The past decades have witnessed hyperthermia therapy (HTT) as an emerging strategy
against malignant tumors. Nanomaterial‐based photothermal therapy (PTT) and magnetic …

BACKGROUND Proteins are synthesized on ribosomes as linear chains of amino acids and
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …

Heat shock proteins 90 (Hsp90) and 70 (Hsp70) are two families of highly conserved ATP-
dependent molecular chaperones that fold and remodel proteins. Both are important …

Conserved families of molecular chaperones assist protein folding in the cell. Here we
review the conceptual advances on three major folding routes:(i) spontaneous, chaperone …

Heat‐shock proteins (Hsps) and their cognates are primary mitigators of cell stress. With
increasingly severe impacts of climate change and other human modifications of the …

Recent studies have revealed that a mild increase in environmental temperature stimulates
the growth of Arabidopsis seedlings by promoting biosynthesis of the plant hormone auxin …

Hsp70 chaperone machineries have pivotal roles in an array of fundamental biological
processes through their facilitation of protein folding, disaggregation, and remodeling. The …

Protein folding in the cell requires ATP-driven chaperone machines such as the conserved
Hsp70 and Hsp90. It is enigmatic how these machines fold proteins. Here, we show that …

Heat shock proteins (HSPs) are a kind of proteins which mostly found in bacterial, plant and
animal cells, in which they are involved in the monitoring and regulation of cellular life …

The HSP90 molecular chaperone is involved in the activation and cellular stabilization of a
range of 'client'proteins, of which oncogenic protein kinases and nuclear steroid hormone …