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

1984

Schulz, G.E. (1984). Definierte molekulare Wechselwirkungen als Basis biologischer Systeme (Defined molecular interactions are crucial for biology). Biologie in unserer Zeit 14, 121-124.

Rice, D.W., Schulz, G.E. & Guest, J.R. (1984). Structural relationship between glutathione reductase and lipoamide dehydrogenase. J. Mol. Biol. 174, 483-496.

Schulz, G.E. (1984). Binding mode and action of FAD in glutathione reductase. In: Flavins and Flavoproteins (eds. R.C. Bray, P.C. Engel & S.G. Mayhew) Walter de Gruyter, Berlin pp. 81-93.

Pai, E.F., Horn, E. & Schulz, G.E. (1984). The coenzyme binding site of glutathione reductase. In: Flavins and Flavoproteins (eds. R.C. Bray, P.C. Engel & S.G. Mayhew) Walter de Gruyter, Berlin, pp. 139-142.

Schirmer, R.H., Lederbogen, F., Krauth-Siegel, R.L., Eisen- brand, G., Schulz, G.E. & Jung, A. (1984). Flavoenzymes as drug targets. In: Flavins and Flavoproteins (eds. R.C. Bray, P.C. Engel & S.G. Mayhew) Walter de Gruyter, Berlin, pp. 847-859.

Max-Planck-Institut für Medizinische Forschung, Heidelberg

1984

Bilzer, M., Krauth-Siegel, R.L., Schirmer, R.H., Akerboom, T., Sies, H. & Schulz, G.E. (1984). Interaction of a glutathione S-conjugate with glutathione reductase. Kinetic and X-ray crystallographic studies. Eur. J. Biochem. 138, 373-378.

Frank, R., Trosin, M., Tomasselli, A.G., Schulz, G.E. & Schirmer, R.H. (1984). Mitochondrial adenylate kinase from bovine heart: homology with the cytosolic isoenzyme in the catalytic region. Eur. J. Biochem. 141, 629-636.

Wieland, B., Tomasselli, A.G., Noda, L.H., Frank, R. & Schulz, G.E. (1984). The amino acid sequence of GTP:AMP phosphotransferase: homology with cytosolic adenylate kinase. Eur. J. Biochem. 143, 331-339.

1983

Pai, E.F. & Schulz, G.E. (1983). The catalytic mechanism of glutathione reductase as derived from X-ray diffraction analyses of reaction intermediates. J. Biol. Chem. 258, 1752-1757.

Pai, E.F., Schulz, G.E., Tomasselli, A.G. & Noda, L.H. (1983). Preliminary X-ray studies on the GTP:AMP-phosphotransferase from beef heart mitochondria. J. Mol. Biol. 164, 347-350.

Schirmer, R.H., Schulz, G.E. & Untucht-Grau, R. (1983). Hypothesis: On the geometry of leukocyte NADPH-oxidase, a membrane flavoenzyme. Interferences from the structure of glutathione reductase. FEBS Lett. 154, 1-4.

Wierenga, R.K., Drenth, J. & Schulz, G.E. (1983). Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD- as well as NADPH-binding domains of glutathione reductase. J. Mol. Biol. 167, 725-739.

Schulz, G.E. (1983). Quantitative comparisons of protein chain folds. In: Numerical Taxonomy: Proceedings of the NATO Advanced Study Institute (Felsenstein, J., ed.) NATO Advanced Study Institute Series G (Ecological Sciences), No. 1, pp. 484-488, Springer Verlag, Heidelberg.

Schirmer, R.H. & Schulz, G.E. (1983). Flavoproteins of known three-dimensional structure. In: Biological Oxidations (Sund, H., Ullrich, V., eds.), pp. 93-113, Springer Verlag, Heidelberg.

1982

Williams, C.H. Jr., Arscott, L.D. & Schulz, G.E. (1982). Amino acid sequence homology between pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase. Proc. Natl. Adad. Sci. USA 79, 2199-2201.

Schulz, G.E. (1982). Strukturelle Organisation von Proteinen. (engl. Edit.) Structural organization of proteins. In: Biophysik, Ein Lehrbuch (Hoppe, W., Lohmann, W., Markl, H., eds.), pp. 396-406, Springer Verlag, Heidelberg.

Pai, E.F. & Schulz, G.E. (1982). Structure and catalytic cycle of the flavoenzyme glutathione reductase. In: Flavins and Flavoproteins (Massey, V., Williams, C.H., eds.), pp. 3-10, Elsevier/North Holland Biomed. Press, New York.

