Results 271 to 280 of about 16,557,675 (399)
Pharmacologic ascorbate (vitamin C) increases ROS, disrupts cellular metabolism, and induces DNA damage in CRPC cells. These effects sensitize tumors to PARP inhibition, producing synergistic growth suppression with olaparib in vitro and significantly delayed tumor progression in vivo. Pyruvate rescue confirms ROS‐dependent activity.
Nicolas Gordon +13 more
wiley +1 more source
Exploring the interplay of electron density distribution and electrostatic potential in the interaction of nilutamide and flutamide with androgen receptors using quantum crystallography. [PDF]
Balasubramanian H +4 more
europepmc +1 more source
A Landscape of Pharmacogenomic Interactions in Cancer
F. Iorio +38 more
semanticscholar +1 more source
LDAcoop: Integrating non‐linear population dynamics into the analysis of clonogenic growth in vitro
Limiting dilution assays (LDAs) quantify clonogenic growth by seeding serial dilutions of cells and scoring wells for colony formation. The fraction of negative wells is plotted against cells seeded and analyzed using the non‐linear modeling of LDAcoop.
Nikko Brix +13 more
wiley +1 more source
Protein-Protein Interactions Modulate a Key Branch Point in Monoterpene Indole Alkaloid Biosynthesis. [PDF]
Carr SC +5 more
europepmc +1 more source
Plecstatin inhibits hepatocellular carcinoma tumorigenesis and invasion through cytolinker plectin
The ruthenium‐based metallodrug plecstatin exerts its anticancer effect in hepatocellular carcinoma (HCC) primarily through selective targeting of plectin. By disrupting plectin‐mediated cytoskeletal organization, plecstatin inhibits anchorage‐dependent growth, cell polarization, and tumor cell dissemination.
Zuzana Outla +10 more
wiley +1 more source
A kinetic model for SCR coated particulate filters—Effect of ammonia-soot interactions
Lidija V. Trandafilović +5 more
openalex +2 more sources
Genome-Wide Mapping of in Vivo Protein-DNA Interactions
David S. Johnson +3 more
semanticscholar +1 more source
We show that the majority of the 18 analyzed recurrent cancer‐associated ERBB4 mutations are transforming. The most potent mutations are activating, co‐operate with other ERBB receptors, and are sensitive to pan‐ERBB inhibitors. Activating ERBB4 mutations also promote therapy resistance in EGFR‐mutant lung cancer.
Veera K. Ojala +15 more
wiley +1 more source

