Redox-proteomics

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Organisms

Homo sapiens (7)
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Paraphaeosphaeria sporulosa (1)
Entamoeba histolytica (1)
Bacillus subtilis subsp. subtilis str. 168 (1)

Repository

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Tissue

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Blood plasma (4)
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Skin (3)
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Disease

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Severe acute respiratory syndrome (1)
Lung adenocarcinoma (1)
Liver disease (1)
Lymphoma (1)
Cancer (1)
Melanoma (1)
Head and neck squamous cell carcinoma (1)
Pancreatic cancer (1)
Brain cancer (1)
Alzheimer's disease (1)

Technology Type

Mass Spectrometry (255)
Shotgun proteomics (154)
Bottom-up proteomics (61)
Data-dependent acquisition (29)
Gel-based experiment (15)
Affinity purification coupled with mass spectrometry proteomics (13)
SWATH MS (11)
Data-independent acquisition (10)
Mass spectrometry assay (4)
Mass spectrometry (4)
Top-down proteomics (4)
SRM/MRM (3)
Mass spectrometry imaging (2)
All-ion fragmentation (2)
MSE (1)
HDMSE (1)
Chemical cross-linking coupled with mass spectrometry proteomics (1)

Instrument Platform

Q Exactive Plus (8)
Orbitrap Exploris 480 (8)
Q Exactive (6)
Liquid Chromatography MS - positive - reverse phase (4)
Orbitrap Fusion Lumos (3)
Liquid Chromatography MS - negative - reverse phase (3)
Instrument (2)
Orbitrap Eclipse (2)
Q Exactive HF-X (2)
Liquid Chromatography MS - alternating - reverse-phase (2)
Bruker Daltonics HCT Ion Trap Mass Spectrometer (1)
2.Orbitrap Astral mass spectrometer coupled with a Vanquish Neo UHPLC system (Thermo Fisher Scientific) (1)
3. Tandem EASY-nanoLC1200 with Orbitrap Fusion Lumos (Thermo Fisher Scientific, MA, USA) (1)
1. Orbitrap melting fluorescence coupled to an EASY nanoLC 1200 system (Thermo Fisher Scientific, MA, USA) (1)
6545 Q-TOF LC/MS (1)
Orbitrap Astral (1)
LTQ Orbitrap Velos (1)
TripleTOF 5600+ (1)
TripleTOF 6600 (1)
Q Exactive HF (1)
LTQ Orbitrap (1)
Flow injection analysis MS - negative (1)
Gas Chromatography MS - positive (1)
Liquid Chromatography MS - alternating - hilic (1)
Liquid Chromatography MS - positive - reverse-phase (1)
Liquid Chromatography MS - negative - reverse-phase (1)
Liquid Chromatography MS - negative - hilic (1)
LTQ - Orbitrap (1)
LTQ-Orbitrap (1)

UNIPROT ID/AC

F2DUU5_HORVV (2)
A0A287VXN7_HORVV (2)
F2CZB1_HORVV (2)
A0A287L8X1_HORVV (2)
A0A287RU36_HORVV (2)
M0X291_HORVV (2)
M0UV11_HORVV (2)
F2DI89_HORVV (2)
A0A287WTB9_HORVV (2)
A0A287I0P8_HORVV (2)
F2CPS3_HORVV (2)
F2EBF8_HORVV (2)
F2EBF9_HORVV (2)
A0A287KM38_HORVV (2)
A0A287PVL8_HORVV (2)
F2CRN3_HORVV (2)
M0VNW9_HORVV (2)
M0Z8T3_HORVV (2)
M0YDP9_HORVV (2)
A0A287U1Y5_HORVV (2)
A0A287LMZ8_HORVV (2)
M0ZA68_HORVV (2)
A0A287IYY7_HORVV (2)
A0A287UX48_HORVV (2)
A0A287XTR7_HORVV (2)
M0WUX2_HORVV (2)
A0A287TQ75_HORVV (2)
M0X2W4_HORVV (2)
M0YD59_HORVV (2)
A0A287XV90_HORVV (2)

CHEBI ID

CHEBI:16113 (2)
CHEBI:15611 (2)
CHEBI:25094 (2)
CHEBI:18186 (2)
CHEBI:16708 (2)
CHEBI:16737 (2)
CHEBI:27897 (2)
CHEBI:30769 (2)
CHEBI:77153 (1)
CHEBI:201559 (1)
CHEBI:131174 (1)
CHEBI:18082 (1)
CHEBI:59579 (1)
CHEBI:37415 (1)
CHEBI:184001 (1)
CHEBI:34974 (1)
CHEBI:88778 (1)
CHEBI:181990 (1)
CHEBI:33064 (1)
CHEBI:218365 (1)
CHEBI:4745 (1)
CHEBI:61793 (1)
CHEBI:135632 (1)
CHEBI:92721 (1)
CHEBI:182736 (1)
CHEBI:38473 (1)
CHEBI:131999 (1)
CHEBI:59440 (1)
CHEBI:181150 (1)
CHEBI:203345 (1)

