Cargando…
Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics
Heat shock protein 90 (HSP90) inhibition is an attractive strategy for cancer treatment. Several HSP90 inhibitors have shown promising effects in clinical oncology trials. However, little is known about HSP90 inhibition-mediated bladder cancer therapy. Here, we report a quantitative proteomic study...
Autores principales: | Li, Qingdi Quentin, Hao, Jian-Jiang, Zhang, Zheng, Krane, L. Spencer, Hammerich, Kai H., Sanford, Thomas, Trepel, Jane B., Neckers, Len, Agarwal, Piyush K. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5427839/ https://www.ncbi.nlm.nih.gov/pubmed/28298630 http://dx.doi.org/10.1038/s41598-017-00143-6 |
Ejemplares similares
-
Histone deacetylase inhibitor-induced cell death in bladder cancer is associated with chromatin modification and modifying protein expression: A proteomic approach
por: LI, QINGDI QUENTIN, et al.
Publicado: (2016) -
Targeting Heat Shock Protein 90 for the Treatment of Malignant Pheochromocytoma
por: Giubellino, Alessio, et al.
Publicado: (2013) -
Post-translational modification and conformational state of Heat Shock Protein 90 differentially affect binding of chemically diverse small molecule inhibitors
por: Beebe, Kristin, et al.
Publicado: (2013) -
Casein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity
por: Mollapour, Mehdi, et al.
Publicado: (2011) -
Posttranslational modification and beyond: interplay between histone deacetylase 6 and heat-shock protein 90
por: Liu, Ping, et al.
Publicado: (2021)