Productive folding of a tethered protein in the chaperonin GroEL–GroES cage
Author:
Funder
JSPS KAKENHI
MEXT-supported Program
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
1. Reconstitution of active dimeric ribulose biphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP;Goloubinoff;Nature,1989
2. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding;Todd;Science,1994
3. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES;Weissman;Cell,1995
4. Co-translational involvement of the chaperonin GroEL in the folding of newly translated polypeptides;Ying;J. Biol. Chem.,2005
5. The crystal structure of the bacterial chaperonin GroEL at 2.8 A;Braig;Nature,1994
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1. Protein chain collapse modulation and folding stimulation by GroEL-ES;Science Advances;2022-03-04
2. Membrane Proteocomplexome of Campylobacter jejuni Using 2-D Blue Native/SDS-PAGE Combined to Bioinformatics Analysis;Frontiers in Microbiology;2020-11-19
3. Chaperonin facilitates protein folding by avoiding initial polypeptide collapse;The Journal of Biochemistry;2018-07-23
4. Folding while bound to chaperones;Current Opinion in Structural Biology;2018-02
5. Cloning and characterization of thermostable GroEL/GroES homologues from Geobacillus thermopakistaniensis and their applications in protein folding;Journal of Biotechnology;2017-07
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