Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin11Edited by W. Baumeister
- 1 January 2002
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 315 (1) , 73-85
- https://doi.org/10.1006/jmbi.2001.5220
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- Group II chaperonins: new TRiC(k)s and turns of a protein folding machineJournal of Molecular Biology, 1999
- Recurrent paralogy in the evolution of archaeal chaperoninsCurrent Biology, 1999
- STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDINGAnnual Review of Biochemistry, 1998
- Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCTPublished by Elsevier ,1998
- GroEL‐Mediated protein foldingProtein Science, 1997
- Molecular chaperones in cellular protein foldingNature, 1996
- The Chaperonin Containing t-complex polypeptide 1 (TCP-1). Multisubunit Machinery Assisting in Protein Folding and Assembly in the Eukaryotic CytosolEuropean Journal of Biochemistry, 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
- MOLECULAR CHAPERONESAnnual Review of Biochemistry, 1991