[HTML][HTML] The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular …
E Basha, GJ Lee, LA Breci, AC Hausrath… - Journal of Biological …, 2004 - ASBMB
The small heat shock proteins (sHSPs) are a ubiquitous class of ATP-independent
chaperones believed to prevent irreversible protein aggregation and to facilitate subsequent
protein renaturation in cooperation with ATP-dependent chaperones. Although sHSP
chaperone activity has been studied extensively in vitro, understanding the mechanism of
sHSP function requires identification of proteins that are sHSP substrates in vivo. We have
used both immunoprecipitation and affinity chromatography to recover 42 proteins that …
chaperones believed to prevent irreversible protein aggregation and to facilitate subsequent
protein renaturation in cooperation with ATP-dependent chaperones. Although sHSP
chaperone activity has been studied extensively in vitro, understanding the mechanism of
sHSP function requires identification of proteins that are sHSP substrates in vivo. We have
used both immunoprecipitation and affinity chromatography to recover 42 proteins that …