinase from baker's yeast (Saccharomyces cerevisiae). Nucleic Acids Res. 15, 7187-7187.

Tomasselli, A.G. & Schulz, G.E. (1987). Structural and functional studies in the adenylate kinase family: on the way to new enzymes. CHIMICAoggi, Jan-Feb, 11-18.

Karplus, P.A. & Schulz, G.E. (1987). The active center of glutathione reductase at 1.54 Å resolution. In: Flavins and Flavoproteins (eds. D.B. McCormick & D.E. Edmondson), Walter de Gruyter, Berlin, pp. 45-54.

Massey, V., Ghisla, S., Ermler, U. & Schulz, G.E. (1987). Studies on the active site of human erythrocyte glutathione reductase using 6-SCN-FAD and 6-mercapto-FAD. In: Flavins and Flavoproteins (eds. D.B. McCormick & D.E. Edmondson), Walter de Gruyter, Berlin, pp. 79-84.

Schirmer, R.H. & Schulz, G.E. (1987). Pyridin nucleotide-linked sulfur metabolism. In: Pyridine Nucleotides (eds. D. Dolphin, R. Poulson & O. Avramovic) John Wiley & Sons, New York, pp. 333-379.

1986

Schulz, G.E., Schiltz, E., Tomasselli, A.G., Frank, R., Brune, M., Wittinghofer, A. &. Schirmer, R.H. (1986). Structural relationships in the adenylate kinase family. Eur. J. Biochem. 161, 127-132.

Dreusicke, D. & Schulz, G.E. (1986). The glycine-rich loop of adenylate kinase forms a giant anion hole. FEBS Lett. 208, 301-304.

1985

Karplus, P.A. & Schulz, G.E. (1985). Prediction of chain flexibility in proteins: A tool for the selection of peptide antigens. Naturwissenschaften 72, 212-213.