Publikationen von Ilme Schlichting

Fedorov, R.; Hartmann, E.; Ghosh, D. K.; Schlichting, I.: Structural basis for the specificity of the nitric-oxide synthase inhibitors W1400 and Nomega-propyl-L-Arg for the inducible and neuronal isoforms. The Journal of Biological Chemistry 278 (46), S. 45818 - 45825 (2003)

Kottke, T.; Dick, B.; Fedorov, R.; Schlichting, I.; Deutzmann, R.; Hegemann, P.: Irreversible photoreduction of flavin in a mutated Phot-LOV1 domain. Biochemistry 42 (33), S. 9854 - 9862 (2003)

Fedorov, R.; Schlichting, I.; Hartmann, E.; Domratcheva, T.; Fuhrmann, M.; Hegemann, P.: Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii. Biophysical Journal 84 (4), S. 2474 - 2482 (2003)

Pylypenko, O.; Rak, A.; Reents, R.; Niculae, A.; Sidorovitch, V.; Cioaca, M.-D.; Bessolitsyna, E.; Thomä, N. H.; Waldmann, H.; Schlichting, I. et al.; Goody, R. S.; Alexandrov, K.: Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase. Molecular Cell 11 (2), S. 483 - 494 (2003)

Fedorov, R.; Ghosh, D. K.; Schlichting, I.: Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes. Archives of Biochemistry and Biophysics 409 (1), S. 25 - 31 (2003)

Kulik, V.; Weyand, M.; Seidel, R.; Niks, D.; Arac, D.; Dunn, M. F.; Schlichting, I.: On the role of αThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase. Journal of Molecular Biology (London) 324 (4), S. 677 - 690 (2002)

Zerbe, K.; Pylypenko, O.; Vitali, F.; Zhang, W.; Rouse, S.; Heck, M.; Vrijbloed, J. W.; Bischoff, D.; Bister, B.; Süssmuth, R. D. et al.; Pelzer, S.; Wohlleben, W.; Robinson, J. A.; Schlichting, I.: Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis. The Journal of Biological Chemistry 277 (49), S. 47476 - 47485 (2002)

Reinstein, J.; Schlichting, I.: Mechanism, specificity and inhibition of nucleotide kinases. Abstracts of Papers of the American Chemical Society 223, S. 31 - 32 (2002)

Weyand, M.; Schlichting, I.; Herde, P.; Marabotti, A.; Mozzarelli, A.: Crystal structure of the beta Ser178--> Pro mutant of tryptophan synthase. A "knock-out" allosteric enzyme. The Journal of Biological Chemistry 277 (12), S. 10653 - 10660 (2002)

Weyand, M.; Schlichting, I.; Marabotti, A.; Mozzarelli, A.: Crystal structures of a new class of allosteric effectors complexed to tryptophan synthase. The Journal of Biological Chemistry 277 (12), S. 10647 - 10652 (2002)

Groot, M.-L.; Vos, M. H.; Schlichting, I.; van Mourik, F.; Joffre, M.; Lambry, J.-C.; Martin, J.-L.: Coherent infrared emission from myoglobin crystals: An electric field measurement. Proceedings of the National Academy of Sciences of the United States of America 99 (3), S. 1323 - 1328 (2002)

Rak, A.; Reents, R.; Pylypenko, O.; Niculae, A.; Sidorovitch, V.; Thomä, N. H.; Waldmann, H.; Schlichting, I.; Goody, R. S.; Alexandrov, K.: Crystallization and preliminary X-ray diffraction analysis of the Rab escort protein-1 in complex with Rab geranylgeranyltransferase. Journal of Structural Biology 136 (2), S. 158 - 161 (2001)

Weyand, M.; Schlichting, I.: Structural basis for the impaired channeling and allosteric inter-subunit communication in the βA169L/βC170W mutant of tryptophan synthase. The Journal of Biological Chemistry 275 (52), S. 41058 - 41063 (2000)

Schlichting, I.; Chu, K.: Trapping intermediates in the crystal: ligand binding to myoglobin. Current Opinion in Structural Biology 10 (6), S. 744 - 752 (2000)

Ostermann, N.; Lavie, A.; Padiyar, S.; Brundiers, R.; Veit, T.; Reinstein, J.; Goody, R. S.; Konrad, M.; Schlichting, I.: Potentiating AZT activation: Structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP. Journal of Molecular Biology (London) 304 (1), S. 43 - 53 (2000)

Ostermann, N.; Lavie, A.; Padiyar, S.; Brundiers, R.; Veit, T.; Reinstein, J.; Goody, R. S.; Konrad, M.; Schlichting, I.: Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP. Journal of Molecular Biology (London) 304 (1), S. 43 - 53 (2000)

Schlichting, I.: Crystallographic structure determination of unstable species. Accounts of Chemical Research 33 (8), S. 532 - 538 (2000)

Ostermann, N.; Schlichting, I.; Brundiers, R.; Konrad, M.; Reinstein, J.; Veit, T.; Goody, R. S.; Lavie, A.: Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate. Structure 8 (6), S. 629 - 642 (2000)

Schlichting, I.; Berendzen, J.; Chu, K.; Stock, A. M.; Maves, S. A.; Benson, D. E.; Sweet, R. M.; Ringe, D.; Petsko, G. A.; Sligar, S. G.: The catalytic pathway of cytochrome P450cam at atomic resolution. Science 287, S. 1615 - 1622 (2000)

Brunori, M.; Vallone, B.; Cutruzzola, F.; Travaglini−Allocatelli, C.; Berendzen, J.; Chu, K.; Sweet, R. M.; Schlichting, I.: The role of cavities in protein dynamics: Crystal structure of a photolytic intermediate of a mutant myoglobin. Proceedings of the National Academy of Sciences of the United States of America 97 (5), S. 2058 - 2063 (2000)