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ProteomicsGlobal redox proteome and phosphoproteome analysis reveals novel mode of Akt regulation
A major knowledge gap in cell signalling is defining the crosstalk between multiple types of post-translational modification (PTM). Here, we take a multi-omic approach (redox proteome, phosphoproteome and total proteome) to delineate signalling networks in adipocytes modulated by reactive oxygen spe...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2019-12-10 | PXD011525 | Pride
Phosphoproteome Akt Crosstalk Redox proteome 
ProteomicsCharacterization of the redox proteome of Drosophila melanogaster S2 cells and w1118 fly eyes.
Reactive oxygen species (ROS) serve as intracellular signaling molecules; however, in excess ROS molecules are damaging to biomacromolecules such as DNA, lipids, and proteins. The excess accumulation of ROS leads to oxidative stress, disrupting redox homeostasis in the cell and has been linked with ...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2023-04-27 | PXD034050 | Pride
Drosophila melanogaster schneider s2 cells Drosophila eye Redox proteome Blue light 
ProteomicsCharacterization of the redox proteome in Drosophila melanogaster aging eyes.
During oxidative stress, reactive oxygen species (ROS) can modify and damage cellular proteins. In particular, the thiol groups of cysteine residues can undergo reversible or irreversible oxidative post-translation modifications (PTMs). Identifying the redox-sensitive cysteines on a proteome-wide sc...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2023-04-27 | PXD036110 | Pride
Drosophila eye Oxidative post-translation modifications Redox proteome Aging 
UnknownProteome-wide quantitative analysis of redox cysteine availability in the Drosophila melanogaster eye reveals oxidation of phototransduction machinery during blue light exposure and age.
Not available
S-EPMC10189289 | biostudies-literature
ProteomicsMechano-redox control of Mac-1 de-adhesion from ICAM-1 by protein disulfide isomerase promotes directional movement under flow
Quantification of the redox state of disulfide bonds in the beta 2 subunit of human recombinant Mac-1 integrin.
ORGANISM(S): Homo sapiens (Human) 
2023-04-09 | PXD032688 | Pride
Mac-1 Disulfide bonds Redox state 
UnknownRedox proteome analysis of auranofin exposed ovarian cancer cells (A2780).
Not available
S-EPMC8966199 | 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 
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. 
ProteomicsRedox Proteome of Skeletal Muscle
Adult and aged mouse gastrocnemius muscle analysed by redox shotgun proteomics, applying a label free quantitative proteomic approach that includes a differential Cysteine labelling step allowing simultaneous identification of up and down regulated proteins between samples and also the identificatio...
ORGANISM(S): Mus musculus (Mouse) 
2014-09-04 | PXD001054 | Pride
Redox Skeletal muscle 
UnknownQuantitative analysis of redox-sensitive proteome with DIGE and ICAT.
Not available
S-EPMC2577071 | biostudies-literature
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