Publications by authors named "Terin D'Amico"
Article Synopsis
- Cruentaren A is a natural compound known for its strong ability to inhibit cancer cell growth, but the exact site where it binds to ATP synthase was previously unclear, hindering the creation of better analogues for cancer treatment.* -
- The researchers used cryogenic electron microscopy (cryoEM) to reveal the structure of cruentaren A bound to ATP synthase, which facilitated the design of new inhibitors by modifying the original compound.* -
- Some derivatives of cruentaren A, including a trans-alkene isomer, showed similar or improved cancer-fighting activity, paving the way for more effective therapies against cancer.*
The 90 kDa heat shock protein (Hsp90) belongs to a group of molecular chaperones that regulate homeostasis via the folding of nascent polypeptides into their biologically active proteins, many of which are involved in cancer development and progression. As a result, inhibition of Hsp90 is an exciting area of research for the treatment of cancer. However, most of the 18 Hsp90 N-terminal inhibitors evaluated in clinical trials exhibited deleterious side effects and toxicities.
View Article and Find Full Text PDFFF ATP synthase is responsible for the production of >95% of all ATP synthesis within the cell. Dysregulation of its expression, activity or localization is linked to various human diseases including cancer, diabetes, and Alzheimer's and Parkinson's disease. In addition, ATP synthase is a novel and viable drug target for the development of antimicrobials as evidenced by bedaquiline, which was approved in 2012 for the treatment of tuberculosis.
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