Watanabe et al., 2009 - Google Patents
Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activityWatanabe et al., 2009
View PDF- Document ID
- 1023657396539037316
- Author
- Watanabe Y
- Nakazaki Y
- Suno R
- Yoshida M
- Publication year
- Publication venue
- Biochemical Journal
External Links
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) …
- 101700014488 CLPB 0 title abstract description 127
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- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4702—Regulators; Modulating activity
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- C12N9/104—Aminoacyltransferases (2.3.2)
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