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MetabolomicsDietary restriction of cysteine and methionine sensitizes gliomas to ferroptosis and induces alterations in energetic metabolism

Ferroptosis is mediated by lipid peroxidation of phospholipids containing polyunsaturated fatty acyl moieties. Glutathione, the key cellular antioxidant capable of inhibiting lipid peroxidation via the activity of the enzyme glutathione peroxidase 4 (GPX-4), is generated directly from the sulfur-...

2023-01-11 | MTBLS5959 | MetaboLights
ProteomicsKetone Bodies-mediated Cysteine Modifications Discovered by Chemical Proteomics
All the studies of ketone body-dependent post-translational modifications (PTMs), notably those mediated by ketone bodies, β-hydroxybutyrate (Bhb) and acetoacetate (Acac), have focused on lysine acylations. However, given the chemically diverse and reactive nature of metabolites generated, it remain...
ORGANISM(S): Homo Sapiens 
PXD066371 |
ProteomicsChemoselective umpolung of thiols to episulfoniums for cysteine bioconjugation
Modification of native cysteine is an important tool in protein research and relies on fast and chemoselective reactions under bioambient conditions. Nucleophilic cysteine can be functionalized with electrophiles, such as maleimides, that carry specific chemical groups, depending on the desired appl...
ORGANISM(S): Escherichia Coli 
2023-12-20 | PXD038723 | JPOST Repository
ProteomicsE2/E3-independent ubiquitin-like protein conjugation by Urm1 is directly coupled to cysteine persulfidation
Posttranslational modifications by ubiquitin-like proteins (UBL) are essential for nearly all cellular processes. Ubiquitin related modifier 1 (Urm1) is a non-canonical UBL which plays a key role in tRNA anticodon thiolation as a sulfur carrier protein (SCP). While Urm1 has also been observed to con...
ORGANISM(S): Chaetomium Thermophilum (ncbitaxon:209285) Saccharomyces Cerevisiae (ncbitaxon:4932) Homo Sapiens (ncbitaxon:9606) 
2021-11-16 | MSV000088390 | MassIVE
MetabolomicsMaternal gut microbiome, pregnancy exposure to environmental contaminants, and child health outcomes: A pilot study exploring potential effect modifications by diet
Not available
ORGANISM(S): Homo sapiens 
ST001040 | MetabolomicsWorkbench
ProteomicsRegulation of hyperoxia-induced neonatal lung injury via posttranslational cysteine redox modifications
Lung tissue from normoxia- or hyperoxia-treated control or SCNN1B overexpression mice were processed with a redox proteomics workflow and analyzed by LC-MS/MS with TMT based quantification. Data was searched with MS-GF+ using PNNL's DMS Processing pipeline.
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2022-08-18 | MSV000090157 | MassIVE
ProteomicsOverexpression of catalase delays age-related cardiac disease by preventing oxidative cysteine modifications
Reactive protein cysteine thiolates are instrumental in redox regulation. Aging associated to oxidative stress, can impair redox signaling by damaging essential cysteine thiolates. Our initial study found that cardiac-specific overexpression of catalase, can protect from oxidative stress and delay c...
ORGANISM(S): Mus musculus (Mouse) 
2018-10-24 | PXD002479 | Pride
Metabolism Proteomics Reversible cysteine thiol oxidation Tmt Post-translational protein modifications Mass spectrometry Cardiac aging and disease 
ProteomicsNAIA for cysteine profiling in HepG2 cells, protein target identification of covalent ligand and studying cysteine oxidative modifications
New cysteine probes, N-acryloylindole-alkynes (NAIAs), have been developed. We have applied NAIA-5 for cysteine profiling in HepG2 cell lysates, and the results have been compared to the conventional cysteine probe iodoacetamide-alkyne (IAA). NAIA-5 allows identification of more ligandable Cys than ...
ORGANISM(S): Homo sapiens (Human) 
2023-06-14 | PXD041264 | Pride
Profiling ligandable cysteines and studying cysteine oxidative modifications in human liver cancer cells hepg2 by naia-5 using bruker timstof ms 
ProteomicsGlobal profiling of phosphorylation-dependent changes in cysteine reactivity
Proteomics has revealed that the ~20,000 human genes engender a far greater number of proteins, or proteoforms, that are diversified in large part by post-translational modifications (PTMs). How such PTMs affect protein structure and function is an active area of research but remains technically cha...
ORGANISM(S): Homo sapiens (Human) 
2022-03-03 | PXD026730 | Pride
Cysteine Activity-based protein profiling Tmt-abpp Mitosis Chemical proteomics Phosphorylation 
UnknownCysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system.
Not available
S-EPMC4340704 | biostudies-literature
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