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ProteomicsVibrio parahaemolyticus LC-MS/MS
The lysine acetylation of proteins is a major post-translational modification that plays an important regulatory role in almost every aspect of cells, both eukaryotes and prokaryotes. Vibrio parahaemolyticus, a model marine bacterium, is a worldwide cause of bacterial seafood-borne illness. Here, we...
ORGANISM(S): Vibrio paraaemolytics RIMD 2210633 
2017-08-23 | PXD000924 | Pride
Acetylome V. parahaemolyticus Lysine acetylation Lysine acetylation motif Interaction network 
ProteomicsDeletion of vp0057 impacts the proteome profile in Vibrio parahaemolyticus
Using bioinformatics analysis, we found that VP0057 may be a potential Ser/Thr protein kinase with phosphorylation activity. Thus, we constructed the vp0057-deletion mutant (∆vp0057) from the wild-type V. parahaemolyticus serotype O3:K6 and employed a mass spectrometry-based proteomic strategy to ch...
ORGANISM(S): Vibrio Parahaemolyticus Rimd 2210633 
PXD021775 |
ProteomicsImpacts of Ser/Thr protein kinase Stk1 on proteome, twitching motility and competitive advantage in Pseudomonas aeruginosaImpacts of Ser/Thr protein kinase Stk1 on proteome, twitching motility and competitive advantage in Pseudomonas aeruginosa
Pseudomonas aeruginosa is a ubiquitous Gram-negative bacterium in the environment and a leading cause of nosocomial infections worldwide. Therefore, it is listed by the World Health Organization as one of the human pathogens that urgently need to develop new antibacterial drugs. Recent findings have...
ORGANISM(S): Pseudomonas aeruginosa PAK 
2021-07-07 | PXD027148 | Pride
Stk1 Ser/thr protein kinase Twitching motility Competitive advantage Pseudomonas aeruginosa. Proteome 
ProteomicsThe characterization of column heating effect in nano-flow liquid chromatography mass spectrometry (nanoLC-MS)-based proteomics
In this study, we systematically compared the proteomics identification results obtained under room temperature and high temperature.
ORGANISM(S): Homo Sapiens 
2020-01-09 | PXD017016 |
ProteomicsProteome-wide Hyposuccinylation of Esophageal Squamous Cell Cancer to Promotion of Tumor Metabolism and Migration
We identify abnormal protein and post-translational modification (PTM) pathways, including significantly downregulated lysine succinylation sites in cancer cells. Focusing on hyposuccinylation, we reveal that this altered PTM was enriched on enzymes of metabolic pathways inextricably linked with can...
ORGANISM(S): Homo Sapiens 
PXD021567 |
ProteomicsHistone PTMs dataset for Hyposuccinylation Derived from Abnormal Metabolism Promotes the Cell Migration of Esophageal Squamous Cell Cancer
We identify abnormal protein and post-translational modification (PTM) pathways, including many downregulated lysine succinylation sites in cancer cells. Focusing on hyposuccinylation, we reveal that this altered PTM was enriched on enzymes of metabolic pathways and the reduced succinyl-CoA may lead...
ORGANISM(S): Homo Sapiens 
PXD021700 |
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