Heat shock proteins (HSPs) are a large group of chaperones found in most eukaryotes and
bacteria. They are responsible for the correct protein folding, protection of the cell against …

Stress proteins (SPs) including heat-shock proteins (HSPs), RNA chaperones, and ER
associated stress proteins are molecular chaperones essential for cellular homeostasis. The …

Antibodies targeting receptor-mediated entry of HCV into hepatocytes confer limited
therapeutic benefits. Evidence suggests that exosomes can transfer genetic materials …

Hsp90 is a dimeric molecular chaperone required for the activation and stabilization of
numerous client proteins many of which are involved in essential cellular processes like …

Exciting progress has recently been made in understanding the replication of hepatitis C
virus, a major cause of chronic hepatitis, liver cirrhosis and hepatocellular carcinoma …

Abstract Positive-sense RNA ((+) RNA) viruses such as hepatitis C virus exploit host cells by
subverting host proteins, remodelling subcellular membranes, co-opting and modulating …

Heat shock proteins (HSPs) are constitutively expressed under physiological conditions in
most organisms but their expression can significantly enhance in response to four types of …

(–)-Epigallocatechin-3-O-gallate (EGCG), the most abundant component of catechins in tea
(Camellia sinensis (L.) O. Kuntze), plays a role against viruses through inhibiting virus …

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 …

Viruses are intracellular pathogens responsible for a vast number of human diseases. Due
to their small genome size, viruses rely primarily on the biosynthetic apparatus of the host for …