Slow, tight-binding inhibition of PDF by actinonin induces

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Ion mobility coupled to native mass spectrometry as a relevant tool to investigate extremely small ligand-induced conformational changes - Analyst (RSC Publishing) DOI:10.1039/C5AN01311A

PDF) Trapping Conformational States Along Ligand-Binding Dynamics of Peptide Deformylase: The Impact of Induced Fit on Enzyme Catalysis

Ion mobility coupled to native mass spectrometry as a relevant tool to investigate extremely small ligand-induced conformational changes - Analyst (RSC Publishing) DOI:10.1039/C5AN01311A

Peptide Deformylase as an Antibacterial Drug Target: Target Validation and Resistance Development

Isabelle ARTAUD, Research Director, PhD, French National Centre for Scientific Research, Paris, CNRS, Chemistry and Biology Interdisciplinar Centre paris Descartes University france

Trapping Conformational States Along Ligand-Binding Dynamics of Peptide Deformylase: The Impact of Induced Fit on Enzyme Catalysis

Isabelle ARTAUD, Research Director, PhD, French National Centre for Scientific Research, Paris, CNRS, Chemistry and Biology Interdisciplinar Centre paris Descartes University france

JCM, Free Full-Text

Frédéric Dardel's research works Paris Descartes University, Paris and other places

Aminopeptidase inhibitors bestatin and actinonin inhibit cell proliferation of myeloma cells predominantly by intracellular interactions - ScienceDirect

Actinonin and Analogs: Inhibitors of Bacterial Peptide Deformylase

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a) Tight-binding approximation is illustrated for κ = 0.0034, (b) WGM