Sort   by:  
 Page size 
ProteomicsFerlins and TgDOC2 in Toxoplasma microneme, rhoptry and dense granule secretion
Stable Isotope Labeling with Amino acids in Cell culture (SILAC) proteomics on the proteinsreleased in a set of T. gondii secretion mutants.
ORGANISM(S): Toxoplasma gondii CtCo5 
2021-09-10 | PXD024210 | Pride
Secretion Toxoplasma gondii 
ProteomicsDiverse Compounds from Pleuromutilin Lead to a Thioredoxin Inhibitor and Inducer of Ferroptosis
The chemical diversification of natural products provides a robust and general method for creation of stereochemically complex and structurally diverse small molecules. The resulting compounds have physicochemical traits different from those in most screening collections, and as such are a rich sour...
ORGANISM(S): Homo sapiens (Human) 
2020-05-26 | PXD012805 | Pride
Ferroptosis Thioredoxin 
ProteomicsClickable Glutathione Approach for Identification of Protein Glutathionylation in Response to Glucose Metabolism
Glucose metabolism and mitochondrial function are closely interconnected with cellular redox-homeostasis. Although glucose starvation, which often occurs in ischemic heart or insufficient vascularization of tumor cells, is known to induce redox-disturbance, global and individual protein glutathionyl...
ORGANISM(S): Homo sapiens (Human) 
2018-10-26 | PXD004026 | Pride
Glutathionylation 
ProteomicsIdentification of a S. aureus virulence factor by activity-based protein profiling (ABPP)
Serine hydrolases play diverse roles in regulating host-pathogen interactions in a number of organisms, yet few have been characterized in the human pathogen Staphylococcus aureus. Here, we describe a chemical proteomic screen that identified 10 previously uncharacterized S. aureus serine hydrolases...
ORGANISM(S): Staphylococcus aureus 
2018-05-17 | PXD009210 | Pride
Abpp S. aureus Serine hydrolase 
ProteomicsChemoproteomic profiling of host and pathogen enzymes active in cholera
Activity-based protein profiling (ABPP) is a chemoproteomic tool for detecting active enzymes in complex biological systems. We used ABPP to identify secreted bacterial and host serine hydrolases that are active in animals infected with the cholera pathogen Vibrio cholerae. Four V. cholerae protease...
ORGANISM(S): Vibrio cholerae O1 str. VC91 
2016-02-22 | PXD003000 | Pride
Vibrio cholerae  rabbit 
ProteomicsMonitoring Fe-S cluster occupancy across the E. coli proteome using chemoproteomics
Iron-sulfur (Fe-S) clusters are ubiquitous metallocofactors involved in redox chemistry, radical generation, and gene regulation. Common methods to monitor Fe-S clusters include spectroscopic analysis of purified proteins, and auto-radiographic visualization of radiolabeled iron distribution in prot...
ORGANISM(S): Escherichia coli 
2024-05-22 | PXD026488 | Pride
Redime Iron-sulfur clusters Isotop-abpp E. coli 
ProteomicsThe antimalarial natural product salinipostin A identifies essential alpha/beta serine hydrolases involved in lipid metabolism in P. falciparum parasites
Salinipostin A (Sal A) is a bicyclic phosphotriester natural product isolated from the marine bacterium Salinospora sp. that exhibits potent antimalarial activity. However, the direct targets and mechanisms by which it exerts its effects are poorly understood. Here, we use semi-synthesis to generate...
ORGANISM(S): Plasmodium falciparum 58.1 
2020-01-24 | PXD016835 | Pride
Salinipostin a Serine hydrolase 
ProteomicsHuman cytomegalovirus-induced host protein citrullination is crucial for viral replication
Citrullination is the conversion of arginine-to-citrulline by protein arginine deiminases (PADs), whose dysregulation is implicated in the pathogenesis of various types of cancers and autoimmune diseases. Consistent with the ability of human cytomegalovirus (HCMV) to induce post-translational modifi...
ORGANISM(S): Homo sapiens (Human) 
2021-07-20 | PXD025818 | Pride
Citrullination 
UnknownMonitoring Fe-S cluster occupancy across the E. coli proteome using chemoproteomics.
Not available
S-EPMC9992348 | biostudies-literature
ProteomicsE. coli monothiol glutaredoxin GrxD replenishes Fe-S clusters to the essential ErpA A-type carrier under low iron stress  
Iron-sulfur (Fe-S) clusters are required for essential biological pathways, including respiration and isoprenoid biosynthesis. Complex Fe-S cluster biogenesis systems have evolved to maintain an adequate supply of this critical protein cofactor. In Escherichia coli, two Fe-S biosynthetic systems, th...
ORGANISM(S): Escherichia coli 
2024-07-13 | PXD053317 | Pride
Iron-sulfur (fe-s) protein Monothiol glutaredoxin grxd A-type carrier erpa Mass spectrometry (ms) E. coli Chemoproteomics Iron metabolism Metal homeostasis 
Sort   by:  
 Page size