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Roberto A. Steiner

Observed names: R. A. Steiner, R. Steiner, R.A. Steiner, Roberto A Steiner, Roberto A. Steiner A, Roberto Steiner, Roberto A. Steiner, Steiner, Roberto, Steiner, Roberto A, Steiner, Roberto A.
Observed institutions: University of Padua, University of Groningen, King's College London, Deutsches Elektronen-Synchrotron DESY, British Heart Foundation, IFOM, European Molecular Biology Laboratory, European Molecular Biology Laboratory, Unilever Research and Development Vlaardingen, University of York
ORCID: 0000-0001-7084-9745
Observed ORCID: 0000-0001-7084-9745
OpenAlex ID: A5028055588
REFMAC 5 for the refinement of macromolecular crystal structures
2011 · Garib N. Murshudov, Pavol Skubák, et al. · Acta Crystallographica Section D Biological Crystallography · 8,321
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REFMAC 5 dictionary: organization of prior chemical knowledge and guidelines for its use
2004 · Alexei A. Vagin, Roberto A. Steiner, et al. · Acta Crystallographica Section D Biological Crystallography · 1,351
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The CCP 4 suite: integrative software for macromolecular crystallography
2023 · Jon Agirre, Mihaela Atanasova, et al. · Acta Crystallographica Section D Structural Biology · 910
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Crystal Structure of the Copper-Containing Quercetin 2,3-Dioxygenase from Aspergillus japonicus
2002 · Fabrizia Fusetti, Klaus H Schröter, et al. · Structure · 220
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Anaerobic enzyme⋅substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase
2002 · Roberto A. Steiner, Kor H. Kalk, et al. · Proceedings of the National Academy of Sciences · 178
Cofactor-independent oxidases and oxygenases
2010 · Susanne Fetzner, Roberto A. Steiner · Applied Microbiology and Biotechnology · 144
The Dynamic Localization of Cytoplasmic Dynein in Neurons Is Driven by Kinesin-1
2016 · Alison E. Twelvetrees, Stefano Pernigo, et al. · Neuron · 122
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Targeted redox inhibition of protein phosphatase 1 by Nox4 regulates eIF2α‐mediated stress signaling
2016 · Celio XC Santos, Anne D Hafstad, et al. · The EMBO Journal · 117
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Structural Basis for Kinesin-1:Cargo Recognition
2013 · Stefano Pernigo, Anneri Lamprecht, et al. · Science · 117
Structural and functional studies on the extracellular domain of BST2/tetherin in reduced and oxidized conformations
2010 · Heidi L. Schubert, Qianting Zhai, et al. · Proceedings of the National Academy of Sciences · 95
EPR characterization of the mononuclear Cu‐containing Aspergillus japonicus quercetin 2,3‐dioxygenase reveals dramatic changes upon anaerobic binding of substrates
2002 · Ingeborg M. Kooter, Roberto A. Steiner, et al. · European Journal of Biochemistry · 92
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Catalytic Mechanism of Cofactor-Free Dioxygenases and How They Circumvent Spin-Forbidden Oxygenation of Their Substrates
2015 · Aitor Hernández-Ortega, Matthew G. Quesne, et al. · Journal of the American Chemical Society · 89
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A small-molecule activator of kinesin-1 drives remodeling of the microtubule network
2017 · Thomas S. Randall, Yan Y. Yip, et al. · Proceedings of the National Academy of Sciences · 80
Structural basis for cofactor-independent dioxygenation of N -heteroaromatic compounds at the α/β-hydrolase fold
2009 · Roberto A. Steiner, Helge J. Janssen, et al. · Proceedings of the National Academy of Sciences · 77
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 · Roberto A. Steiner, Ingeborg M. Kooter, et al. · Biochemistry · 74
Structural insight into M-band assembly and mechanics from the titin-obscurin-like-1 complex
2010 · Stefano Pernigo, Atsushi Fukuzawa, et al. · Proceedings of the National Academy of Sciences · 71
The light chains of kinesin-1 are autoinhibited
2016 · Yan Y. Yip, Stefano Pernigo, et al. · Proceedings of the National Academy of Sciences · 63
Fisher's information in maximum-likelihood macromolecular crystallographic refinement
2003 · Roberto A. Steiner, Andrey A. Lebedev, et al. · Acta Crystallographica Section D Biological Crystallography · 61
SKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain
2017 · Anneri Sanger, Yan Y. Yip, et al. · Journal of Cell Science · 47
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Direct Evidence for a Peroxide Intermediate and a Reactive Enzyme–Substrate–Dioxygen Configuration in a Cofactor‐free Oxidase
2014 · Soi Bui, David von Stetten, et al. · Angewandte Chemie International Edition · 47
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Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors
2018 · Stefano Pernigo, Magda S Chegkazi, et al. · eLife · 44
Rapid and efficient room-temperature serial synchrotron crystallography using the CFEL TapeDrive
2022 · Kara A Zielinski, Andreas Prester, et al. · IUCrJ · 39
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New insight into cofactor-free oxygenation from combined experimental and computational approaches
2016 · Soi Bui, Roberto A Steiner · Current Opinion in Structural Biology · 39
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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 · Roberto A. Steiner, Wolfram Meyer-Klaucke, et al. · Biochemistry · 37
Origin of the Proton-transfer Step in the Cofactor-free (1H)-3-Hydroxy-4-oxoquinaldine 2,4-Dioxygenase
2014 · Aitor Hernandez-Ortega, Matthew G. Quesne, et al. · Journal of Biological Chemistry · 35
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Works count: 121
Citation count: 12,830
H-index: 28
I10-index: 42
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