DisagMech1 JBC2
نویسندگان
چکیده
Background: A novel chaperone, cpSRP43, recognizes and disassembles the aggregates formed by its client proteins. Results: The client proteins of cpSRP43 form stable disc-shaped aggregates with the chaperone recognition motif displayed on the surface. Conclusion: The surface-exposed motif on the aggregate allows it to be recognized by its chaperone. Significance: Understanding the structure and energetics of protein aggregates provides insights into the mechanism of their disassembly.
منابع مشابه
Dange et al., JBC2
1) From the Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA 2) Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 10115, USA 3) present address: Kavli Institute of NanoScience, Department of BioNanoScience, Technical University Delft, Lorentzweg , 2628 CJ Delft, The Netherlands 4) present address: De...
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تاریخ انتشار 2013