[HTML][HTML] The multifaceted nature of αB-crystallin
J Hayashi, JA Carver - Cell Stress and Chaperones, 2020 - Elsevier
In vivo, small heat-shock proteins (sHsps) are key players in maintaining a healthy
proteome. αB-crystallin (αB-c) or HspB5 is one of the most widespread and populous of the
ten human sHsps. Intracellularly, αB-c acts via its molecular chaperone action as the first line
of defence in preventing target protein unfolding and aggregation under conditions of
cellular stress. In this review, we explore how the structure of αB-c confers its function and
interactions within its oligomeric self, with other sHsps, and with aggregation-prone target …
proteome. αB-crystallin (αB-c) or HspB5 is one of the most widespread and populous of the
ten human sHsps. Intracellularly, αB-c acts via its molecular chaperone action as the first line
of defence in preventing target protein unfolding and aggregation under conditions of
cellular stress. In this review, we explore how the structure of αB-c confers its function and
interactions within its oligomeric self, with other sHsps, and with aggregation-prone target …
