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Time-resolved structural analysis of an RNA-cleaving DNA catalyst.
Nature 601, 144-149 (2022)
https://doi.org/10.1038/s41586-021-04225-4
- Kirchgässler N, Rosenbach H, Span I
Stability and Activity of the 10–23 DNAzyme Under Molecular Crowding Conditions.
Methods in Molecular Biology 2439, 79-89 (2022)
https://doi.org/10.1007/978-1-0716-2047-2_6
- Rosenbach H, Span I
Obtaining Crystals of Nucleic Acids in Complex with the Protein U1A Using the Soaking Method
Methods in Molecular Biology 2439, 105-115 (2022)
https://doi.org/10.1007/978-1-0716-2047-2_8
- Rosenbach H, Steger G
Fluorescence-Based Kinetic Measurements for RNA-Cleaving DNAzymes
Methods in Molecular Biology 2439, 65-77 (2022)
https://doi.org/10.1007/978-1-0716-2047-2_5
- Steger G, Rosenbach H, Span I (Eds)
DNAzymes
Methods in Molecular Biology 2439, (2022)
https://link.springer.com/book/10.1007/978-1-0716-2047-2
- Rosenbach H, Borggräfe J, Victor J, Wuebben C, Schiemann O, Hoyer W, Steger G, Etzkorn M, Span I
Influence of monovalent metal ions on metal binding and catalytic activity of the 10–23 DNAzyme
Biological Chemistry 402, 99-111 (2021)
https://doi.org/10.1515/hsz-2020-0207
- Patricia Rodríguez-Maciá, Lisa M. Galle, Ragnar Bjornsson, Christian Lorent, Ingo Zebger, Yoshitaka Yoda, Stephen P. Cramer, Serena DeBeer, Ingrid Span and James A. Birrell
Caught in the Hinact: Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O2-stable State of [FeFe] Hydrogenase
Angewandte Chemie International Edition 59, 2-11 (2020)
https://doi.org/10.1002/anie.202005208
https://onlinelibrary.wiley.com/doi/10.1002/anie.202005208
- Rosenbach H, Victor J, Borggräfe J, Biehl R, Steger G, Etzkorn M, Span I.
Expanding crystallization tools for nucleic acid complexes using U1A protein variants
Journal of Structural Biology 210, 107480 (2020)
https://doi.org/10.1016/j.jsb.2020.107480
- Rosenbach H, Victor J, Etzkorn M, Steger G, Riesner D, Span I
Molecular Features and Metal Ions that Influence 10-23 DNAzyme Activity
Molecules 25, 3100 (2020)
https://doi.org/10.3390/molecules25133100
Special Issue "Advances in Catalytic DNA"
- Galle L, Cutsail III G, Nischwitz V, DeBeer S, Span I
Spectroscopic characterization of the Co-substituted C-terminal domain of Rubredoxin-2
Biological Chemistry 399, 787-798 (2018)
https://doi.org/10.1515/hsz-2018-0142
https://www.degruyter.com/view/journals/bchm/399/7/article-p787.xml
- Pascual-Ortiz M, Saiardi A, Walla E, Jakopec V, Künzel NA, Span I, Vangala A, Fleig U
Asp1 Bifunctional Activity Modulates Spindle Function via Controlling Cellular Inositol Pyrophosphate Levels in Schizosaccharomyces pombe
Mol. Cell. Biol. 38, e00047-18 (2018)
http://dx.doi.org/10.1128/MCB.00047-18
http://mcb.asm.org/content/38/9/e00047-18.abstract
- E. N. Trana, J. M. Nocek, J. V. Woude, I. Span, S. M Smith, A. C. Rosenzweig, B. M. Hoffman
Charge-Disproportionation Symmetry Breaking Creates a Heterodimeric Myoglobin Complex with Enhanced Affinity and Rapid Intracomplex Electron Transfer
J. Am. Chem. Soc. 138, 12615–12628 (2016)
http://dx.doi.org/10.1021/jacs.6b07672
http://pubs.acs.org/doi/abs/10.1021/jacs.6b07672
- S. G. Kathman, I. Span, A. T. Smith, Z. Xu, J. Zhan, A. C. Rosenzweig, A. V. Statsyuk
A Small Molecule That Switches a Ubiquitin Ligase From a Processive to a Distributive Enzymatic Mechanism.
