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UnknownMitochondrial Methionyl-tRNA Formyltransferase Deficiency Alleviates Metaflammation by Modulating Mitochondrial Activity in Mice.
Not available
S-EPMC10051599 | biostudies-literature
UnknownConformational change of Escherichia coli initiator methionyl-tRNA(fMet) upon binding to methionyl-tRNA formyl transferase.
Not available
S-EPMC117066 | biostudies-literature
UnknownMethionyl-tRNA formyltransferase utilizes 10-formyldihydrofolate as an alternative substrate and impacts antifolate drug action.
Not available
S-EPMC10197868 | biostudies-literature
UnknownTranslation initiation in Saccharomyces cerevisiae mitochondria: functional interactions among mitochondrial ribosomal protein Rsm28p, initiation factor 2, methionyl-tRNA-formyltransferase and novel protein Rmd9p.
Not available
S-EPMC1840066 | biostudies-literature
UnknownPvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase.
Not available
S-EPMC6402982 | biostudies-literature
UnknownReducing the fitness cost of antibiotic resistance by amplification of initiator tRNA genes.
Not available
S-EPMC1459004 | biostudies-literature
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 
UnknownClinical and functional characterisation of the combined respiratory chain defect in two sisters due to autosomal recessive mutations in MTFMT.
Not available
S-EPMC4046648 | biostudies-literature
UnknownFormylation facilitates the reduction of oxidized initiator methionines.
Not available
S-EPMC11572973 | biostudies-literature
UnknownMitochondrial methionyl N-formylation affects steady-state levels of oxidative phosphorylation complexes and their organization into supercomplexes.
Not available
S-EPMC6166738 | biostudies-literature
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