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ProteomicsSPROX full curve on E. coli lysate
To probe the thermodynamic stability of proteins within the E. coli proteome through proteomic technique SPROX.
ORGANISM(S): Escherichia coli 
2023-01-03 | PXD035834 | Pride
E. coli Sprox Stability 
ProteomicsLarge-Scale Analysis of Breast Cancer-Related Conformational Changes in Proteins using SILAC-SPROX
Proteomic methods for disease state characterization and biomarker discovery have traditionally utilized quantitative mass spectrometry methods to identify proteins with altered expression levels in disease states. Here we report on the large-scale use of protein folding stability measurements to ch...
ORGANISM(S): Homo sapiens (Human) 
2017-07-10 | PXD006703 | Pride
Mcf-7 Chemical denaturation Bt-474 Mda-mb-468 Protein folding 
ProteomicsDiscovery of Age-Related Protein Folding Stability Differences in the Mouse Brain Proteome
Described here is the application of thermodynamic stability measurements to study age-related differences in the protein folding and stability of proteins in a rodent model of ageing. Using the Stability of Proteins from Rates of Oxidation (SPROX) technique the thermodynamic stability profiles wer...
ORGANISM(S): Mus musculus (Mouse) 
2016-12-22 | PXD005184 | Pride
Mouse Ageing Sprox Itraq 
ProteomicsDIA-SPROX E.coli and S.cerevisiae Midpoints
The stability of proteins from rates of oxidation (SPROX) technique is a mass spectrometry-based approach for making protein folding stability measurements on the proteomics scale. The development and application of SPROX, to date, has involved the use of quantitative bottom-up proteomics and data d...
ORGANISM(S): Escherichia coli Saccharomyces cerevisiae (Baker's yeast) 
2026-03-03 | PXD066697 | Pride
ProteomicsDiscovery of Tamoxifen and N-Desmethyl Tamoxifen Protein Targets in MCF-7 Cells Using Large-Scale Protein Folding and Stability Measurements
The proteins in an MCF-7 cell line were probed for tamoxifen (TAM) and n-desmethyl tamoxifen (NDT) induced stability changes using the Stability of Proteins from Rates of Oxidation (SPROX) technique in combination with two different quantitative proteomics strategies. Together the SILAC- and iTRAQ-S...
ORGANISM(S): Homo sapiens (Human) 
2019-11-08 | PXD006732 | Pride
Silac Tamoxifen Sprox Mcf-7 N-desmethyl tamoxifen 
ProteomicsDiscovery of Tamoxifen and N-Desmethyl Tamoxifen Protein Targets in MCF-7 Cells Using Large-Scale Protein Folding and Stability Measurements, part 2
The proteins in an MCF-7 cell line were probed for tamoxifen (TAM) and n-desmethyl tamoxifen (NDT) induced stability changes using the Stability of Proteins from Rates of Oxidation (SPROX) technique in combination with two different quantitative proteomics strategies. Together the SILAC- and iTRAQ-S...
ORGANISM(S): Homo sapiens (Human) 
2019-11-08 | PXD006747 | Pride
Tamoxifen Sprox N-desmethyl tamoxifen 
ProteomicsMManassantin A iTRAQ-SPROX Drug Mode-of-Action
Manassantin A is a natural product that has been isolated from the perennial herb Saururus chinensis Baill and the aquatic plant Saururus cernuus. Manassantin A has been shown to possess potent hypoxia inducible factor 1 alpha (HIF-1α) inhibitory activity in a cell-based assay screen of thousands o...
ORGANISM(S): Homo sapiens (Human) 
2016-07-12 | PXD002304 | Pride
Drug mode-of-action Stability of proteins from rates of oxidation (sprox) Mda-mb-231 Protein-ligand binding interactions Manassantin a Itraq 
ProteomicsSmall molecules reveal differential shifts in stability and protein binding for G-quadruplex RNA
The potential of therapeutically targeting RNA with small molecules continues to grow yet progress is hindered by difficulties in determining specific mechanisms of action, including impacts on RNA-protein binding. RNA G-quadruplexes (rGQs) are a particularly promising target due to their range of b...
ORGANISM(S): Homo sapiens (Human) 
2026-06-23 | PXD060264 | Pride
Proteomics Rna Sprox 
UnknownTop-Down Stability of Proteins from Rates of Oxidation (TD-SPROX) Approach for Measuring Proteoform-Specific Folding Stability.
Not available
S-EPMC11809260 | biostudies-literature
UnknownLarge-Scale Analysis of Breast Cancer-Related Conformational Changes in Proteins Using SILAC-SPROX.
Not available
S-EPMC5605765 | biostudies-literature
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