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MetabolomicsExogenous L-Alanine promotes phagocytosis multidrug-resistant bacterial pathogens (V. parahaemolyticus-infected spleen metabolomics)

Multidrug-resistant bacteria present a major threat to public health. Therefore, new drugs or approaches are urgently needed to manage and mitigate this threat. Here, we screen the molecular candidates that allow the survival of mice upon Vibrio parahaemolyticus infection by integrated p...

2024-09-26 | MTBLS7996 | MetaboLights
ProteomicsSystematic analysis of lysine malonylation in Streptococcus mutans
Lysine malonylation is an evolutionarily conserved PTM from bacteria to mammals and involves malonyl-coenzyme (CoA) as a cofactor. Since the malonyl group has an acidic carboxylic group under physiological pH, malonylated lysine is negatively charged, which might impact on protein function and enzym...
ORGANISM(S): Streptococcus mutans UA159 
2022-11-17 | PXD038045 | Pride
Malonylation Biofilm Post-translational modification Streptococcus mutans 
ProteomicsS-glutathionylation proteome profiling of Streptococcus mutans
S-glutathionylation is an important post-translational modification (PTM) process that targets the protein cysteine thiol by the addition of glutathione (GSH). This modification can prevent proteolysis from over-oxidation of protein cysteine residue during the condition of oxidative or nitrosative s...
ORGANISM(S): Streptococcus mutans UA159 
2020-07-14 | PXD019564 | Pride
S-glutathionylation  streptococcus mutans  post-translational modification 
UnknownAn-Luo-Hua-Xian Pill Improves the Regression of Liver Fibrosis in Chronic Hepatitis B Patients Treated with Entecavir.
Not available
S-EPMC9817059 | biostudies-literature
ProteomicsLysine lactylation regulates biofilm formation of streptococcus mutans
Lactate produced in glycolysis has recently been discovered to modify lysine residues on eukaryotic proteins, a post-translational modification (PTM) called lysine lactylation (Kla). This modification not only participates in regulating gene expression through lactylation of histones, but also impac...
ORGANISM(S): Escherichia coli 
2023-08-24 | PXD037027 | Pride
Lactylation  streptococcus mutans  biofilm 
ProteomicsProteomic analysis of Streptococcus mutans after RpoA-K173R mutation
Functional experiments have found a significant increase in EPS synthesis upon the elimination of lactylation at RpoA Lys173. Thus we investigated the regulatory mechanisms by proteomic approah.
ORGANISM(S): Streptococcus mutans UA159 
2023-08-24 | PXD042680 | Pride
Rna polymerase Streptococcus mutans 
ProteomicsTargeting Supramolecular Active Complexes of Nav 1.7/Nav 1.8 to Relieve Chronic Neuropathic Pain
The aim of this project was to identify the proteins participating in assemble of supramolecular active complex containing Nav1.7 and Nav1.8 in dorsal root ganglia (DRG) of mice with nerve injury 6 weeks. DRG and spinal dorsal horn (SDH) tissues were collected from spared nerve injury mice and sham-...
ORGANISM(S): Mus musculus (Mouse) 
2026-07-29 | PXD039251 | Pride
Mouse Lc-ms Drg 
UnknownGenetic analyses reveal independent domestication origins of the emerging oil crop Paeonia ostii, a tree peony with a long-term cultivation history.
Not available
S-EPMC5509724 | biostudies-literature
UnknownIntracellular MicroRNA imaging using telomerase-catalyzed FRET ratioflares with signal amplification.
Not available
S-EPMC6677110 | biostudies-literature
ProteomicsProteome profiling of Candida albicans
The complex ecological dynamics between Streptococcus mutans and Candida albicans within dental plaque biofilms play a pivotal role in the etiology of dental caries. To investigate the "contact-independent" interactions between these two species, we developed a transwell co-culture system. Utilizing...
ORGANISM(S): Candida albicans (Yeast) 
2025-01-25 | PXD059152 | Pride
Candida albicans Streptococcus mutans Lc-ms/ms 
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