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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
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 
2025-07-22 | PXD066371 |
ProteomicsSICyLIA-cTMT enables dissecting redox proteome dynamics with high accuracy and depth at micrograms scale (PART 5 = Human mammary breast cancer associated fibroblasts)
Cysteine oxidative modifications are fundamental signaling events that regulate cellular functions under both physiological and pathological conditions. However, our understanding of these modifications is limited by their low abundance and the technical challenges associated with studying their dyn...
ORGANISM(S): Homo sapiens (Human) 
2025-10-01 | PXD061855 | Pride
Redox proteomics  mass spectrometry  oxidative signaling  fibroblasts  cancer  obesity  redox stress. 
UnknownRegulation of hyperoxia-induced neonatal lung injury via post-translational cysteine redox modifications.
Not available
S-EPMC9307955 | biostudies-literature
UnknownNovel oxidative modifications in redox-active cysteine residues.
Not available
S-EPMC3047142 | biostudies-literature
ProteomicsRedox proteomics in NO-mediated protection on hypoxic cardiomyocyte
We developed a mass spectrometry (MS)-based quantitative approach using a set of novel iodoacetyl-based cysteine-reactive isobaric tags (iodoTMT) endowed with unique irreversible Cys-reactivities to differentially quantify the multiple redox-modified forms of a Cys site in the original cellular cont...
ORGANISM(S): Rattus norvegicus (Rat) 
2016-06-27 | PXD000274 | Pride
S-nitrosylation Mass spectrometry Hypoxia Redox cysteine modifications Redox-proteomics 
ProteomicsA quantitative tissue-specific landscape of protein redox regulation during aging
Mammalian tissues engage in specialized physiology that is regulated by post-translational protein modification. A major mode of protein regulation is initiated by reactive oxygen species (ROS) that reversibly modify protein cysteine residues. ROS regulate a myriad of biological processes and ROS ...
ORGANISM(S): Mus musculus (Mouse) 
2020-02-27 | PXD017050 | Pride
Cpt Redox Aging Cysteine proteomics 
UnknownHarnessing Redox Cross-Reactivity To Profile Distinct Cysteine Modifications.
Not available
S-EPMC4883004 | biostudies-literature
ProteomicsQuantitative analysis of redox proteome reveals protein thiol switches regulating fundamental processes in developmental hematopoiesis
Fetal and adult hematopoietic stem and progenitor cells (HSPCs) are characterized by distinct redox homeostasis that may influence their differential cellular behaviour in normal and malignant haematopoiesis. In this work, we have applied a quantitative mass spectrometry-based redox proteomic approa...
ORGANISM(S): Homo sapiens (Human) 
2022-06-09 | PXD033115 | Pride
Oxidative modifications Oxidative stress Redox proteomics Hydrogen peroxide Human embryonic stem cells 
ProteomicsRedox-proteomic analysis of pancreatic β-cells upon glucose stimulation
Redox signaling mediated by reversible oxidative cysteine thiol modifications is crucial for driving cellular adaptation to dynamic environmental changes, maintaining homeostasis, and ensuring proper function. This is particularly critical in pancreatic β-cells, which are highly metabolically active...
ORGANISM(S): Mus musculus (Mouse) Rattus norvegicus (Rat) 
2024-09-30 | PXD052765 | Pride
Iodotmt Redox proteomics 
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