Journal of Molecular Biology
On the release of the formyl group from nascent protein
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Quantification of IDP-73152, a novel antibiotic, in plasma from mice, rats and humans using an ultra-high performance liquid chromatography/tandem mass spectrometry method for use in pharmacokinetic studies
2017, Journal of Pharmaceutical and Biomedical AnalysisCitation Excerpt :Although the synthetic process between prokaryotic and eukaryotic cells is generally comparable, there are some notable differences, including the initiation step of the synthesis (e.g., the formylation of the peptide at the N-terminal methionine and subsequent deformylation), between the two cell systems [3,4]. Peptide deformylase (PDF), a metalloprotease, catalyzes the specific removal of the N-formyl moiety at the initiation of the peptide biosynthesis in prokaryotic cells [5–9]. Accordingly, an inhibitor of PDF could be biologically regarded as an antibiotic agent: Such an inhibitor is thought to exert bacteriocidal/bacteriostatic activities, with potential pro-inflammatory effects by activating phagocytes to release antimicrobial peptides [10].
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2016, Bioorganic and Medicinal Chemistry LettersSynthesis, antibacterial activity, and biological evaluation of formyl hydroxyamino derivatives as novel potent peptide deformylase inhibitors against drug-resistant bacteria
2014, European Journal of Medicinal ChemistryCo-translational mechanisms of protein maturation
2014, Current Opinion in Structural BiologyCitation Excerpt :This order of events establishes a multistep control process allowing SRP to faithfully select proteins destined for co-translational translocation and grants SRP privileged access to nascent chains right when they emerge at the tunnel exit. Interestingly, SRP and PDF do not bind competitively to ribosomes [13], which is in line with the virtually complete deformylation of the entire E. coli proteome including SRP substrates [78,79]. However, the footprints of SRP and PDF bound separately to the ribosome predict a steric clash upon simultaneous binding of both factors (Figure 2b).
Improved detection of variants in recombinant human interferon alpha-2a products by reverse-phase high-performance liquid chromatography on a core-shell stationary phase
2014, Journal of Pharmaceutical and Biomedical AnalysisPurification and use of E. coli peptide deformylase for peptide deprotection in chemoenzymatic peptide synthesis
2013, Protein Expression and Purification
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Present address: Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge, England.