Publications by authors named "Eric T Sugarman"
Heat shock protein (HSP90), a highly conserved molecular chaperon, is indispensable for the maturation of newly synthesized poly-peptides and provides a shelter for the turnover of misfolded or denatured proteins. In cancers, the client proteins of HSP90 extend to the entire process of oncogenesis that are associated with all hallmarks of cancer. Accumulating evidence has demonstrated that the client proteins are guided for proteasomal degradation when their complexes with HSP90 are disrupted.
View Article and Find Full Text PDFPurpose: To investigate the antitumor activity of a mitochondrial-localized HSP90 inhibitor, Gamitrinib, in multiple glioma models, and to elucidate the antitumor mechanisms of Gamitrinib in gliomas.
Experimental Design: A broad panel of primary and temozolomide (TMZ)-resistant human glioma cell lines were screened by cell viability assays, flow cytometry, and crystal violet assays to investigate the therapeutic efficacy of Gamitrinib. Seahorse assays were used to measure the mitochondrial respiration of glioma cells.
Article Synopsis
- Telomere maintenance during DNA replication is crucial for most advanced cancers, as it involves the activation of telomerase, which is found in 85%-90% of these tumors.
- In the remaining 10%-15% of cancers, an alternative method called ALT helps maintain telomeres through DNA recombination.
- Recent research has led to promising drugs, like 6-thio-dG, that specifically target telomerase-positive cancers and may offer new treatment options, especially for therapy-resistant types.