J. Am. Chem. Soc. 137, 12442-12445 (2015)
http://dx.doi.org/10.1021/jacs.5b06839
http://pubs.acs.org/doi/abs/10.1021/jacs.5b06839
- I. Span, K. Wang, W. Eisenreich, A. Bacher, Y. Zhang, E. Oldfield, M. Groll
Insights into the Binding of Pyridines to the Iron-Sulfur Enzyme IspH
J. Am. Chem. Soc. 136, 7926-7932 (2014)
http://dx.doi.org/10.1021/ja501127j
http://pubs.acs.org/doi/abs/10.1021/ja501127j
- Span I, Wang K, Eisenreich W, Bacher A, Zhang Y, Oldfield E, Groll M
Insights into the Binding of Pyridines to the Iron-Sulfur Enzyme IspH
J. Am. Chem. Soc. 136 (22), 7926-32 (2014)
- I. Span, K. Wang, W. Wang, J. Jauch, W. Eisenreich, A. Bacher, E. Oldfield, M. Groll
Structures of fluoro, amino, and thiol inhibitors bound to the [Fe4S4] protein IspH
Angew. Chem. Intl. Ed. 52, 2118–2121 (2013)
http://dx.doi.org/10.1002/anie.201208469
http://onlinelibrary.wiley.com/doi/10.1002/anie.201208469/abstract
- free radicals involved in IspH catalysis? An EPR and crystallographic investigation.W. Wang, K. Wang, I. Span, J. Jauch, A. Bacher, M. Groll, E. Oldfield
Are free radicals involved in IspH catalysis? An EPR and crystallographic investigation
J. Am. Chem. Soc. 134, 11225-11234 (2012)
http://dx.doi.org/10.1021/ja303445z
http://pubs.acs.org/doi/abs/10.1021/ja303445z
- I. Span, K. Wang, W. Wang, Y. Zhang, A. Bacher, W. Eisenreich, K. Li, C. Schulz, E. Oldfield, M. Groll
Discovery of acetylene hydratase activity of the iron-sulphur protein IspH
Nat. Commun. 3, 1042 (2012)
http://dx.doi.org/10.1038/ncomms2052
https://www.nature.com/articles/ncomms2052
- I. Span, T. Gräwert, A. Bacher, W. Eisenreich, M. Groll
Crystal Structures of Mutant IspH Proteins Reveal a Rotation of the Substrate’s Hydroxymethyl Group during Catalysis
J. Mol. Biol. 416, 1-9 (2012)
https://doi.org/10.1016/j.jmb.2011.11.033
http://www.sciencedirect.com/science/article/pii/S0022283611012745
- T. Gräwert*, I. Span*, W. Eisenreich, F. Rohdich, J. Eppinger, A. Bacher, M. Groll
Probing the reaction mechanism of IspH protein by x-ray structure analysis
Proc. Natl. Acad. Sci. U. S. A. 107, 1077-1081 (2010)
http://dx.doi.org/10.1073/pnas.0913045107
http://www.pnas.org/content/107/3/1077.abstract
- T. Gräwert, I. Span, A. Bacher, M. Groll
Reductive dehydroxylation of allyl alcohols by IspH protein
Angew. Chem. Intl. Ed. 48, 8802–8809 (2010)
http://dx.doi.org/10.1002/anie.201000833
http://onlinelibrary.wiley.com/doi/10.1002/anie.201000833/abstract
- T. Gräwert, F. Rohdich, I. Span, A. Bacher, W. Eisenreich, J. Eppinger, M. Groll
Structure of Active IspH Enzyme from Escherichia coli Provides Mechanistic Insights into Substrate Reduction
Angew. Chem. Intl. Ed. 48, 5756–5759 (2009)
http://dx.doi.org/10.1002/anie.200900548
http://onlinelibrary.wiley.com/doi/10.1002/anie.200900548/abstract
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