Historical Background
In the cell, the correct folding of many proteins depends on the function of preexisting ones known as molecular chaperones (for a review see Hartl and Hayer-Hartl 2009). These, were defined as proteins that bind to and stabilize an otherwise unstable conformation of another protein, and by controlling binding and release, facilitate its correct fate in vivo, be it folding, oligomeric assembly, transport to a particular subcellular compartment, or disposal by degradation. Molecular chaperones do not convey steric information specifying correct folding: instead, they prevent incorrect interactions within and between nonnative peptides, thus typically increasing the yield but not the rate of folding reactions.
Molecular chaperones are ubiquitous and comprise several protein families that are structurally unrelated (Hartl and Hayer-Hartl 2009). The Hsp70s and the Chaperonin families have been extensively studied. Hsp70homologs are widespread in...
Keywords
- Apical Domain
- Bardet Biedl Syndrome
- Transmission Ratio Distortion
- polyQ Expansion Protein
- Bardet Biedl Syndrome Gene
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References
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Nolasco, S., Gonçalves, J., Soares, H. (2016). CCTα. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6438-9_550-1
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DOI: https://doi.org/10.1007/978-1-4614-6438-9_550-1
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