HSP90 is a vital chaperone protein conserved across all organisms. As a chaperone protein,
it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits …

The use of drug-like macrocycles is emerging as an exciting area of medicinal chemistry,
with several recent examples highlighting the favorable changes in biological and …

Background Molecular docking methods are commonly used for predicting binding modes
and energies of ligands to proteins. For accurate complex geometry and binding energy …

In the last decade, the molecular chaperone HSP90 has emerged as an important target in
cancer therapeutics and has subsequently become the focus of several drug discovery and …

Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential
role in many cellular processes including cell cycle control, cell survival, hormone and other …

The molecular chaperone Hsp90 (90 kDa heat-shock protein) is a remarkably versatile
protein involved in the stress response and in normal homoeostatic control mechanisms. It …

The molecular chaperone Hsp90 (heat shock protein 90) is a promising target in cancer
therapy. Preclinical and clinical evaluations of a variety of Hsp90 inhibitors have shown anti …

The 90 kDa heat shock proteins (Hsp90) are responsible for the conformational maturation
of nascent polypeptides and the rematuration of denatured proteins. Proteins dependent …

There is growing interest within the pharmaceutical community to undertake biological
targets that involve protein− protein 1 and, in general, biomacromolecular interactions 2 (PPI …

Abstract Heat shock protein 90 (Hsp90) has evolved as a cancerous cell growth regulator by
stabilising various oncogenic kinases. Upon the Hsp90 inhibition, the expression of its client …