STEINER, ROBERTO
STEINER, ROBERTO
Dipartimento di Scienze Biomediche - DSB
1,3-dipolar cycloaddition of phenyl azide to norbornene in aqueous solutions
1995 Wijnen, Jan W.; Steiner, Roberto; Engberts, Jan B. F. N.
A small-molecule activator of kinesin-1 drives remodeling of the microtubule network
2017 Randall, T. S.; Yip, Y. Y.; Wallock-Richards, D. J.; Pfisterer, K.; Sanger, A.; Ficek, W.; Steiner, R.; Beavil, A. J.; Parsons, M.; Dodding, M. P.
Anaerobic enzyme·substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase
2002 Steiner, R.; Kalk, K. H.; Dijkstrat, B. W.
Binding of Myomesin to Obscurin-Like-1 at the Muscle M-Band Provides a Strategy for Isoform-Specific Mechanical Protection
2017 Pernigo, S.; Fukuzawa, A.; Beedle, A. E. M.; Holt, M.; Round, A.; Pandini, A.; Garcia-Manyes, S.; Gautel, M.; Steiner, R.
Catalytic Mechanism of Cofactor-Free Dioxygenases and How They Circumvent Spin-Forbidden Oxygenation of Their Substrates
2015 Hernandez-Ortega, A.; Quesne, M. G.; Bui, S.; Heyes, D. J.; Steiner, R.; Scrutton, N. S.; De Visser, S. P.
Coagulation Factor XIII-A Subunit Missense Mutation in the Pathobiology of Autosomal Dominant Multiple Dermatofibromas
2020 Supsrisunjai, C.; Hsu, C. -K.; Michael, M.; Duval, C.; Lee, J. Y. W.; Yang, H. -S.; Huang, H. -Y.; Chaikul, T.; Onoufriadis, A.; Steiner, R.; Ariens, R. A. S.; Sarig, O.; Sprecher, E.; Eskin-Schwartz, M.; Samlaska, C.; Simpson, M. A.; Calonje, E.; Parsons, M.; Mcgrath, J. A.
Cofactor-independent oxidases and oxygenases
2010 Fetzner, S.; Steiner, R.
Crystal Structure of the Copper-Containing Quercetin 2,3-Dioxygenase from Aspergillus japonicus
2002 Fusetti, F.; Schroter, K. H.; Steiner, R.; Van Noort, P. I.; Pijning, T.; Rozeboom, H. J.; Kalk, K. H.; Egmond, M. R.; Dijkstra, B. W.
Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4- oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Rü61a: A cofactor-devoid dioxygenase of the α/β-hydrolase-fold superfamily
2007 Steiner, R.; Frerichs-Deeken, U.; Fetzner, S.
Cu-Dependent Quercetin Dioxygenase
2013 Steiner, R.
Direct evidence for a peroxide intermediate and a reactive enzyme-substrate-dioxygen configuration in a cofactor-free oxidase
2014 Bui, S.; Von Stetten, D.; Jambrina, P. G.; Prange, T.; Colloc'H, N.; De Sanctis, D.; Royant, A.; Rosta, E.; Steiner, R.
DNA variability in five crystal structures of d(CGCAATTGCG)
2004 Valls, N.; Wright, G.; Steiner, R.; Murshudov, G. N.; Subirana, J. A.
EPR characterization of the mononuclear Cu-containing Aspergillus japonicus quercetin 2,3-dioxygenase reveals dramatic changes upon anaerobic binding of substrates
2002 Kooter, I. M.; Steiner, R.; Dijkstra, B. W.; Van Noort, P. I.; Egmond, M. R.; Huber, M.
Fisher's information in maximum-likelihood macromolecular crystallographic refinement
2003 Steiner, R.; Lebedev, A. A.; Murshudov, G. N.
Flat model bulk solvent correction in the {programREFMAC}
2000 Steiner, R.; Murshudov, G. N.
Fragment-linking peptide design yields a high-affinity ligand for microtubule-based transport
2021 Cross, J. A.; Chegkazi, M. S.; Steiner, R.; Woolfson, D. N.; Dodding, M. P.
Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by x-ray crystallography: Inhibition, ordering effect, and mechanistic insights
2002 Steiner, R.; Kooter, I. M.; Dijkstra, B. W.
Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 2. X-ray absorption studies of native enzyme and anaerobic complexes with the substrates quercetin and myricetin
2002 Steiner, R.; Meyer-Klaucke, W.; Dijkstra, B. W.
Introduction to the virtual thematic issue on room-temperature biological crystallography
2023 Steiner, Roberto
Joint neutron/X-ray crystal structure of a mechanistically relevant complex of perdeuterated urate oxidase and simulations provide insight into the hydration step of catalysis
2021 Mcgregor, L.; Foldes, T.; Bui, S.; Moulin, M.; Coquelle, N.; Blakeley, M. P.; Rosta, E.; Steiner, R.