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ProteomicsHuman cancer cell MCF-7 IP-PTEN MS
The MCF-7 cells were lysed using RIPA lysis buffer with a high salinity content to break out non-covalent binding of proteins. Then IP under partially denaturing conditions was performed and demonstrated that anti-PTEN precipitates were detected as smear bands, then mass spectrometry analysis of the...
ORGANISM(S): Homo sapiens (Human) 
2022-04-04 | PXD021544 | Pride
Human Breast cancer Pten Ms 
ProteomicsMCF-7 Flag-need8 IP-MS
To allow the proteomic identification of proteins modified with Nedd8, we firstly employed affinity purification and mass spectrometry to interrogate Nedd8 interactome.
ORGANISM(S): Homo sapiens (Human) 
2022-04-01 | PXD011368 | Pride
Human Breast cancer cell Ip-ms Mcf-7 
ProteomicsMCF-7 PTEN-Nedd8 IP-MS
We intended to elucidate the underlying mechanism of PTEN-Nedd8 in tumorigenesis. So, we firstly employed affinity purification and mass spectrometry to interrogate PTEN-Nedd8 interactome in nucleus.
ORGANISM(S): Homo sapiens (Human) 
2022-05-20 | PXD011395 | Pride
Human Breast cancer cell Nedd8 Pten Ip-ms 
ProteomicsDeacetylation Induced Nuclear Condensation of HP1γ Promotes Multiple Myeloma Drug Resistance
Functional crosstalk between histone modifications and chromatin remodeling has emerged as a key regulatory mode of transcriptional control during drug resistance, but the underlying mechanisms are not fully understood. Here we demonstrate that different proteins and their acetylation modification r...
ORGANISM(S): Homo Sapiens 
2023-02-20 | PXD040298 |
MetabolomicsLipidomic profiling reveals distinct differences in plasma lipid composition in healthy, prediabetic and type 2 diabetic individuals

The relationship between dyslipidemia and type 2 diabetes mellitus (T2D) has been extensively reported, but the global lipid profiles, especially in the East Asia population, associated with the development of T2D remain to be characterized. Liquid chromatography coupled to tandem mass spectromet...

2017-04-26 | MTBLS352 | MetaboLights
ProteomicsCaspase-2 is a condensate-mediated deubiquitinase in protein quality control
When cells encounter proteome stresses, caspase-2 accumulates in a ubiquitin-rich condensate, which functions as a deubiquitinase to cleave the overloaded ubiquitinated proteins.
ORGANISM(S): Homo Sapiens 
PXD041964 |
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