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TranscriptomicsActinonin induced changes in gene expression profiles in MEFs
Retrograde signaling induced remodelling of nuclear gene expression from mitochondrial ribosomal dysfunction was analyzed. Global expression profile changes in mouse embryonic fibroblasts were assesed under actinonin treatment 6, 24, 48 and 72 hours post drug addiction. Control and four different ti...
ORGANISM(S): Mus musculus 
2013-07-05 | E-GEOD-44109 | biostudies-arrayexpress
TranscriptomicsActinonin induced changes in gene expression profiles in MEFs
Retrograde signaling induced remodelling of nuclear gene expression from mitochondrial ribosomal dysfunction was analyzed. Global expression profile changes in mouse embryonic fibroblasts were assesed under actinonin treatment 6, 24, 48 and 72 hours post drug addiction.
ORGANISM(S): Mus musculus 
2013-07-05 | GSE44109 | GEO
UnknownA single point mutation in the Plasmodium falciparum FtsH1 metalloprotease confers actinonin resistance.
Not available
S-EPMC7386903 | biostudies-literature
UnknownThe Inhibition and Resistance Mechanisms of Actinonin, Isolated from Marine Streptomyces sp. NHF165, against Vibrio anguillarum.
Not available
S-EPMC5020083 | biostudies-literature
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 
ProteomicsWhole lysate and ribosome enriched fractions analyses of the amino terminal status of Escherichia coli at the steady state and upon deformylation inhibition
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 
2015-07-21 | PXD001979 | Pride
Formylation/post-translational modifications/actinonin/acetylation/antibiotics 
UnknownDelineation of alternative conformational states in Escherichia coli peptide deformylase via thermodynamic studies for the binding of actinonin.
Not available
S-EPMC2644421 | biostudies-literature
UnknownStructural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.
Not available
S-EPMC4420530 | biostudies-literature
ProteomicsProteome-wide analysis of the amino terminal status of Escherichia coli proteins at the steady-state and upon deformylation inhibition
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 
2015-07-21 | PXD002012 | Pride
Antibiotics Post-translational modifications Acetylation Actinonin Formylation 
GenomicsMus musculus
Actinonin induced changes in gene expression profiles in MEFs
PRJNA188698 | ENA
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