Heat shock proteins (HSPs) are a large family of chaperones that are involved in protein
folding and maturation of a variety of “client” proteins protecting them from degradation …

The 70-kDa heat shock proteins (HSP70s) are abundantly present in cancer, providing
malignant cells selective advantage by suppressing multiple apoptotic pathways, regulating …

Various artificial transmembrane transporters, designed to function through mobile carrier or
channel mechanisms, have been developed in the past decade. With the aid of structural …

Hydrophobic tagging (HyT) is a potential therapeutic strategy for targeted protein
degradation (TPD). Norbornene was discovered as an unprecedented hydrophobic tag in …

The 70-kDa heat shock protein (HSP70) family of molecular chaperones represents one of
the most ubiquitous classes of chaperones and is highly conserved in all organisms …

Small-molecule chemical probes or tools have become progressively more important in
recent years as valuable reagents to investigate fundamental biological mechanisms and …

In all organisms, heat-shock proteins (HSPs) provide an ancient defense system. These
proteins act as molecular chaperones by assisting proper folding and refolding of misfolded …

Among the heat shock proteins (HSP), HSP27, HSP70 and HSP90 are the most studied
stress-inducible HSPs, and are induced in response to a wide variety of physiological and …

Perturbations in cellular chloride concentrations can affect cellular pH and autophagy and
lead to the onset of apoptosis. With this in mind, synthetic ion transporters have been used to …

Heat shock protein 70 (Hsp70a) is a molecular chaperone that is expressed in response to
stress. In this role, Hsp70 binds to its protein substrates and stabilize them against …