Partial Occlusion of Both Cavities of the Eukaryotic Chaperonin with Antibody Has No Effect upon the Rates of β-Actin or α-Tubulin Folding
Open Access
- 1 February 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (7) , 4587-4591
- https://doi.org/10.1074/jbc.275.7.4587
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin.Nature Structural & Molecular Biology, 1999
- Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCTPublished by Elsevier ,1998
- Structure of the Substrate Binding Domain of the Thermosome, an Archaeal Group II ChaperoninCell, 1997
- The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complexNature, 1997
- A variant to the “random approximation” of the reference-free alignment algorithmUltramicroscopy, 1996
- Pathway Leading to Correctly Folded β-TubulinCell, 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
- The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.Proceedings of the National Academy of Sciences, 1993