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ProteomicsER-associated degradation of Eag1 potassium channels by the RING E3 ubiquitin ligase MKRN1: the presence of a dual ubiquitination system
Mutations in the human gene encoding the neuron-specific Eag1 voltage-gated K+ channel are associated with neurodevelopmental diseases, indicating an important role of Eag1 during brain development. A disease-causing Eag1 mutant channel is linked to defective protein stability that involves enhanced...
ORGANISM(S): Homo sapiens (Human) 
2021-09-10 | PXD023984 | Pride
Ring e3 Mkrn1 
ProteomicsPhosphorylation of claudin-11 - Mass spectrometry analysis confirmed the phosphorylation of human claudin-11 at tyrosine 191 and tyrosine 192
Mass spectrometry analysis confirmed the phosphorylation of human claudin-11 at tyrosine 191 and tyrosine 192
ORGANISM(S): Homo sapiens (Human) 
2018-08-29 | PXD010908 | Pride
Claudin-11 Phosphorylation Human 
UnknownReduced mitochondria membrane potential and lysosomal acidification are associated with decreased oligomeric Aβ degradation induced by hyperglycemia: A study of mixed glia cultures.
Not available
S-EPMC8786178 | biostudies-literature
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 
ProteomicsActivation of Akt, Nrf2, and NF-κB signal transduction pathways in the liver as a mechanism of survival for torpid Myotis ricketti Bats
Unfolded protein accumulation in the lumen of endoplasmic reticulum (ER) induced by cold exposure is termed UPRER. Some mammals hibernate to overcome cold winter. We investigated whether hibernating bats are under UPRER and activate Akt, Nrf2, and NF-κB signaling pathways that are critical for cell ...
ORGANISM(S): Myotis ricketti 
2020-11-17 | PXD016109 | Pride
Mitochondria Eif2 Akt Hibernation Upr And lc-ms/ms Nf-κb Bats Proteomics Liver 
UnknownA Comparative Study of the Influence of Nitrogen Content and Structural Characteristics of NiS/Nitrogen-Doped Carbon Nanocomposites on Capacitive Performances in Alkaline Medium.
Not available
S-EPMC8308313 | biostudies-literature
UnknownConstructing a Carbon-Encapsulated Carbon Composite Material with Hierarchically Porous Architectures for Efficient Capacitive Storage in Organic Supercapacitors.
Not available
S-EPMC9223422 | biostudies-literature
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 
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