Interactions of GroEL/GroES with a Heterodimeric Intermediate during α2β2 Assembly of Mitochondrial Branched-chain α-Ketoacid Dehydrogenase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference43 articles.
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5. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
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1. Selected reaction monitoring as an effective method for reliable quantification of disease‐associated proteins in maple syrup urine disease;Molecular Genetics & Genomic Medicine;2014-06-04
2. Chaperonins induce an amyloid-like transformation of ovine prion protein: The fundamental difference in action between eukaryotic TRiC and bacterial GroEL;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2011-12
3. GroEL-Assisted Protein Folding: Does It Occur Within the Chaperonin Inner Cavity?;International Journal of Molecular Sciences;2009-05-12
4. The 69 kDaEscherichia colimaltodextrin glucosidase does not get encapsulated underneath GroES and folds throughtransmechanism during GroEL/ GroES‐assisted folding;The FASEB Journal;2007-05-10
5. An Expanded Conformation of Single-Ring GroEL-GroES Complex Encapsulates an 86 kDa Substrate;Structure;2006-11
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