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MetabolomicsFatty acid oxidation protects cancer cells from apoptosis through increasing mitochondrial membrane lipids

Overcoming resistance to chemotherapies remains a major unmet need for cancers such as triple negative breast cancer (TNBC). Therefore, mechanistic studies to provide insight for drug development are urgently needed to overcome TNBC therapy resistance. Recently, an important role of fatty acid β-...

2022-05-31 | MTBLS4709 | MetaboLights
ProteomicsAccurate proteome-wide measurement of methionine oxidation in aging mouse brains
The oxidation of methionine side chains has emerged as an important posttranslational modification of proteins. A diverse array of low-throughput and targeted studies have suggested that the oxidation of methionine residues in select proteins can have diverse impacts on cell physiology, ranging from...
ORGANISM(S): Mus musculus (Mouse) 
2022-05-23 | PXD031238 | Pride
Methionine oxidation Brain Mouse Aging 
ProteomicsProtein folding stabilities are a major determinant of oxidation rates for buried methionine residues
The oxidation of protein-bound methionines to form methionine sulfoxides has a broad range of biological ramifications and it is therefore important to delineate factors that influence methionine oxidation rates within a protein. Previously, neighboring residue effects and solvent accessibility (SA)...
ORGANISM(S): Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) Escherichia coli 
2022-04-22 | PXD030245 | Pride
Protein stability Methionine Lumos Quantitative proteomics Oxidation-reduction 
OtherProtein methionine sulfoxide dynamics in Arabidopsis thaliana under oxidative stress.
Data from ProteomeXchange, PXD ID: PXD001286. Experiment: TP3_MetCofr, file: folder summary. Published as part of Mol Cell Proteomics. 2015 Feb 18 . From the Abstract: {{i}} ... Methionine oxidation, studied here, is a reversible posttranslational modification, which is emerging as a mechanism by w...
ORGANISM(S): Ath1 
GPM32320014280 | GPMDB
Resource Reanalysis 
ProteomicsQuantitative analysis of in vivo methionine oxidation of the human proteome
A novel stable isotope labelling strategy was developed to quantify methionine oxidation in an unstressed human proteome. Cell extracts were oxidized with 18O labelled hydrogen peroxide following cell lysis in order to convert all unoxidized methionine residues to an oxidized version with a heavy l...
ORGANISM(S): Homo sapiens (Human) 
2019-12-09 | PXD014629 | Pride
Methionine oxidation Unstressed proteome Human cell line 
ProteomicsMethionine Alkylation as an Approach to Quantify Methionine Oxidation Using Mass Spectrometry
Post-translational oxidation of methionine residues can destabilize proteins or modify their functions. Although levels of methionine oxidation can provide important information regarding the structural integrity and regulation of proteins, their quantitation is often challenging as analytical proce...
ORGANISM(S): Escherichia coli 
2024-02-08 | PXD045497 | Pride
Methionine oxidation  methionine alkylation  proteomics Mass spectrometry (ms) 
ProteomicsThe dynamics of protein-bound methionine oxidation events in Arabidopsis thaliana during oxidative stress
Reactive oxygen species such as hydrogen peroxide can modify proteins via direct oxidation of their sulfur-containing amino acids, cysteine and methionine. Methionine oxidation, studied here, is a reversible posttranslational modification, which is increasingly suggested as a mechanism by which prot...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2015-03-24 | PXD001286 | Pride
Methionine oxidation Catalase mutant Oxidative stress Arabidopsis thaliana 
ProteomicsGlobal analysis of methionine oxidation provides a census of folding stabilities for the human proteome
Most natural proteins fold into a native conformation stabilized by non-covalent interactions. The energy difference between native and denatured states (Gfolding) is highly variable between proteins and can range from less than -10 kcal per mole for highly stable proteins to positive values for int...
ORGANISM(S): Homo sapiens (Human) 
2018-11-21 | PXD011456 | Pride
Human Protein stability Methionine oxidation Lumos Quantitative proteomics Protein folding 
ProteomicsQuantitative mapping of methionine sensitivity to oxidation in the two-copper chaperone PcuC from Cereibacter sphaeroides
Copper is typically coordinated by histidine, cysteine, or methionine residues in enzyme or chaperones and these residues are particularly sensitive to oxidation. However, it remains unclear whether copper-coordinating residues exhibit different sensitivity to oxidation compared to their non-coordin...
ORGANISM(S): Cereibacter sphaeroides Bacteria 
2026-02-09 | PXD062219 | Pride
Methionine oxidation Cofactor biosynthesis Periplasm Copper chaperone Oxaziridine 
ProteomicsQuantitative analysis of in vivo methionine oxidation of the human proteome
A novel stable isotope labelling stategy was developed to quantify methionine oxidation in an unstressed human proteome. Cell extracts were oxidized with 18O labelled hydrogen peroxide following cell lysis in order to convert all unoxidized methionine residues to an oxidized version with a heavy la...
ORGANISM(S): Homo sapiens (Human) 
2019-07-26 | PXD014770 | Pride
Methionine oxidation Unstressed proteome Human cell line 
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