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TranscriptomicsTranscriptional profiles of TIMP-2 and Ala+TIMP-2 A549 overexpressing cells and in tumor xenografts.
TIMP-2 is an endogenous angiogenesis inhibitor, i.e. inhibits endothelial cell proliferation and tumor angiogenesis. As a result, TIMP-2 inhibits tumor growth and progression to metastasis. Understanding, therefore, the mechanisms of TIMP-2-mediated tumor growth inhibition would provide further supp...
ORGANISM(S): Homo sapiens 
2013-01-28 | E-GEOD-38408 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of Kaposi sarcoma, normal skin and primary cells
Identification of the relationships of Kaposi sarcoma (KS), normal skin to various cell cultures. The effects of KS herpes virus, the infectious cause of KS, on infected endothelial cells are also investigated.
ORGANISM(S): Homo sapiens 
2004-08-01 | E-MEXP-66 | biostudies-arrayexpress
ProteomicsPhosphosecretome profiling and kinase-substrate interaction screening reveal key extracellular c-Src-regulated pathways
Secreted protein kinases are responsible for the phosphorylation of a vast number of extracellular phosphoproteins. The tyrosine kinase c-Src is secreted through the vesicular trafficking pathway, however, mechanistic insights into extracellular substrate specificity and potential therapeutic opport...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2023-05-30 | PXD036069 | Pride
Post translational modification The tissue inhibitors of metalloproteinases Pxxp motif Src tyrosine kinase Timps Tumor growth inhibition Phosphoproteomic Blocking antibodies Secretome 
TranscriptomicsTranscription profiling of nude mice tumor biopsies generated by the injection of mesenchymal stem cells (MSC)
Transformed MSC were injected subcutaneously into the flank of athymic CD1 nude mice (C/River). Biopsies of 1.5 cm spindle cell tumours were taken.
ORGANISM(S): Homo sapiens 
2006-12-26 | E-MEXP-562 | biostudies-arrayexpress
Proteomicsc-Abl Dependent Tyrosine Phosphorylation of theCo-chaperone Aha1 Regulates Interaction with Hsp90
The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function. The co-chaperone Aha1 stimulates Hsp90 ATPase activity tailoring the chaperone function to specific “client” proteins. The intracellular signaling mechanisms directly regulating Aha1 association wi...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080713 | MassIVE
TranscriptomicsWee1 Inhibition sensitizes prostate cancer cells to Hsp90 inhibitor to activate the intrinsic apoptotic pathway
Heat shock protein 90 (Hsp90) is an essential evolutionarily conserved molecular chaperone in eukaryotes. Cancer cells rely on Hsp90 to chaperone activated oncoproteins, and its involvement in numerous signaling pathways makes it an attractive target for drug development. Surprisingly, however, the ...
ORGANISM(S): Homo sapiens 
2013-01-10 | E-GEOD-38972 | biostudies-arrayexpress
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