Arscott, L.D. & Williams, Jr., C.H. & Schulz, G.E. (1982). Pig heart lipoamide dehydrogenase and human erythrocyte glutathione reductase – homology in each of the three domains. In: Flavins and Flavoproteins (Massey, V., Williams, C.H., eds.), pp. 44-48, Elsevier/North Holland Biomed. Press, New York.

Pfaff, E., Mussgay, M., Böhm, H.O., Schulz, G.E. & Schaller, H. (1982). Antibodies against a preselected peptide recognize and neutralize foot and mouth disease virus. EMBO J. 1, 869-874.

Schulz, G.E., Schirmer, R.H. & Pai, E.F. (1982). The FAD-binding site of glutathione reductase. J. Mol. Biol. 160, 287-308.

Pai, E.F., Schirmer, R.H. & Schulz, G.E. (1982). Structure of the complex of the flavoenzyme glutathione reductase with NADPH. In: Structure of Complexes between Biopolymers and Low-Molecular-Weight Molecules (Bartmann, W., Snatzke, G., eds.), pp. 39-52, Heyden & Sons Acad. Publ., London.

1981

Leberman, R., Schulz, G.E. & Suck, D. (1981). Crystallization and preliminary X-ray diffraction data of the EF-Tu EF-Ts (EF-T) complex of E. coli. FEBS Lett. 124, 279-281.

Schulz, G.E. (1981). Protein-Differenzierung: Entwicklung neuartiger Proteine im Laufe der Evolution. Angew. Chem. 93, 143-151. Protein differentiation: emergence of novel proteins during evolution. Angew. Chem. Internatl. Edit. Engl. 20, 143-151.

Pai, E.F., Schirmer, R.H. & Schulz, G.E. (1981). The mode of binding of nucleotides to glutathione reductase. In: Structural Aspects of Recognition and Assembly in Biological Macromolecules (Balaban, M. Sussman, J. L., Traub, W., Yonath, A., eds.), pp. 75-86, Balaban ISS, Rehovot & Philadelphia.

Thieme, R., Pai, E.F., Schirmer, R.H. & Schulz, G.E. (1981). The three-dimensional structure of glutathione reductase at 2 Å resolution. J. Mol. Biol. 152, 763-782.

1980

Schulz, G.E. (1980). The significance of similarities between protein chain folds. In: Protein Folding (Jänicke, R., ed.), pp. 199-214, Elsevier/North Holland Biomed. Press, Amsterdam.

Schirmer, R.H., Pai, E.F., Schiltz, E., Schulz, G.E. & Untucht-Grau, R. (1980). Identification of peptides in electron density maps of proteins: sequencing strategies for proteins of known structure. In: Methods in Peptide and Protein Sequence Analysis (Birr, Chr., ed.), pp. 267-283, Elsevier/North Holland Biomed. Press, Amsterdam.

Schulz, G.E., Schirmer, R.H. & Pai, E.F. (1980). The three-dimensional structure of glutathione reductase and its substrate complexes at 0.3 nm resolution. In: Flavins and Flavoproteins (Yagi, K., Yamano, T., eds.), pp. 557-567, Japan Scientific Societies Press, Tokyo.

Schulz, G.E. (1980). Gene duplication in glutathione reductase. J. Mol. Biol. 138, 335-347.

1979

Schulz, G.E. (1979). Structural similarities between proteins. In: Protein Structure, Function and Industrial Applications (Hofmann, E., Pfeil, W., Aurich, H., eds.), pp. 133-142, Vol. 52, Proceedings of the 12^th FEBS Meeting, Dresden.

Schulz, G.E. & Schirmer, R.H. (1979). Principles of Protein Structure. Advanced Text in Chemistry, 314 Seiten, Springer Verlag, New York. About 20,000 copies sold. About 2000 citations in 2008. Translated to Japanese 1980, translated to Russian 1982.

Schulz, G.E. (1979). Nucleotide Binding Proteins. In: Molecular Mechanisms of Biological Recognition (Balaban, M., ed.), pp. 79-94, Elsevier/North Holland Biomed. Press, Amsterdam.

Untucht-Grau, R., Schulz, G.E. & Schirmer R.H. (1979). The C-terminal fragment of human glutathione reductase contains the postulated catalytic histidine. FEBS Lett. 105, 244-248.

Sander, C. & Schulz, G.E. (1979). Degeneracy of the information contained in amino acid sequences: evidence from overlaid genes. J. Mol. Evol. 13, 245-252.

