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MetabolomicsThioridazine induce phospholipid accumulation and necroptosis in breast cancer cells
An antipsychotic drug, Thioridazine has been shown to inhibit a broad spectrum of cancer cells. However, its molecular mechanism is still not well understood. In the present study, we have shown that thioridazine induces cytostatic effects in both parental and tamoxifen-resistant cancer cells throug...
2025-02-20 | MTBLS11870 | MetaboLights
MetabolomicsDeadly Duality of PEBP1: Shutting off Necroptosis, Turning on Ferroptosis
Not available
ORGANISM(S): Mus musculus 
ST001334 | MetabolomicsWorkbench
ProteomicsQuantitative proteomics characterization of proteins modified by very long chain fatty acids (VLCFAs) under necroptosis
Necroptosis is a caspase-independent form of regulated cell death that is characterized by membrane permeabilization and rupture. This membrane rupture is responsible for the inflammatory properties of necroptosis and is critical for disease states involving this process. In efforts to understand ho...
ORGANISM(S): Homo sapiens (Human) 
2021-05-25 | PXD022527 | Pride
Ionstar proteomics acylation necroptosis 
TranscriptomicsGene expression profiling of L-540 Hodgkin lymphoma cell line after in vitro and in vivo treatment with Givinostat in combination with Sorafenib
Relapsed/refractory Hodgkin lymphoma (HL) is an unmet medical need requiring new therapeutic options. Interactions between the histone deacetylase inhibitor Givinostat and the RAF/MEK/ERK inhibitor Sorafenib were examined in HDLM-2 and L-540 HL cell lines. Exposure to Givinostat/Sorafenib induced a ...
ORGANISM(S): Homo sapiens 
2015-03-01 | E-GEOD-65483 | biostudies-arrayexpress
TranscriptomicsGene expression profiling of HDLM-2 Hodgkin lymphoma cell line after in vitro and in vivo treatment with Givinostat in combination with Sorafenib
Relapsed/refractory Hodgkin lymphoma (HL) is an unmet medical need requiring new therapeutic options. Interactions between the histone deacetylase inhibitor Givinostat and the RAF/MEK/ERK inhibitor Sorafenib were examined in HDLM-2 and L-540 HL cell lines. Exposure to Givinostat/Sorafenib induced a ...
ORGANISM(S): Homo sapiens 
2015-03-01 | E-GEOD-65479 | biostudies-arrayexpress
ProteomicsSystematic comparative analysis of extracellular vesicles following apoptosis, necroptosis and ferroptosis
The formation of extracellular vesicles (EVs) has emerged as a novel paradigm in cell-to-cell communication during health and disease. According to the type of cell death modalities, the intercellular functions of EVs may be influenced by their biogenesis and composition. To identify a possible EV c...
ORGANISM(S): Mus musculus (Mouse) 
2023-10-12 | PXD039297 | Pride
Necroptosis Extracellular vesicles Ferroptosis Apoptosis Cell death 
TranscriptomicsRNA-seq of mice TRAF2/Casp-8LPC-KO tumors
This model was used to study the relationship between NF-kB and PCD regulation and generated mice with combined conditional ablation of Traf2 and Caspase-8 (TRAF2/Casp-8LPC-KO) in order to block apoptosis and specifically study the role of necroptosis in Traf2-deficient hepatocytes in vivo.
ORGANISM(S): Mus musculus 
2019-05-31 | E-MTAB-4598 | biostudies-arrayexpress
ProteomicsQuantitative analysis of phosphoproteome in necroptosis
we conducted a systemic quantitative analysis of phosphoproteome regulated by RIPK1 kinase across a time course from complex I to complex IIb formation during necroptosis of FADD deficient Jurkat cells induced by TNFα
ORGANISM(S): Homo Sapiens 
PXD025313 |
ProteomicsOligomerisation-driven MLKL ubiquitylation antagonises necroptosis
Mixed lineage kinase domain-like (MLKL) is the executioner in the caspase 8-independent form of programmed cell death called necroptosis. Once Receptor Interacting serine/threonine Protein Kinase 3 (RIPK3) is activated by upstream cell death signals, it phosphorylates MLKL and triggers the oligomeri...
ORGANISM(S): Mus musculus (Mouse) 
2021-04-28 | PXD015537 | Pride
Ubiquitylation Oligomerisation Membranes Necroptosis Mlkl 
GenomicsQuantitative analysis of phosphoproteome in necroptosis reveals a role of TRIM28 phosphorylation in promoting necroptosis-induced cytokine production
Quantitative analysis of phosphoproteome in necroptosis reveals a role of TRIM28 phosphorylation in promoting necroptosis-induced cytokine production
PRJNA718774 | ENA
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