Small-molecule drug discovery has traditionally focused on occupancy of a binding site that
directly affects protein function, and this approach typically precludes targeting proteins that …

The accumulation of misfolded proteins in the human brain is one of the critical features of
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …

The growing knowledge about the influence of transposable elements (TE s) on (a) long‐
term genome and transcriptome evolution;(b) genomic, transcriptomic and epigenetic …

Most proteins must fold into defined three-dimensional structures to gain functional activity.
But in the cellular environment, newly synthesized proteins are at great risk of aberrant …

The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

Abstract Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that
facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched …

The molecular chaperone heat shock protein 90 (HSP90) has been used by cancer cells to
facilitate the function of numerous oncoproteins, and it can be argued that cancer cells …

Highlights•Hsp90 is a molecular chaperone that modulates the function of many client
proteins.•Morphogenesis is an important Candida albicans virulence trait.•Hsp90 regulates …

Molecular chaperones govern proteome health to support cell homeostasis. An essential
eukaryotic component of the chaperone system is Hsp90. Using a chemical-biology …

Heat shock protein 90 (Hsp90), one of the most abundant and conserved molecular
chaperones, is essential in eukaryotic cells.[1, 2] Different from other well‑known mo‑lecular …