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Posttranslational modifications of protein cysteine thiols play a significant role in redox regulation and the pathogenesis of human diseases. However, the cellular redox landscape in terms of quantitative, site-specific occupancies of thiol modifications at the proteome level, especially under phys...
ORGANISM(S): Mus musculus (Mouse) 
2020-08-13 | PXD019913 | Pride
Quantitative profiling of protein s-glutathionylation (SSG) reveals redox-dependent regulation of macrophage function during nanoparticle-induced oxidative stress
ORGANISM(S): Mus musculus (Mouse) 
2016-08-02 | PXD003356 | Pride
Extracellular Vesicle (EV) secretion has been observed from most types of normal and tumor cells. These EVs contain a variety of distinctive cargo where tumor-derived serum proteins in EVs secreted into the bloodstream can be used to provide a minimally invasive method for clinical monitoring. We ha...
ORGANISM(S): Homo Sapiens (human) 
Proteomic data from technical developments of a nanowell-mediated two-dimensional (2D) reversed-phase nanoflow liquid chromatography (LC) separation for in-depth proteome profiling of low-nanogram samples.
ORGANISM(S): Homo sapiens (Human) 
2018-10-18 | PXD010150 | Pride
Discovery proteomics on three R. toruloides strains with differing Pnt1 expression (WT IFO 0880, OE-Pnt1, and delta Pnt1) grown on either xylose or xylose and glycerol at mid-log phase.
ORGANISM(S): Rhodosporidium Toruloides Np11 (ncbitaxon:1130832) 
2022-07-21 | MSV000089938 | MassIVE
A 2D-LC-MS/MS strategy coupled with TMT-10 labeling was applied to mouse pancreatic beta cells (hetaTC-6) induced with ER stress by Thapsigargin to study the global proteome and protein cysteine PTM changes under ER stress. Samples were digested with trypsin, labeled with 10-plex TMT, then analyzed ...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2021-05-29 | MSV000087543 | MassIVE
Redox proteomic data from the heart of young mice, old mice, or mice treated with SS31. Quantification of protein-S-glutathionylation was performed using an established redox proteomics workflow. LC-MS/MS raw data were searched with MS-GF+ against the mouse protein sequence database from the Uniprot...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2020-04-23 | MSV000085329 | MassIVE
The S-glutathionylation and phosphorylation proteomes of mouse hearts were analyzed using shotgun proteomics methods in order to assess the effects of aging and the ability of mitochondrion-targeted drug SS-31 to reverse age-related changes. There was a nearly universal increase in S-gluthationylati...
ORGANISM(S): Mus Musculus 
2022-03-16 | PXD024247 | panorama
Global proteomic, redox proteomic, and phosphoproteomic data from mouse C10 epithelial cells and skeletal muscle tissue, no treatments used for method development experiments using these biological sytems. Global proteomic, redox proteomic, phosphoproteomic, and acetylomic data from mouse Beta-TC-6 ...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2024-07-06 | MSV000095264 | MassIVE
Development and evaluation of an autosampler for integrating nanoPOTS with LC-MS. Includes proteomic data from nanoPOTS-based sample preparation, including diluted peptides of Shewanella oneidensis MR-1, single cultured MCF10A cells, and single cells from three Acute Myeloid Leukemia (AML) cell line...
ORGANISM(S): Shewanella Oneidensis Mr-1 (ncbitaxon:211586) Homo Sapiens (ncbitaxon:9606) 
2020-04-05 | MSV000085230 | MassIVE
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