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MetabolomicsTFAM loss induces nuclear actin assembly upon mDia2 malonylation to promote liver cancer metastasis
The mechanisms underlying cancer metastasis remain poorly understood. Here, we report that TFAM deficiency rapidly and stably induced spontaneous lung metastasis in mice with liver cancer. Interestingly, unexpected polymerization of nuclear actin was observed in TFAM-knockdown HCC cells when cytoske...
2022-06-23 | MTBLS4307 | MetaboLights
UnknownEffects of non-pharmacological interventions on biochemical hyperandrogenism in women with polycystic ovary syndrome: a systematic review and network meta-analysis.
Not available
S-EPMC11744805 | biostudies-literature
ProteomicsProteomic changes of C. sakazakii BAA-894 exposed to p-coumaric acid
interaction of Cronobacter sakazakii with p-coumaric acid
ORGANISM(S): Cronobacter Sakazakii Atcc Baa-894 
2022-03-03 | PXD032021 |
ProteomicsA “One-step” Strategy for the Global Characterization of Core-Fucosylated Glycoproteome
Core fucosylation, a special type of N-linked glycosylation, is important in tumor proliferation, invasion, metastatic potential, and therapy resistance. However, the core-fucosylated glycoproteome has not been extensively profiled due to the low abundance and poor ionization efficiency of glycosyla...
ORGANISM(S): Homo Sapiens 
2024-04-02 | PXD051139 |
ProteomicsEndoglycosidases- treated N-glycosylation site identification
Glycoproteins, representing over 50% of human proteins and most biopharmaceuticals, are crucial for regulating various biological processes. The complexity of multiple glycosylation sites often leads to incomplete sequence coverage and ambiguous glycan modification profiles. Here, we developed an in...
ORGANISM(S): Homo Sapiens 
2024-12-30 | PXD059329 |
ProteomicsDecoding protein glycosylation by an integrative mass spectrometry-based de novo sequencing strategy
Glycoprotein is one of the most complex biomacromolecule，accounting for over 50% of total human proteins and the majority of biopharmaceuticals, exerting profound influences on various essential biological processes. With multiple N-glycosylation sites and O- glycosylation sites on the protein backb...
ORGANISM(S): Homo Sapiens Bos Taurus 
2024-08-24 | PXD055221 |
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