The chaperonin TRiC is blocked by native and glycated prion protein
Author:
Funder
Russian Science Foundation
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference25 articles.
1. Functional profiling of asymmetrically-organized human CCT/TRiC chaperonin;Araki;Biochem. Biophys. Res. Commun.,2016
2. Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains;Kim;Trends Biochem. Sci.,1994
3. Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis;Meyer;Cell,2003
4. The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin;Llorca;EMBO J.,2001
5. Chaperonin TRiC assists the refolding of sperm-specific glyceraldehyde-3-phosphate dehydrogenase;Naletova;Arch. Biochem. Biophys.,2011
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1. Cryo-EM structure of bovine chaperonin TRiC/CCT in open conformation;Vestnik Moskovskogo universiteta. Seria 16. Biologia;2023-12-21
2. Are Gastrointestinal Microorganisms Involved in the Onset and Development of Amyloid Neurodegenerative Diseases?;Microbiology Research;2023-11-20
3. Contribution of Extracellular Vesicles and Molecular Chaperones in Age-Related Neurodegenerative Disorders of the CNS;International Journal of Molecular Sciences;2023-01-04
4. Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases;International Journal of Molecular Sciences;2022-03-02
5. Functional genomics screen identifies proteostasis targets that modulate prion protein (PrP) stability;Cell Stress and Chaperones;2021-02-05
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