21 research outputs found
Standard (S2S) versus iterative-2 (IT2S) stage population analysis of daunorubicin (D1) and daunorubicinol (D2) pharmacokinetics
0info:eu-repo/semantics/publishe
Use of plasma cytotoxic activity to model cytotoxic pharmacodynamics of anticancer drugs.
0info:eu-repo/semantics/publishe
Co-modelling of daunorubicin (D1) and daunorubicinol (D2) plasma pharmacokinetics (PKs) and pharmacodynamics (PDs)
0info:eu-repo/semantics/publishe
Co-modelling of daunorubicin and daunorubicinol pharmacokinetics
0info:eu-repo/semantics/publishe
Daunorubicin (DNR) plasma pharmacokinetics (PKs) and pharmacodynamics (PDs)
0info:eu-repo/semantics/publishe
Plasmacidal activity (PCA) in plasma of acute myelocytic leukemia (AML) patients (pts) receiving daunorubicin (DNR)
0info:eu-repo/semantics/publishe
Heat shock protein 90 inhibition: rationale and clinical potential
Heat shock protein 90 (HSP90) is a molecular chaperone protein essential for cellular survival. Functionally, HSPs promote proper protein folding, prevent misfolding, and restore three-dimensional protein structure which is critical following toxic cellular stresses. Recently, targeting HSP90 pharmacologically has gained traction in cancer therapy. Oncogenic cells depend on their ability to withstand endogenous (anoxia, nutrient deprivation, pH changes, and deranged signaling pathways) and exogenous (chemotherapy and radiation therapy) stressors for survival. Pharmacological inhibition of HSP90 destabilizes proteins and leads to degradation through the proteasome. This article will review the utility of HSP90 inhibition, as well as the current adoption in clinical trials and practice