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ProteomicsS-nitrosylation of p53 in A375 cells
Nitric oxide (NO) is a pleiotropic signaling molecule that affects numerous biological functions. One unique posttranslational modification of proteins by NO is termed S-nitrosylation (SNO), but the role in modulating key proteins’ function in melanoma has not been fully characterized. In the presen...
ORGANISM(S): Homo sapiens (Human) 
2025-07-21 | PXD031807 | Pride
A375 Mass spectrometry S-nitrosylation P53 Melanoma cells 
ProteomicsProteomic analysis of S-nitrosylation in HUVECs
HUVECs stimulated with HG+oxLDL or Mannitol+nLDL were subjected to the biotin-switch assay to enrich the S-nitrosylated proteins, the S-nitrosylated proteins were resolved by SDS-PAGE and gels were silver stained. Mass spectrometry was conducted to determine proteins with S-nitrosylation.
ORGANISM(S): Homo sapiens (Human) 
2021-06-03 | PXD025295 | Pride
S-nitrosylation Oxldl Mass spectrometry Huvecs Hg 
TranscriptomicsTranscription profiling of human bronchial epithelial cells stimulated with the commensal bacterium S. salivarius K12 of the pathogens S. aureus, P. aeruginosa, or S. enteritidis
Human bronchial epithelial cells (16HBE14O-) were stimulated with the commensal bacterium S. salivarius K12, or the pathogens S. aureus, P. aeruginosa, or S. enteritidis (subtype Typhimurium) for 1 hour.
ORGANISM(S): Homo sapiens 
2008-10-30 | E-FPMI-13 | biostudies-arrayexpress
ProteomicsIdentification of the S-sulfenylated residues of GSNOR1 in Arabidopsis
The major mechanism by which H2O2 executes its physiological functions is through oxidation of sulfur in the target proteins. Thiol groups of protein cysteine (Cys) could be oxidized by H2O2 to sulfenic, a process also known as S-sulfenylation. Therefore, we reasoned that the activity of GSNOR1 migh...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-01-23 | PXD056375 | Pride
H2o2  gsnor1  s-sulfenylation 
ProteomicsS-nitrosation of SCF E3 ligase components regulates hormonal signaling in Arabidopsis
E3 ubiquitin ligases mediate the last step of the ubiquitination pathwayin the ubiquitin-proteasome system (UPS). By targeting transcriptional regulators for their turnover, E3s play a crucial role in every aspect of plant biology. In plants, SKP1/CULLIN1/F-BOX PROTEIN (SCF)-type E3 ubiquitin ligase...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2022-04-04 | PXD030054 | Pride
S-nitrosation  hormonal signaling  arabidopsis 
ProteomicsS. pombe LC-MS G4-binding proteins_2
Affinity-purification study of G-quadruplex binding proteins from the S. pombe proteomics.
ORGANISM(S): Schizosaccharomyces pombe 927 
2021-09-09 | PXD020921 | Pride
Lc-ms G-quadruplex S. pombe 
ProteomicsThe garlic compound allicin causes strong disulfide stress and protein S-sulfoallylation as revealed by proteomics and transcriptomics in Staphylococcus aureus
Allicin from garlic is an antimicrobial substance that is effective against several ESKAPE pathogens, including methicillin-resistant Staphylococcus aureus (MRSA). However, the antimicrobial mode action of allicin has not been revealed in Gram-positive bacteria. Here, we have studied the changes in ...
ORGANISM(S): Staphylococcus aureus 
2022-02-28 | PXD010338 | Pride
Proteomics Allicin stress Transcriptomics Staphylococcus aureus S-sulfoallylation 
ProteomicsPhos-tag SDS-PAGE followed by LC-MS/MS analysis of in vitro phosphorylated Nab2, Foxk1, and HURP
Purified GST-fused Nab2, Foxk1, and HURP were incubated with ATP in the presence or absence of His-tagged active ERK in vitro, separated by Phos-tag SDS-PAGE, and visualized by CBB staining. The most shifted regions of protein bands on the Phos-tag-containing gels were excised, digested with trypsin...
ORGANISM(S): Mus Musculus (mouse) 
2022-03-03 | PXD028837 | JPOST Repository
UnknownSDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MS.
Not available
S-EPMC4598734 | biostudies-literature
ProteomicsDirect analysis of IFITM3 S-fatty-acylation, part 2
Given our laboratory interest in IFITM3 S-fatty-acylation and antiviral activity, we sought to directly characterize fatty acids that are covalently attached to the Cys residues of IFITM3. IFITM3 comprises two S-fatty-acylation sites (C71 and C72) in proximity of a intramembrane domain, and anothe...
ORGANISM(S): Homo sapiens (Human) 
2018-03-28 | PXD008401 | Pride
Ifitm3 S-fatty-acylation Site identification S-palmitoylation 
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