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ProteomicsPeroxynitrite-mediated post-translational modification of human glutamine synthetase
The aim of the project was to understand the mechanisms that underlie the oxidative inactivation of human glutamine synthetase (HsGS). For that purpose, we expressed and purified recombinant HsGS, exposed it in phosphate buffer to peroxynitrite (ONOO-) and assessed the functional and structural cons...
ORGANISM(S): Homo sapiens (Human) 
2023-05-10 | PXD037583 | Pride
Peroxynitrite Glutamine synthetase Oxidative stress Protein oxidation Nitrotyrosine 
UnknownOxidative Post-translational Modifications Accelerate Proteolytic Degradation of Calprotectin.
Not available
S-EPMC6534964 | biostudies-literature
ProteomicsReactive Metabolite-induced Protein Glutathionylation Mechanistically Accounts for Acetaminophen Hepatotoxicity
Although covalent protein binding is established as the pivotal event underpinning acetaminophen (APAP) toxicity, its mechanistic details remain unclear. In this study, we demonstrated that APAP induces widespread protein glutathionylation in a time-, dose- and bioactivation-dependent manner in Hepa...
ORGANISM(S): Homo Sapiens (human) 
2018-09-20 | PXD009986 | JPOST Repository
UnknownSirtuin Oxidative Post-translational Modifications.
Not available
S-EPMC8652059 | biostudies-literature
UnknownOxidative Post-translational Protein Modifications upon Ischemia/Reperfusion Injury.
Not available
S-EPMC10812827 | biostudies-literature
ProteomicsIdentification of sulfenylation patterns in Plasmodium falciparum using a non-dimedone based probe
Plasmodium falciparum causes the deadliest form of malaria. Adequate redox control is crucial for this protozoan parasite to overcome oxidative and nitrosative challenges, thus enabling its survival. Sulfenylation is an oxidative post-translational modification, which acts as a molecular on/off swit...
ORGANISM(S): Plasmodium Falciparum (ncbitaxon:5833) 
MSV000086125 | MassIVE
ProteomicsSpecific post-translational modifications of VDAC3 in ALS-SOD1 model cells identified by High-Resolution Mass Spectrometry
Damage induced by oxidative stress is a key driver of the selective motor neuron death in amyotrophic lateral sclerosis (ALS). Mitochondria are among the main producers of ROS, but they also suffer particularly from their harmful effects. Voltage-dependent anion-selective channels (VDACs) are the mo...
ORGANISM(S): Mus musculus (Mouse) 
2023-03-11 | PXD036728 | Pride
Deamidation  amyotrophic lateral sclerosis  voltage dependent anion channel  post-translational modifications  mitochondria  ros  mass spectrometry analysis  orbitrap fusion tribrid  neurodegeneration  sod1. 
UnknownOxidative Post-Translational Modifications of an Amyloidogenic Immunoglobulin Light Chain Protein.
Not available
S-EPMC5774984 | biostudies-literature
ProteomicsS.cerevisiae - Whole organism, SC (Silvaetal,natstructmolbiol,2015)
abundance based on Spectral counting, Interaction consistency score: 5.8, Coverage: 10
ORGANISM(S): 4932 
2015-00-00 | 743986671 | PAXDB
ProteomicsTop-down proteomics of membrane proteoforms from HeLa cells and mouse hippocampus
Comprehensive characterization of membrane proteins at the level of proteoforms in complex biological samples by top-down mass spectrometry is of vital importance in revealing their precise functions. Based on a novel membrane protein separation technology, we obtained a dataset of membrane proteofo...
ORGANISM(S): Homo Sapiens Mus Musculus 
2023-02-08 | PXD039949 |
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