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ProteomicsThe changes in HNSCC cell lines (e.g., CAL-27 cetuximabR) after being treated with Cetuximab (500 ug/ml) for at least 2 months. We used LC-MS/MS to identify the main acetylation sites in resistance cell lines. In this study, it was found that the acetylation of STAT1 might hinder the downstream signaling of IFN-γ
Recent clinical trials revealed that prior use of Cetuximab may interfere with ICB efficacy. In this study, STAT1 protein levels changed after continued Cetuximab treatment (500 ug/ml). We used LC-MS/MS to compare the acetylation sites in wild-type and resistant cells. We proposed that the acetylati...
ORGANISM(S): Homo sapiens (Human) 
2025-12-29 | PXD054332 | Pride
Human Lc-msms Hnscc Cetuximab resistance Acetylation 
ProteomicsThe changes in cetuximab resistant HNSCC cell lines (e.g., OECM1-cetuximabR and CAL-27 cetuximabR) after being treated with Cetuximab (500 ug/ml) for at least 2 months. We used LC-MS/MS to identify the main phosphorylation sites in resistance cell lines.
Recent clinical trials revealed that prior use of Cetuximab may interfere with ICB efficacy. In this study, STAT1 protein levels changed after continued Cetuximab treatment (500 ug/ml). We used LC-MS/MS to compare the phosphorylation sites in wild-type and resistant cells. We proposed that the phosp...
ORGANISM(S): Homo sapiens (Human) 
2025-12-29 | PXD054186 | Pride
Human Lc-msms Hnscc Cetuximab resistance Phosphorylation 
ProteomicsThe changes in HNSCC cell lines (e.g., OECM1) when treated with Cetuximab (500 ug/ml) at different passages. We used LC-MS/MS to identify the main target pathway. These findings could significantly enhance our evidence.
Recent clinical trials revealed that prior use of Cetuximab may interfere with ICB efficacy. In this study, STAT1 protein levels changed after continued Cetuximab treatment (500 ug/ml). We collected serial passages of cetuximab resistance HNSCC cell lines to perform LC-MS/MS. We identified the IFN p...
ORGANISM(S): Homo sapiens (Human) 
2025-12-29 | PXD054113 | Pride
Human Lc-msms Hnscc Cetuximab 
ProteomicsComparative O-GlcNAc Proteomic Analysis Reveals a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness
O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT). Despite the reported association of O-GlcNAcylation with cancer metastasis, the O-GlcNAc proteome profile for cancer aggressiveness remains largely uncharac-terized. Here we r...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD029627 | Pride
Lung adenocarcinoma  o-glcnac transferase  o-glcnacylation  sam68 
UnknownActin-binding protein G (AbpG) participates in modulating the actin cytoskeleton and cell migration in Dictyostelium discoideum.
Not available
S-EPMC4357508 | biostudies-literature
UnknownPilloin, A Flavonoid Isolated from Aquilaria sinensis, Exhibits Anti-Inflammatory Activity In Vitro and In Vivo.
Not available
S-EPMC6320910 | biostudies-literature
UnknownSurvival-related genes are diversified across cancers but generally enriched in cancer hallmark pathways.
Not available
S-EPMC9066720 | biostudies-literature
UnknownComparative O-GlcNAc Proteomic Analysis Reveals a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness.
Not available
S-EPMC8749979 | biostudies-literature
UnknownPostoperative rhinosinusitis and microbiological outcomes following endoscopic endonasal approaches: A retrospective analysis of 300 patients.
Not available
S-EPMC12718862 | biostudies-literature
UnknownTherapeutic stress triggers tumor STAT1 acetylation to disarm immunotherapy.
Not available
S-EPMC12711663 | biostudies-literature
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