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UnknownHSP90AA1 is an unfavorable prognostic factor for hepatocellular carcinoma and contributes to tumorigenesis and chemotherapy resistance.
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S-EPMC11736399 | biostudies-literature
ProteomicsNew antimicrobial agents development
With the growing antibiotic resistance of Staphylococcus aureus, it is urgent to discover new antimicrobials to solve this problem. By bacterial growth based high-throughput screening, we identified two compounds, C218-0546 and STK848198, with effective antimicrobial activity against S. aureus. This...
ORGANISM(S): Staphylococcus Aureus 
2024-05-20 | PXD052423 |
ProteomicsIntegrated Single-Cell Proteomics Analysis on an Active Matrix Digital Microfluidic Chip
We introduce and implement a comprehensive single-cell proteomics sample pre-treatment solution based on an active matrix digital microfluidics chip(AM-DMF-SCP). This platform accommodates high-throughput single-cell isolation and seamless, non-destructive sample pre-treatment, characterized by its ...
ORGANISM(S): Homo Sapiens 
2024-04-15 | PXD048434 |
ProteomicsMass-spectroscopic quantification of CHAC1-regulated protein cysteine S-glutathionylation
S-glutathionylation is an important post-translational modification of a cysteine residue of target protein. We applied a quantitative redox proteomics approach to identify the specific cysteine residues as targets of S-glutathionylation. Using this approach, we profiled CHAC1-associated changes in ...
ORGANISM(S): Mus Musculus 
2024-03-12 | PXD050569 |
ProteomicsProteomic analysis of hydrolase levels in the lysosomes from macrophages stimulated with or without LPS via LC_MS
Proteomic analysis of hydrolase levels in the lysosomes from macrophages stimulated with or without LPS via liquid chromatography–mass spectrometry (LC-MS), highlighting the expected LPS-induced increase in accumulation of proteases, ribonucleases (RNase) and other hydrolases.
ORGANISM(S): Mus Musculus 
2024-10-14 | PXD056776 |
ProteomicsDetection of residual peptides of SARS-CoV-2 peptide after a 24-hour co-incubation with h-lysoTRAP via proteomic analysis
To gain a deeper insight into the residual SARS-CoV-2 peptides after degradation, we directly detected fragments (lower than 10 (kilodalton) kDa) of degraded SARS-CoV-2 via LC-MS, and overlapped these with the 3D crystal structure of SARS-CoV-2 proteins.
ORGANISM(S): Severe Acute Respiratory Syndrome Coronavirus 2 
2024-10-18 | PXD056987 |
ProteomicsDegradation analysis of SARS-CoV-2 proteins by h-lysoTRAP
To investigate the degradation activity of proteases inside lysosomal "TRAP", we conducted proteomic analysis of lysosomal "TRAP" with trapped authentic SARS-CoV-2.
ORGANISM(S): Severe Acute Respiratory Syndrome Coronavirus 2 
2024-10-18 | PXD056985 |
ProteomicsDegradation analysis of SARS-CoV-2 proteins after incubation with h-lysoTRAP based on the proteomics data
To investigate the degradation activity of proteases inside lysosomal "TRAP", we conducted proteomic analysis of lysosomal "TRAP" with trapped authentic SARS-CoV-2.
ORGANISM(S): Severe Acute Respiratory Syndrome Coronavirus 2 
2024-10-15 | PXD056801 |
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