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MetabolomicsAberrant L-Fucose accumulation and increased core fucosylation are metabolic liabilities in mesenchymal glioblastoma (Xenograft assays)

Glioblastoma (GBM) is a common and deadly form of brain tumor in adults. Dysregulated metabolism in GBM offers an opportunity to deploy metabolic interventions as precise therapeutic strategies. To identify the molecular drivers and the modalities by which different molecular subgroups of GBM exp...

2022-11-08 | MTBLS730 | MetaboLights
MetabolomicsAberrant L-Fucose accumulation and increased core fucosylation are metabolic liabilities in mesenchymal glioblastoma (Stem cell and cell line assays)

Glioblastoma (GBM) is a common and deadly form of brain tumor in adults. Dysregulated metabolism in GBM offers an opportunity to deploy metabolic interventions as precise therapeutic strategies. To identify the molecular drivers and the modalities by which different molecular subgroups of GBM exp...

2022-11-08 | MTBLS4708 | MetaboLights
ProteomicsImproving the Accuracy and Efficiency of Core Fucose Identification Using Machine Learning
In this study, we employed artificial intelligence to address the challenges in identifying core fucose due to migration effects. By knocking out the FUT8 gene in normal mouse brains, we ensured accurate labeling of non-core fucosylated glycans, enabling the identification of mannose glycans with co...
ORGANISM(S): Mus musculus (Mouse) 
2025-09-29 | PXD062880 | Pride
Core fucose Mouse brain Intact glycopeptides Fut8 knockout 
ProteomicsA “Two birds One Stone” Strategy for Site-specific Analysis of the Core Fucosylation and O-GlcNAcylation
Core fucosylation and O-GlcNAcylation are two most famous protein glycosylations and regulate diverse physiological and pathological processes in living organism. Core fucosylation is a protein glycosylation in which a L-fucose residue attaches to the innermost N-acetylglucosamine (GlcNAc) of N-glyc...
ORGANISM(S): Homo Sapiens 
2023-12-04 | PXD047486 |
GenomicsAberrant L-Fucose accumulation and increased core fucosylation are specific metabolic liabilities in mesenchymal glioblastoma
Aberrant L-Fucose accumulation and increased core fucosylation are specific metabolic liabilities in mesenchymal glioblastoma
PRJNA834980 | ENA
TranscriptomicsFucose-mediated transcriptional activation of the fcs operon by FcsR in Streptococcus pneumoniae
In this study, we explore the impact of fucose on the transcriptome of S. pneumoniae D39. The expression of various genes and operons, including the fucose uptake PTS and utilization operon (fcs operon), was altered in the presence of fucose. By means of quantitative RT-PCR and β-galactosidase analy...
ORGANISM(S): Streptococcus pneumoniae D39 
2015-04-23 | E-GEOD-65673 | biostudies-arrayexpress
TranscriptomicsAberrant L-Fucose accumulation and increased core fucosylation are specific metabolic liabilities in mesenchymal glioblastoma
Dysregulated metabolism in glioblastoma (GBM), the deadliest brain tumor of adults, offers an opportunity to deploy metabolic interventions as precise therapeutic strategies. To identify the molecular drivers and the modalities by which different molecular subgroups of GBM exploit metabolic rewiring...
ORGANISM(S): Homo sapiens 
2022-11-08 | GSE202200 | GEO
UnknownCore-6 fucose and the oligomerization of the 1918 pandemic influenza viral neuraminidase.
Not available
S-EPMC4862876 | biostudies-literature
ProteomicsA Sensitive and Reversible Labeling Strategy Enables Global Mapping of the Core-Fucosylated Glycoproteome on Cell Surfaces
Core fucosylation, the attachment of α1,6-fucose to the innermost GlcNAc residue of N-glycans, is a unique protein glycosylation in living organisms. It plays significant roles in diverse physiological and pathological processes, and its upregulation has been observed in many cancers. Core fucosylat...
ORGANISM(S): Homo Sapiens 
2022-08-13 | PXD036051 |
ProteomicsProteomic identification of the proteins that co-precipitated with FUT8
Essential roles of FUT8 SH3 domain in core fucosylation
ORGANISM(S): Homo Sapiens (human) 
2020-04-29 | PXD018032 | JPOST Repository
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