In the past few decades, the development of heat shock protein 90 (Hsp90) inhibitors for
cancer treatment has not stopped. About twenty compounds have been evaluated in the …

Abstract The 90-kiloDalton (kD) heat shock protein (Hsp90) is a ubiquitous, ATP-dependent
molecular chaperone whose primary function is to ensure the proper folding of several …

Tumor hypoxia is a common feature in most solid tumors and is associated with
overexpression of the hypoxia response pathway. Overexpression of the hypoxia‐inducible …

HSP90 is a member of the family of heat shock proteins responsible for folding proteins into
mature conformations and thus maintaining their biological function in cells. Since it is …

The review summarizes recent advances in the synthesis of C2‐halogenated nitrogen
heterocycles via nucleophilic halogenation of corresponding N‐oxides as well as …

A pharmacophore-hybridized strategy based on previously reported HSP90 C-terminal
inhibitors was utilized to prepare 32 aryl/penta-1, 4-dien-3-one/amine hybrids. Among them …

Ocular diseases featuring pathologic neovascularization are the leading cause of blindness,
and anti-VEGF agents have been conventionally used to treat these diseases. Recently …

Despite the development of advanced therapeutic regimens such as molecular targeted
therapy and immunotherapy, the 5-year survival of patients with lung cancer is still less than …

A series of O-substituted analogs of the C-ring-truncated scaffold of deguelin designed as
heat shock protein 90 (HSP90) C-terminal inhibitors were investigated as novel antitumor …

Heat shock proteins are essential molecular chaperones that play crucial roles in stabilizing
protein structures, facilitating the repair or degradation of damaged proteins, and …