Recent cancer therapies have focused on targeting biology networks through a single
regulatory protein. Heat shock protein 90 (hsp90) is an ideal oncogenic target as it regulates …

A combination of mutasynthesis, precursor‐directed biosynthesis and semisynthesis
provides access to new ansamitocin derivatives including new nanostructured particle–drug …

Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone (90 kDa) that functions as
a dimer. This protein facilitates the folding, assembly, and stabilization of more than 400 …

The potential of “customizable units” to generate structural diversity for biological screenings
is highlighted in this proof‐of‐concept synthesis of new peptides related to the potent …

2.1 Introduction: Receptor Allosterism allosteric molecules are fundamentally different from
molecules that bind to the natural receptor binding pocket for endogenous hormones and …

Classical Hsp90 inhibitors target the N-terminal ATP binding site. While these inhibitors
have had some clinical success, treatment with these molecules leads to a dramatic …

The heat shock proteins (Hsps) are a family of highly conserved proteins involved in the
regulation of numerous cellular processes including those associated with cancer. Inhibiting …

dc. description. abstract This thesis describes C-terminal heat shock protein 90 (Hsp90)
modulators as potential anticancer agents. The McAlpine lab developed two molecules …