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Mitochondria execute essential metabolic, biosynthetic, and signaling functions, yet the regulatory principles governing their proteome remain incompletely understood. Here, we develop a thermal proteome profiling (TPP) workflow applied directly to purified mitochondria, enabling systematic analy...

2025-12-08 | MTBLS7386 | MetaboLights
We developed a robust method termed Dali that identifies phosphorylation events that alter protein thermal stability as a proxy for function.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-06-18 | PXD016750 | Pride
Protein Thermal Stability Changes Induced by the Global Methylation Inhibitor 3-deazaneplanocin A (DZNep)
Protein methylation is emerging as an important modification beyond epigenetics. However, systems-wide analyses of protein methylation function lag behind compared to other modifications. Recently, thermal stability analyses have been developed which provide a proxy of a protein functional status. H...
ORGANISM(S): Mus musculus (Mouse) 
2023-04-27 | PXD038939 | Pride
The membrane proteins are essential targets to understand cellular function. The unbiased identification of membrane protein targets is still the bottleneck for a system- level understanding of cellular response to stimuli or perturbations. It has been suggested to enrich the soluble proteome with m...
ORGANISM(S): Rattus norvegicus (Rat) 
2023-03-20 | PXD037153 | Pride
Altered thermal solubility measurement techniques are emerging as powerful tools to assess ligand binding, post-translational modification, protein-protein interactions, and many other cellular processes that affect protein state under various cellular conditions. Thermal solubility or stability pro...
ORGANISM(S): Escherichia coli 
2024-02-14 | PXD031800 | Pride
We combined quantitative mass spectrometry with thermal profiling to systematically analyze the thermal stability and solubility of proteins during the eukaryotic cell cycle on a proteome-wide scale.
ORGANISM(S): Homo sapiens (Human) 
2018-05-02 | PXD008646 | Pride
Heat shock proteins are responsible for protein folding in cells. HSP90 is one of the most important chaperones in human cells, and inhibiting HSP90 is a potential strategy for cancer therapy. Multiple HSP90 inhibitors have been in clinical trials. However, none of them has been approved for disease...
ORGANISM(S): Homo sapiens (Human) 
2023-05-10 | PXD037575 | Pride
We have developed a mass spectrometry-based approach that allowed us to quantitatively monitor protein stability across a broad range of temperatures at the proteome scale (meltome). We profiled the meltomes of several microorganisms and eukaryotic species including human, allowing to investigate th...
ORGANISM(S): Danio rerio (Zebrafish) (Brachydanio rerio) Picrophilus torridus Oleispira antarctica Arabidopsis thaliana (Mouse-ear cress) Mus musculus (Mouse) Drosophila melanogaster (Fruit fly) Caenorhabditis elegans Geobacillus stearothermophilus Homo sapiens (Human) Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) Escherichia coli Saccharomyces cerevisiae (Baker's yeast) Bacillus subtilis 
2020-04-29 | PXD011929 | Pride
DZNep (3-deazaneplanocin A) is commonly used to reduce lysine methylation. DZNep inhibits S-adenosyl-L-homocysteine hydrolase (AHCY), preventing the conversion of S-adenosyl-L-homocysteine (SAH) into L-homocysteine and reducing the level of S-adenosylmethionine (SAM). As a result, the SAM to SAH rat...
ORGANISM(S): Homo sapiens 
2024-08-02 | GSE268629 | GEO
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