1978

Schulz, G.E. & Rosenbaum, G. (1978). The multi-wire proportional chamber as an area detector for protein crystallography in comparison with photographic film; guidelines for future developments of area detectors. Nuclear Instruments and Methods 152, 205-208.

Schulz, G.E., Schirmer, R.H., Sachsenheimer, W. & Pai, E.F. (1978). The structure of the flavoenzyme glutathione reductase. Nature 273, 120-124.

Pai, E.F., Schirmer, R.H. & Schulz, G.E. (1978). Structural studies on crystalline glutathione reductase from human erythrocytes. In: Mechanism of Oxidizing Enzymes (Singer, T. P., Ondarza, R. N., eds.), pp.17-22, Elsevier/North Holland Biomed. Press, Amsterdam.

1977

Schulz, G.E. (1977). Regeln für Strukturen globulärer Proteine. Angew. Chem. 89, 24-33. Structural rules for globular proteins. Angew. Chem. Internatl. Edit. Engl. 16, 23-32.

Zappe, H.A., Krohne-Ehrich, G. & Schulz, G.E. (1977). Low resolution structure of human erythrocyte glutathione reductase. J. Mol. Biol. 113, 141-152.

Sachsenheimer, W. & Schulz, G.E. (1977). Two conformations of crystalline adenylate kinase. J. Mol. Biol. 114, 23-36.

Pai, E.F., Sachsenheimer, W., Schirmer, R.H. & Schulz, G.E. (1977). Substrate positions and induced-fit in crystalline adenylate kinase. J. Mol. Biol. 114, 37-45.

Schulz, G.E. (1977). Recognition of phylogenetic relationships from polypeptide chain fold similarities. J. Mol. Evol. 9, 339-342.

Kabsch, W., Gast, W.H., Schulz, G.E. & Leberman, R. (1977). Low resolution structure of partially trypsin-degraded polypeptide elongation factor EF-Tu from Escherichia coli. J. Mol. Biol. 117, 999-1012.

1976

Harmsen, A., Leberman, R. & Schulz, G.E. (1976). Comparison of protein crystal diffraction patterns and absolute intensities from synchrotron and conventional X-ray sources. J. Mol. Biol. 104, 311-314.

Leberman, R., Wittinghofer, A. & Schulz, G.E. (1976). Polymorphism in crystalline elongation factor Tu-GDP from Escherichia coli. J. Mol. Biol. 106, 951-961.

Gast, W.H., Leberman, R., Schulz, G.E. & Wittinghofer, A. (1976). Crystals of partially trypsin digested elongation factor Tu. J. Mol. Biol. 106, 943-950.

1975

Schulz, G.E. & Schirmer, R.H. (1975). Structural studies on crystalline adenylate kinases. In: Structure and Conformation of Nucleic Acids and Protein-Nucleic Acid Interactions (Sundaralingam, M., Rao, S. T., eds.), pp. 303-315, University Park Press, Baltimore.

Noda, L., Schulz, G.E. & von Zabern, I. (1975). Crystalline adenylate kinase from carp muscle. Eur. J. Biochem. 51, 229-235.

Schulz, G.E., Zappe, H., Worthington, D.J. & Rosemeyer, M.A. (1975). Crystals of human erythrocyte glutathione reductase. FEBS Lett. 54, 86-88.

1974

Schulz, G.E., Elzinga, M., Marx, F. & Schirmer, R.H. (1974). Three-dimensional structure of adenylate kinase. Nature 250, 120-123.

Schulz, G.E. & Schirmer, R.H. (1974). Topological comparison of adenylate kinase with other proteins. Nature 250, 142-144.

Schulz, G.E., Barry, C.D., Friedmann, J., Chou, P.Y., Fasman, G.D., Finkelstein, A.V., Lim, V.I., Ptitsyn, O.B., Kabat, E.A., Wu, T.T., Levitt, M., Robson, B. & Nagano, K. (1974). Comparison of predicted and experimentally determined secondary structure of adenylate kinase. Nature 250, 140-142.

1973

Schulz, G.E., Biedermann, K., Kabsch, W. & Schirmer, R.H. (1973). Low resolution structure of adenylate kinase. J. Mol. Biol. 80, 857-864.

1970

Schirmer, I., Schirmer, R.H., Schulz, G.E. & Thuma, E. (1970). Purification, characterization and crystallization of pork myokinase. FEBS Lett. 10, 333-338.

Cramer, F., von der Haar, F., Holmes, K.C., Saenger, W., Schlimme, E. & Schulz, G.E. (1970). Crystallization of phenylalanine specific transfer ribonucleic acid. J. Mol. Biol. 51, 523-530.