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Journal of Inorganic Biochemistry|July 8, 2008
Outsmarting metallo-beta-lactamases by mimicking their natural evolutionPeter OelschlaegerBiomolecules|January 26, 2024
Molecular Mechanisms and the Significance of Synonymous MutationsPeter OelschlaegerCurrents in Pharmacy Teaching & Learning|December 14, 2017
Change in self-assessed comfort level of first-year pharmacy students as an alternative approach to measure teaching effectiveness and learning outcomesPeter OelschlaegerBiomolecules|August 6, 2021
β-Lactamases: Sequence, Structure, Function, and InhibitionPeter OelschlaegerJournal of Molecular Biology|December 13, 2006
Hydroxyl groups in the betabeta sandwich of metallo-beta-lactamases favor enzyme activity: Tyr218 and Ser262 pull down the lidPeter Oelschlaeger, Juergen PleissJournal of Molecular Biology|June 11, 2005
Hydroxyl groups in the (beta)beta sandwich of metallo-beta-lactamases favor enzyme activity: a computational protein design studyPeter Oelschlaeger, Stephen L MayoProteins|October 21, 2009
A binding free energy decomposition approach for accurate calculations of the fidelity of DNA polymerasesRobert Rucker, Peter Oelschlaeger, Arieh WarshelAntimicrobial Agents and Chemotherapy|May 2, 2012
Systematic analysis of metallo-β-lactamases using an automated databaseMichael Widmann, Jürgen Pleiss, Peter OelschlaegerAntibiotics (Basel, Switzerland)|December 23, 2023
Strategies to Name Metallo-β-Lactamases and Number Their Amino Acid ResiduesPeter Oelschlaeger, Heba Kaadan, Rinku DhunganaBiochemistry|July 30, 2003
Modeling domino effects in enzymes: molecular basis of the substrate specificity of the bacterial metallo-beta-lactamases IMP-1 and IMP-6Peter Oelschlaeger, Rolf D Schmid, Juergen PleissPageof 5