A5074831122- Heat shock proteins research
- Immunotherapy and Immune Responses
- thermodynamics and calorimetric analyses
- Ferroptosis and cancer prognosis
- Physiological and biochemical adaptations
- Endoplasmic Reticulum Stress and Disease
- Glutathione Transferases and Polymorphisms
- Circular RNAs in diseases
- Research on Leishmaniasis Studies
- interferon and immune responses
Indiana University Bloomington
2020-2023
Indiana University School of Medicine
2020-2023
The heat stress response activates the transcription factor shock 1 (HSF1), which subsequently upregulates proteins to maintain integrity of proteome. HSF1 activation requires nuclear localization, trimerization, DNA binding, phosphorylation and gene transactivation. Phosphorylation at S326 is an important regulator transcriptional activity. mediated by AKT1, mTOR, p38, MEK1 DYRK2. Here, we observed AKT1 independently mTOR. AKT2 also phosphorylated but showed weak ability activate HSF1....
Abstract Heat shock factor 1 (HSF1) is a stress-responsive transcription that promotes cancer cell malignancy. To provide better understanding of the biological processes regulated by HSF1, here we developed an HSF1 activity signature (HAS) and found it was negatively associated with antitumor immune cells in breast tumors. Knockdown decreased tumor size caused influx several cells, most notably CD8+ T cells. Depletion rescued reduction growth HSF1-deficient tumors, suggesting prevents...
Abstract Breast cancer is the leading cause of related deaths in women. The presence cytotoxic immune cells, specifically CD8+ T breast tumors associated with better patient outcomes. Our goal to understand mechanisms that regulate infiltration cells. This will turn, improve treatment and enhance overall survival. Utilizing a novel HSF1 activity gene signature, we observed was negatively cells patients. Both CIBERSORT analysis TCGA data as well direct assessment primary specimens...
Abstract The heat stress response activates the transcription factor shock 1 (HSF1), which subsequently upregulates proteins to maintain integrity of proteome. HSF1 activation requires nuclear localization, trimerization, DNA binding, phosphorylation, and gene transactivation. Phosphorylation at S326 is an important regulator transcriptional activity. mediated by AKT1, mTOR, p38, MEK1. Here, we observe that AKT1 independent mTOR. AKT2 also phosphorylated but showed weak ability activate...
Abstract Heat shock factor 1 (HSF1) is a stress-responsive transcription that promotes cancer cell malignancy. A novel HSF1 Activity Signature (HAS) was found to be negatively associated with antitumor immune cells in breast tumors. Knockdown of decreased tumor size and caused an influx several cells, most notably CD8+ T cells. Depletion prevented tumors from shrinking after knockdown HSF1, suggesting prevents avoid immune-mediated killing. also suppress expression CCL5, chemokine for...
Abstract Breast cancer is the second leading cause of cancer-related death in women. The presence cytotoxic immune cells, specifically CD8+ T breast tumors associated with better patient outcomes. Understanding mechanisms that regulate infiltration cells into could improve treatment and enhance overall survival. Utilizing a novel HSF1 activity gene signature, we observed was negatively patients. Both CIBERSORT analysis TCGA data as well direct assessment primary specimens demonstrated high...