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MetabolomicsDietary restriction of cysteine and methionine sensitizes gliomas to ferroptosis and induces alterations in energetic metabolism

Ferroptosis is mediated by lipid peroxidation of phospholipids containing polyunsaturated fatty acyl moieties. Glutathione, the key cellular antioxidant capable of inhibiting lipid peroxidation via the activity of the enzyme glutathione peroxidase 4 (GPX-4), is generated directly from the sulfur-...

2023-01-11 | MTBLS5959 | MetaboLights
TranscriptomicsMutation of the cysteine residues that coordinate the WhiB [4Fe-4S] cluster prevents in vivo DNA binding by both WhiB and WhiA
The purpose of this experiment was to show that the iron-sulphur cluster ([4Fe-4S]) of whiB is essential for the DNA binding by WhiB and WhiA. The \\"serine version of whiB\\" mentioned below is a whiB in which the 4 cysteine residues which coordinate the [4Fe-4S] cluster were mutated to serines. Ch...
ORGANISM(S): Streptomyces venezuelae 
2021-08-16 | E-MTAB-10818 | biostudies-arrayexpress
ProteomicsMSP-MS of Cathepsin L and Cathepsin V pH 5.5
MSP-MS of Cathepsin L and Cathepsin V pH 5.5 at 37C
ORGANISM(S): Synthetic Construct (ncbitaxon:32630) 
MSV000088091 | MassIVE
ProteomicsDruggable Serine Proteases of Leishmania by Activity‐Based Protein Profiling
Leishmaniasis are a group of diseases caused by parasitic protozoa of the genus Leishmania. Current treatments are limited by difficult administration, high cost, poor efficacy, toxicity, and growing resistance. New agents, with new mechanisms of action, are urgently needed to treat the disease. Alt...
ORGANISM(S): Leishmania mexicana 
2022-07-04 | PXD033616 | Pride
Activity-based protein profiling Leishmania Serine protease 
ProteomicsMSP-MS of PC1 and PC2 pH 5.5 at 37C
MSP-MS of PC1 and PC2 pH 5.5 at 37C. Part of Neuropeptide processing study
ORGANISM(S): Synthetic Construct (ncbitaxon:32630) 
MSV000088092 | MassIVE
ProteomicsFunctional Proteomic Profiling of Secreted Serine Proteases in Health and Inflammatory Bowel Disease
Dysregulated proteolysis plays a pivotal role in the pathophysiology of inflammatory bowel disease. Nonetheless, the identity of overactive proteases released by human colonic mucosa remains unknown. Herein, we employed a serine protease-targeted activity-based probe (ABP) coupled with mass spectral...
ORGANISM(S): Homo sapiens (Human) 
2018-05-18 | PXD009450 | Pride
Inflammation Functional proteomics Activity-based probe Serine protease Inflammatory bowel disease 
UnknownUnexpected Activity of a Novel Kunitz-type Inhibitor: INHIBITION OF CYSTEINE PROTEASES BUT NOT SERINE PROTEASES.
Not available
S-EPMC5016662 | biostudies-literature
UnknownDescription of staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease.
Not available
S-EPMC97868 | biostudies-literature
UnknownCoumarin as a structural component of substrates and probes for serine and cysteine proteases.
Not available
S-EPMC7219385 | biostudies-literature
UnknownPosttranslational modifications of serine protease TMPRSS13 regulate zymogen activation, proteolytic activity, and cell surface localization.
Not available
S-EPMC8503615 | biostudies-literature
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