Metabolite Name

(S)-Hexahydropyrrolo[1,2-a]pyrazine-1,4-dione (2)
Diisopropylamine (2)
1,10-Phenanthroline (2)
Ethyl isopropyl sulfide (2)
Methacrylamide (2)
(5Z,9Z,12Z)-octadeca-5,9,12-trienoic acid (2)
2-Hexenyl acetate (2)
1H-Imidazole-1-acetic acid (2)
N-Acetyl-Leu (2)
(2R,3R)-2-Aminooctadecane-1,3-diol (2)
Pyroglutamylproline (2)
Phenyl-Alanine (2)
D-Tyrosine (2)
1-Palmitoylphosphatidylcholine (2)
Rhodamine B (2)
2-Methylimidazole (2)
9-Arabinofuranosyladenine (2)
DL-Proline (2)
9,12-Octadecadiynoic acid (2)
Indoline (2)
2,4-Dimethylquinoline (2)
1-Cyclohexyl-4-(1,2-diphenylethyl)piperazine (2)
Baikiain (2)
Cis-Vitamin K1 (2)
9-beta-d-Arabinofuranosylguanine (2)
Di-N-propylamine (2)
Dieporeticanin (2)
Choline sulfate (2)
Octadeca-9,11-dienoic acid (2)
Furanone A (2)

First Public Date

2026 (6)
2025 (3)
2023 (3)
2024 (1)
2022 (1)
2021 (1)
2020 (1)
2019 (1)
2016 (1)
2014 (1)
2013 (1)

Classification

protozoa (1)
bacteria (1)

Modification

15.994915 (2)
227.126991 (1)
9.030194 (1)
89.011293 (1)
37.006603 (1)
-2.01565 (1)
396.083866 (1)
119.004099 (1)
765.099559 (1)
56.026215 (1)
59.036279 (1)
31.989829 (1)
6-dioxaoctanediamine derivatized cysteine (1)
2x(15)N labeled L-lysine (1)
57.021464 (1)

Release Date

2025 (61)
2021 (54)
2023 (52)
2022 (43)
2020 (42)
2019 (35)
2018 (25)
2016 (25)
2015 (24)
2024 (22)
2014 (19)
2017 (15)
2013 (12)
2026 (9)
2011 (8)
2012 (6)
2010 (6)
2009 (6)
2008 (2)
2007 (2)
2006 (1)
2004 (1)

Lab affiliation

University of Vienna, Faculty of Chemistry, Department of Analytical Chemistry (23)
CRUK Scotland Institute for Cancer Research - Switchback Rd, Bearsden, Glasgow G61 1BD - United Kingdom (6)
Department of Inflammation and Immunity, Gastroenterology and Hepatology. Cleveland Clinic, Cleveland Ohio, USA (6)
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599 USA (5)
Pacific Northwest National Laboratory, USA (3)
Li2D (3)
University of Colorado Skaggs School of Pharmacy (2)
Department of Clinical Science, University of Bergen, Norway (2)
Dalhousie University (2)
Department of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC, United States (2)
Center for Functional Protein Assemblies (CPA), Department of Bioscience, TUM School of Natural Sciences, Technical University of Munich (TUM), Ernst-Otto-Fischer-Stra?e 8, 85748 Garching, Germany (2)
Biological Chemistry Department, David Geffen School of Medicine, UCLA (2)
Research Unit for Molecular Medicine, Department of Clinical Medicine, Aarhus University and Aarhus University Hospital, Aarhus, Denmark (2)
Center for Neuroscience and Cell Biology – University of Coimbra (2)
Lund Stem Cell Center, Division of Molecular Hematology, Lund University, Lund, Sweden (2)
CEA-Marcoule, ProGénoMIX platform, DRF-Li2D, 30207 Bagnols-sur-Cèze, France (2)
John Innes Centre Dept. Molecular Microbiology Head of Department Norwich UK (1)
BBSRC Discovery Fellow & BMC Microbiome Managing Editor Arthur Willis Environmental Research Centre University of Sheffield Sheffield S10 1AE (1)
CSIRO Agriculture, Western Australia (1)
Head of Discovery Proteomics Facility, Oxford (1)
Max Planck Institute of Biochemistry Department of Proteomics and Signal Transduction Munich, Germany (1)
Beijing Institute of Genomics, Chinese Academy of Sciences (1)
University of Nebraska, Lincoln (1)
College of Food Science and Technology, Nanjing Agricultural University, Nanjing, China (1)
ADLQ (1)
State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan 430070, China (1)
University Hospital Bern (1)
Professor University Research Chair in Integrative Mitochondrial Biology Interdisciplinary School of Health Sciences, Faculty of Health Sciences University of Ottawa RGN building, 451 Smyth Road, Ottawa, ON K1H 8M5 Canada (1)
Department of Chemistry,Department of Life Sciences,National Cheng Kung University, Tainan, Taiwan (1)
Department of Chemisry & Biochemistry at Montanan State University, Bozeman, MT (1)

