GroEL/GroES-dependent Reconstitution of α2β2 Tetramers of Human Mitochondrial Branched Chain α-Ketoacid Decarboxylase
Open Access
- 1 April 1999
- journal article
- Published by Elsevier BV
- Vol. 274 (15), 10395-10404
- https://doi.org/10.1074/jbc.274.15.10395
Abstract
No abstract availableThis publication has 39 references indexed in Scilit:
- The Hsp70 and Hsp60 Chaperone MachinesCell, 1998
- The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complexNature, 1997
- Molecular chaperones in cellular protein foldingNature, 1996
- Structure of the Heat Shock Protein Chaperonin-10 of Mycobacterium lepraeScience, 1996
- The crystal structure of the GroES co-chaperonin at 2.8 Å resolutionNature, 1996
- Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groesCell, 1995
- Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domainsTrends in Biochemical Sciences, 1994
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- Symmetric Complexes of GroE Chaperonins as Part of the Functional CycleScience, 1994
- MOLECULAR CHAPERONESAnnual Review of Biochemistry, 1991