Dr. Jon Uranga

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unigoe
 

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  • 2023 | Journal Article | 
    ​ ​Mechanisms of Cysteine‐Lysine Covalent Linkage ‐ The Role of Reactive Oxygen Species and Competition with Disulfide Bonds​
    Ye, J.; Bazzi, S.; Fritz, T.; Tittmann, K. ; Mata, R. A.   & Uranga, J. ​ (2023) 
    Angewandte Chemie. International Edition, art. e202304163​.​ DOI: https://doi.org/10.1002/anie.202304163 
    ​Details  DOI 
  • 2023 | Journal Article | 
    ​ ​Modulating Secondary Structure Motifs through Photo‐labile Peptide Staples​
    Lāce, I.; Bazzi, S.; Uranga, J. ; Schirmacher, A.; Diederichsen, U.; Mata, R. A. & Simeth, N. A.​ (2023) 
    ChemBioChem, art. e202300270​.​ DOI: https://doi.org/10.1002/cbic.202300270 
    ​Details  DOI  PMID  PMC 
  • 2023 | Journal Article | 
    ​ ​Dynamic Protonation States Underlie Carbene Formation in ThDP-Dependent Enzymes: A Theoretical Study​
    Uranga, J. ; Rabe von Pappenheim, F.; Tittmann, K. & Mata, R. A.​ (2023) 
    The Journal of Physical Chemistry. B, Condensed Matter, Materials, Surfaces, Interfaces & Biophysical, art. acs.jpcb.3c03137​.​ DOI: https://doi.org/10.1021/acs.jpcb.3c03137 
    ​Details  DOI 
  • 2023 | Journal Article | 
    ​ ​One‐ and Two‐ Electron Reductions in MiniSOG and their Implication in Catalysis​
    Azpitarte, O.; Zudaire, A.; Uranga, J. ; Lopez, X.; Salassa, L.; Formoso, E. & Rezabal, E.​ (2023) 
    ChemPhysChem, art. e202300091​.​ DOI: https://doi.org/10.1002/cphc.202300091 
    ​Details  DOI 
  • 2023 | Journal Article | 
    ​ ​The Catalytic Mechanism of Acetoacetate Decarboxylase: A Detailed Study of Schiff Base Formation, Protonation States, and Their Impact on Catalysis​
    Uranga, J.   & Mata, R. A.​ (2023) 
    Journal of Chemical Information and Modeling, 63(10) pp. 3118​-3127​.​ DOI: https://doi.org/10.1021/acs.jcim.3c00241 
    ​Details  DOI 
  • 2022 | Journal Article | 
    ​ ​Widespread occurrence of covalent lysine–cysteine redox switches in proteins​
    Rabe von Pappenheim, F.; Wensien, M.; Ye, J.; Uranga, J. ; Irisarri, I. ; de Vries, J.   & Funk, L.-M. et al.​ (2022) 
    Nature Chemical Biology, 18(4) pp. 368​-375​.​ DOI: https://doi.org/10.1038/s41589-021-00966-5 
    ​Details  DOI 
  • 2022 | Journal Article | 
    ​ ​Ground-state destabilization by electrostatic repulsion is not a driving force in orotidine-5′-monophosphate decarboxylase catalysis​
    Rindfleisch, S.; Krull, M.; Uranga, J. ; Schmidt, T.; Rabe von Pappenheim, F.; Kirck, L. L. & Balouri, A. et al.​ (2022) 
    Nature Catalysis, 5(4) pp. 332​-341​.​ DOI: https://doi.org/10.1038/s41929-022-00771-w 
    ​Details  DOI 
  • 2021 | Journal Article | 
    ​ ​A lysine–cysteine redox switch with an NOS bridge regulates enzyme function​
    Wensien, M.; Rabe von Pappenheim, F.; Funk, L.-M.; Kloskowski, P.; Curth, U.; Diederichsen, U.   & Uranga, J.  et al.​ (2021) 
    Nature, 593(7859) pp. 460​-464​.​ DOI: https://doi.org/10.1038/s41586-021-03513-3 
    ​Details  DOI 
  • 2021 | Journal Article | 
    ​ ​Theoretical Studies of the Acid–Base Equilibria in a Model Active Site of the Human 20S Proteasome​
    Uranga, J. ; Hasecke, L.; Proppe, J.; Fingerhut, J. & Mata, R. A.​ (2021) 
    Journal of Chemical Information and Modeling, 61(4) pp. 1942​-1953​.​ DOI: https://doi.org/10.1021/acs.jcim.0c01459 
    ​Details  DOI 
  • 2019 | Journal Article | 
    ​ ​Low-barrier hydrogen bonds in enzyme cooperativity​
    Dai, S.-B.; Funk, L. M. ; Rabe von Pappenheim, F.; Sautner, V.; Paulikat, M.; Schröder, B. & Uranga, J.  et al.​ (2019) 
    Nature, 573(7775) pp. 609​-613​.​ DOI: https://doi.org/10.1038/s41586-019-1581-9 
    ​Details  DOI  PMID  PMC 

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