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ProteomicsPI3K/mTOR specific phospho-antibody microarray to study the effect of rapamycin to the innate immune respsonse
To comprehensively analyze the effects of mTORC1 inhibition on GSK3, we employed the use of a PI3K/mTOR-specific phospho-antibody microarray that analyzed the site-specific phosphorylation of over 130 kinases within the PI3K/mTOR pathway. The phosphorylation levels of different kinases in monocytes...
ORGANISM(S): Homo sapiens 
2010-11-25 | E-GEOD-25520 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of human monocytes after treatment vehicle, isotype control antibody, TREM1 antibody, LPS, isotype control antibody plus LPS and TREM1 antibody plus LP to invesigate innate immune responses to TREM-1 activation
TREM-1 is an orphan immunoreceptor expressed on monocytes, macrophages, and neutrophils. TREM-1 associates with and signals via the adapter protein DAP12/TYROBP, which contains an immunoreceptor tyrosine-based activation motif (ITAM). TREM-1 activation by receptor cross-linking is pro-inflammatory, ...
ORGANISM(S): Homo sapiens 
2008-04-05 | E-GEOD-9988 | biostudies-arrayexpress
TranscriptomicsGene expression profiles of Herceptin-resistant breast cancer cells
Herceptin (trastuzumab) is a humanized monoclonal antibody targeted to the Her2 receptor tyrosine kinase. Despite a robust response rate to Herceptin-based therapies in Her2-positive patients, resistance frequently arises within one year of the initial response. To address the mechanism of Hercept...
ORGANISM(S): Homo sapiens 
2009-08-21 | E-GEOD-15043 | biostudies-arrayexpress
ProteomicsPI3Kalpha Immunocomplex Identification
Mass Spectrometry Analysis of PI3Ka Immunocomplex via immunoprecipitation and SDS-PAGE separation
ORGANISM(S): Homo sapiens (Human) 
2022-02-16 | PXD021306 | Pride
P85alpha antibody Pi3kalpha Immunoprecipitation Map4 protein 
TranscriptomicsMutant PI3K cooperates with HER2 to promote mammary tumor formation and induces trastuzumab resistance in vivo
HER2 (ERBB2) gene amplification and PIK3CA mutations often co-occur in breast cancer, and aberrant activation of the PI3K pathway has been implicated in resistance to HER2-directed therapies. We have created a mouse model of HER2-overexpressing (HER2+), PIK3CAH1047R-mutant breast cancer. Mice expres...
ORGANISM(S): Mus musculus 
2013-09-03 | E-GEOD-41118 | biostudies-arrayexpress
GenomicsCharacterizing the profiles of Ebf1 in mouse fat cells (ChIP-seq)
ChIP-seq data from mouse adipocyte. Mature 3T3-L1 adipocytes were cross-linked with 1% formaldehyde 10 days after induction with MDI. Frozen cell pellets were submitted to the Broad Institute for subsequent analysis of Ebf1-bound regions using anti-Ebf1 antibody (Abnova H00001879-M01).
ORGANISM(S): Mus musculus 
2014-06-10 | E-GEOD-58330 | biostudies-arrayexpress
ProteomicsProteomic profiling of colorectal cancer cell culture samples treated with apoptosis- and mTOR inhibitors under normoxia and hypoxia
To examine changes in tyrosine kinase activity in colorectal cancer cell culture samples treated with apoptosis inhibitors or/and mTOR inhibitors, under normoxic or/and hypoxic experimental conditions.
ORGANISM(S): Homo sapiens 
2016-06-15 | E-MTAB-3870 | biostudies-arrayexpress
UnknownAngiotensin II stimulates phosphorylation of an ectodomain-truncated platelet-derived growth factor receptor-beta and its binding to class IA PI3K in vascular smooth muscle cells.
Not available
S-EPMC1513282 | biostudies-literature
TranscriptomicsPI3K inhibition results in enhanced estrogen receptor function and dependence in hormone receptor-positive breast cancer
Activating mutations of PIK3CA are the most frequent genomic alterations in estrogen receptor (ER)-positive breast tumors and selective PI3Kα inhibitors are in clinical development. The activity of these agents, however, is not homogenous and only a fraction of patients bearing PIK3CA-mutant ER-posi...
ORGANISM(S): Homo sapiens 
2015-04-29 | E-GEOD-64033 | biostudies-arrayexpress
UnknownO-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
Not available
S-EPMC2816021 | biostudies-literature
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