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
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