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Watanabe et al., 2009 - Google Patents

Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity

Watanabe et al., 2009

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Document ID
1023657396539037316
Author
Watanabe Y
Nakazaki Y
Suno R
Yoshida M
Publication year
Publication venue
Biochemical Journal

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Snippet

The ClpB chaperone forms a hexamer ring and rescues aggregated proteins in co-operation with the DnaK system. Each subunit of ClpB has two nucleotide-binding modules, AAA (ATPase associated with various cellular activities)-1 and AAA-2, and an 85-Å (1 Å= 0.1 nm) …
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