Publication date

2022 (57)
2026 (56)
2025 (44)
2024 (33)
2021 (33)
2020 (30)
2023 (25)
2018 (16)
2017 (15)
2019 (14)
2016 (11)
2011 (7)
2015 (6)
2014 (4)

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Redox proteomics reveal a role for peroxiredoxinylation in stress protection.

The redox state of proteins is essential for their function and guarantees cell fitness. Peroxiredoxins protect cells against oxidative stress, maintain redox homeostasis, act as chaperones, and transmit hydrogen peroxide signals to redox regulators. Despite the profound structural and functional...

2025-07-17 | MTBLS11979 | MetaboLights

Comprehensive chemical proteomics for target deconvolution of the redox active drug auranofin

Chemical proteomics encompasses novel drug target deconvolution methods in which compound modification is not required. Herein we use Thermal Proteome Profiling, Functional Identification of Target by Expression Proteomics and multiplexed redox proteomics for deconvolution of auranofin targets to ai...

ORGANISM(S): Homo sapiens (Human)

2020-03-19 | PXD016776 | Pride

Anticancer effect of deuterium depleted water - comprehensive proteomics analysis suggests a redox disbalance mechanism

The proteomics data is derived from 4 parts of samples prepared and analysed by nanoLC-MS/MS. In order to make appropriate statistical analysed could be performed, all treatments were performed in biological replicates. The number of replicates was 4 for protein abundances analysis (part 1), 2 for t...

ORGANISM(S): Homo sapiens (Human)

2019-09-26 | PXD011085 | Pride

Anticancer Proteomics Redox disbalance Deuterium depleted water

Redox Proteomics Analysis of Auranofin Exposed Ovarian Cancer Cells

The effects of Auranofin (AF) on protein expression and protein oxidation in A2780 cancer cells were explored through a robust investigative strategy based on joint expression proteomics and redox proteomics determinations. Bioinformatics analysis of the proteomics data supports the view that the mo...

ORGANISM(S): Homo sapiens (Human)

2022-05-19 | PXD028681 | Pride

Cysteine Auranofin Gold Ovarian cancer Redox proteomics

Redox proteomics analysis of Arabidopsis wild type and grxs12 mutants

For an overall evaluation of the protein redox status in grxs12 leaves, the iodoTMT-based redox proteomics approach was employed. After protein extraction, the free thiols in Cys were NEM-blocked, and then the Cys thiols with reversible oxidations such as sulfenic acids (-SOH), S-glutathionylation (...

ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress)

2026-01-16 | PXD059068 | Pride

Arabidopsis Redox proteomics Grxs12 mutants Iodotmt label

Thiol redox proteomics: Characterization of thiol-based post-translational modifications.

Not available

S-EPMC10764013 | biostudies-literature

Redox proteomics DIALRP to study MND response in DU145 cells

In this study, we developed a label-free redox proteomics method using data-independent acquisition mass spectrometry (DIA-MS), termed DIALRP, to comprehensively analyze cysteine oxidative modifications in the prostate cancer cell line DU145 under oxidative stress induced by menadione (MND).

ORGANISM(S): Homo Sapiens (human)

2025-07-31 | PXD057921 | JPOST Repository

Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.

Not available

S-EPMC8004825 | biostudies-literature

Characterization of Entamoeba histolytica adapted to auranofin by combined transcriptomics and redox proteomics

PRJNA739471 | ENA

S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics

Protein S-thiolation is a post-translational thiol-modification that controls redox-sensing transcription factors and protects active site cysteine residues against irreversible oxidation. In Bacillus subtilis the MarR-type repressor OhrR was shown to sense organic hydroperoxides via formation of mi...

ORGANISM(S): Bacillus subtilis subsp. subtilis str. 168

2011-07-04 | GSE27637 | GEO

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