TRiC/CCT chaperonins are essential for maintaining myofibril organization, cardiac physiological rhythm, and lifespan
Author:
Affiliation:
1. Department of Biology, Molecular Biology and Heart Institutes; San Diego State University; CA USA
2. Development, Aging and Regeneration Program; Sanford Burnham Prebys Medical Discovery Institute; La Jolla CA USA
Funder
National Institutes of Health
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Reference41 articles.
1. Review: cellular substrates of the eukaryotic chaperonin TRiC/CCT;Dunn;J Struct Biol,2001
2. Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies;Yam;Nat Struct Mol Biol,2008
3. Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCT;Russmann;Proc Natl Acad Sci USA,2012
4. The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT;Joachimiak;Cell,2014
5. Interactions of subunit CCT3 in the yeast chaperonin CCT/TRiC with Q/N-rich proteins revealed by high-throughput microscopy analysis;Nadler-Holly;Proc Natl Acad Sci USA,2012
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