The Structure of ClpB A Molecular Chaperone that Rescues Proteins from an Aggregated State

Abstract

Molecular chaperones assist protein folding by facilitating their "forward" folding and preventing aggregation. However, once aggregates have formed, these chaperones cannot facilitate protein disaggregation. Bacterial ClpB and its eukaryotic homolog Hsp104 are essential proteins of the heat-shock response, which have the remarkable capacity to rescue… (More)
DOI: 10.1016/S0092-8674(03)00807-9

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@article{Lee2003TheSO, title={The Structure of ClpB A Molecular Chaperone that Rescues Proteins from an Aggregated State}, author={Sukyeong Lee and Mathew E. Sowa and Yo-hei Watanabe and Paul B. Sigler and Wah Chiu and Masasuke Yoshida and Francis T. F. Tsai}, journal={Cell}, year={2003}, volume={115}, pages={229-240} }