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UnknownStress triggers gut dysbiosis via CRH-CRHR1-mitochondria pathway.
Not available
S-EPMC11442948 | biostudies-literature
ProteomicsProteomic and phosphoproteomic landscape reveals the functional contributions of circadian gene Bmal1 in rat nucleus pulposus cells
Intervertebral disc degeneration (IDD) is a major cause of low back pain (LBP), and the pathogenesis remains unknown. Recently, an autoregulating circadian rhythm was identified in intervertebral discs (IVDs), the abolition of which led to IDD. The genetic disruption of the mouse IVD molecular clock,...
ORGANISM(S): Rattus Norvegicus 
PXD029273 |
ProteomicsRIPK2 promotes colorectal cancer metastasis by protecting YAP degradation from ITCH-mediated ubiquitination
Colorectal cancer (CRC) is a leading cause of cancer death. RIPK2 is identified as a poor prognostic marker, promoting metastasis via bacterial invasion. High RIPK2-expressing tumor cells show enhanced invasiveness. This dataset comprises quantitative proteomic profiles of colorectal cancer (CRC) ce...
ORGANISM(S): Homo Sapiens 
2025-03-03 | PXD061372 |
ProteomicsDiscovery of Novel MLKL PROTAC Degrader for the Treatment of Hepatocellular Carcinoma via Promoting Parthanatos
Chen et al. discovered a highly potent and selective MLKL-targeted PROTAC C116 that effectively induces MLKL degradation and promotes parthanatos in HCC cells. More significantly, C116 was able to induce in vivo MLKL degradation and exerts anti-tumor activities in an orthotopic HCC tumor model, posi...
ORGANISM(S): Mus Musculus 
PXD069462 |
ProteomicsInsight of novel biomarkers for papillary thyroid carcinoma through multi-omics
Our multi-omics analysis of local patients demonstrated significant distinctions compared to TCGA-THCA cohorts, highlighting the unique genetic characteristics of Chinese individuals with PTC. We identified novel biomarkers that hold potential for diagnosis and prognosis of PTC. Furthermore, develop...
ORGANISM(S): Homo Sapiens 
PXD044815 |
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 |
UnknownRobust estimation of bacterial cell count from optical density.
Not available
S-EPMC7499192 | biostudies-literature
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