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ProteomicsPeptide artificial formylation in bottom–up proteomics analyses
The primary objective of this study was to explain excessive formylation rate of peptides that did not come in contact with concentrated formic acid.
ORGANISM(S): Francisella tularensis subsp. holarctica 
2020-06-10 | PXD016597 | Pride
Bottom–up proteomics Formic acid Peptide formylationartificial modifications  bottom–up proteomics  formic acid  peptide formylation Artificial modifications 
ProteomicsFormylation facilitates the reduction of oxidized initiator methionines
Within a cell, protein-bound methionines can be oxidized by reactive oxygen species (ROS) or monooxygenases, and subsequently reduced by methionine sulfoxide reductases (Msrs). Methionine oxidation can result in structural damage or be the basis of functional regulation of enzymes. In addition to pa...
ORGANISM(S): Escherichia coli 
2024-11-06 | PXD048776 | Pride
N-formylation  methionine sulfoxide reductase (msr)  proteomics  mass spectrometry (ms)  methionine oxidation 
ProteomicsEstablishing a MS-based assay for in vivo peptide deformylase inhibition in Bacillus subtilis
The peptide deformylase inhibitor actinonin was used to treat Bacillus subtilis 168, and the proteome was analyzed using UPLC-MSE. The goal was to identify proteins that retain N-terminal formylation of the initial methionine after actinonin treatment that could be used to establish a microplate ass...
ORGANISM(S): Bacillus subtilis subsp. subtilis str. 168 
2026-02-11 | PXD064376 | Pride
Peptide deformylase Antibiotics Proteomics N-formylation Bacillus subtilis 
UnknownFormylation facilitates the reduction of oxidized initiator methionines.
Not available
S-EPMC11572973 | biostudies-literature
ProteomicsSW480 N-terminal peptide analysis
N-terminal peptide analysis of SW480 cell line for Nt-formylation.
ORGANISM(S): Homo sapiens (Human) 
2023-07-20 | PXD039053 | Pride
Sw480 N-terminome Human Inrich 
UnknownSuppression of Formylation Provides an Alternative Approach to Vacant Codon Creation in Bacterial In Vitro Translation.
Not available
S-EPMC7756408 | biostudies-literature
UnknownMutations in three distinct loci cause resistance to peptide deformylase inhibitors in Bacillus subtilis.
Not available
S-EPMC2663100 | biostudies-literature
UnknownPeptide Deformylase (def) is essential in Mycobacterium smegmatis, but the essentiality is compensated by inactivation of methionine formylation.
Not available
S-EPMC6815462 | biostudies-literature
ProteomicsPeptide collision cross section of 22 post-translational modifications
The present study investigates the ion mobility characteristics of synthetic peptides carrying 22 different post-translational modifications by Ion Mobility-Mass Spectrometry. Samples were kindly provided by the ProteomeTools project.
ORGANISM(S): Homo sapiens (Human) 
2023-08-25 | PXD042416 | Pride
Tims Ptm Post-translational modifications Collision cross section Ccs Ion mobility 
ProteomicsProteome-wide analysis of the amino terminal status of Escherichia coli proteins at the steady-state
A proteome-wide analysis was performed in Escherichia coli to identify the impact on protein N-termini of the antibiotic actinonin specifically inhibiting peptide deformylase (PDF). A new strategy and tool suite (SILProNaQ) was employed to provide large scale N-terminus acetylation yield quantitatio...
ORGANISM(S): Escherichia coli 
2015-07-22 | PXD001983 | Pride
Formylation/post-translational modifications/actinonin/acetylation/antibiotics 
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