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Anna M Rydzik

Showing results (21-30 of 35) with videos related to

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Antimicrobial Agents and Chemotherapy|December 16, 2015
Comparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition ProfilesAnne Makena, Azer Ö Düzgün, Jürgen Brem, et al.
Antimicrobial Agents and Chemotherapy|July 13, 2016
Interaction of Avibactam with Class B Metallo-β-LactamasesMartine I Abboud, Christian Damblon, Jürgen Brem, et al.
Journal of Medicinal Chemistry|August 1, 2013
Assay platform for clinically relevant metallo-β-lactamasesSander S van Berkel, Jürgen Brem, Anna M Rydzik, et al.
Chemistry (Weinheim an Der Bergstrasse, Germany)|December 15, 2015
Cation-π Interactions Contribute to Substrate Recognition in γ-Butyrobetaine Hydroxylase CatalysisJos J A G Kamps, Amjad Khan, Hwanho Choi, et al.
Nature Communications|March 6, 2014
Non-enzymatic chemistry enables 2-hydroxyglutarate-mediated activation of 2-oxoglutarate oxygenasesHanna Tarhonskaya, Anna M Rydzik, Ivanhoe K H Leung, et al.
Nucleic Acids Research|July 2, 2017
mRNA cap analogues substituted in the tetraphosphate chain with CX2: identification of O-to-CCl2 as the first bridging modification that confers resistance to decapping without impairing translationAnna M Rydzik, Marcin Warminski, Pawel J Sikorski, et al.
Angewandte Chemie (International Ed. in English)|March 3, 2017
<sup>19</sup> F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-β-LactamaseMartine I Abboud, Philip Hinchliffe, Jürgen Brem, et al.
ACS Chemical Biology|July 8, 2011
Structure-guided design of cell wall biosynthesis inhibitors that overcome β-lactam resistance in Staphylococcus aureus (MRSA)Carlos Contreras-Martel, Ana Amoroso, Esther C Y Woon, et al.
Nature Chemistry|November 21, 2014
Rhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibitionJürgen Brem, Sander S van Berkel, WeiShen Aik, et al.
Chemical Science|February 27, 2015
Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification, <sup>19</sup>F-labelling, crystallisation, data collection, and structure determination, table of crystallographic data, table of crystallographic parameters and refinement statistics, figures showing binding mode and distances, procedures for mass spectrometry measurements, differential scanning fluorimetry measurements, stopped-flow measurements and other kinetics measurements. See DOI: 10.1039/c4sc01752hClick here for additional data fileJürgen Brem, Weston B Struwe, Anna M Rydzik, et al.
Pageof 4

Showing results (21-30 of 35) with videos related to

Sort By:
Pageof 4
Antimicrobial Agents and Chemotherapy|December 16, 2015
Comparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition ProfilesAnne Makena, Azer Ö Düzgün, Jürgen Brem, et al.
Antimicrobial Agents and Chemotherapy|July 13, 2016
Interaction of Avibactam with Class B Metallo-β-LactamasesMartine I Abboud, Christian Damblon, Jürgen Brem, et al.
Journal of Medicinal Chemistry|August 1, 2013
Assay platform for clinically relevant metallo-β-lactamasesSander S van Berkel, Jürgen Brem, Anna M Rydzik, et al.
Chemistry (Weinheim an Der Bergstrasse, Germany)|December 15, 2015
Cation-π Interactions Contribute to Substrate Recognition in γ-Butyrobetaine Hydroxylase CatalysisJos J A G Kamps, Amjad Khan, Hwanho Choi, et al.
Nature Communications|March 6, 2014
Non-enzymatic chemistry enables 2-hydroxyglutarate-mediated activation of 2-oxoglutarate oxygenasesHanna Tarhonskaya, Anna M Rydzik, Ivanhoe K H Leung, et al.
Nucleic Acids Research|July 2, 2017
mRNA cap analogues substituted in the tetraphosphate chain with CX2: identification of O-to-CCl2 as the first bridging modification that confers resistance to decapping without impairing translationAnna M Rydzik, Marcin Warminski, Pawel J Sikorski, et al.
Angewandte Chemie (International Ed. in English)|March 3, 2017
<sup>19</sup> F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-β-LactamaseMartine I Abboud, Philip Hinchliffe, Jürgen Brem, et al.
ACS Chemical Biology|July 8, 2011
Structure-guided design of cell wall biosynthesis inhibitors that overcome β-lactam resistance in Staphylococcus aureus (MRSA)Carlos Contreras-Martel, Ana Amoroso, Esther C Y Woon, et al.
Nature Chemistry|November 21, 2014
Rhodanine hydrolysis leads to potent thioenolate mediated metallo-β-lactamase inhibitionJürgen Brem, Sander S van Berkel, WeiShen Aik, et al.
Chemical Science|February 27, 2015
Studying the active-site loop movement of the São Paolo metallo-β-lactamase-1†Electronic supplementary information (ESI) available: Procedures for protein expression and purification, <sup>19</sup>F-labelling, crystallisation, data collection, and structure determination, table of crystallographic data, table of crystallographic parameters and refinement statistics, figures showing binding mode and distances, procedures for mass spectrometry measurements, differential scanning fluorimetry measurements, stopped-flow measurements and other kinetics measurements. See DOI: 10.1039/c4sc01752hClick here for additional data fileJürgen Brem, Weston B Struwe, Anna M Rydzik, et al.
Pageof 4