Defining the eukaryotic cytosolic chaperonin-binding sites in human tubulins
- 17 November 2000
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 304 (1), 81-98
- https://doi.org/10.1006/jmbi.2000.4177
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Evidence That β-Tubulin Induces a Conformation Change in the Cytosolic Chaperonin Which Stabilizes Binding: Implications for the Mechanism of Action,Biochemistry, 2000
- A chaperone with a hydrophilic surface.Nature Structural & Molecular Biology, 1999
- Atomic structures of tubulin and FtsZTrends in Cell Biology, 1998
- Chaperonin-Mediated Folding in the Eukaryotic Cytosol Proceeds through Rounds of Release of Native and Nonnative FormsCell, 1997
- Newly-Synthesized β-Tubulin Demonstrates Domain-Specific Interactions with the Cytosolic ChaperoninBiochemistry, 1996
- Analysis of chaperonin‐containing TCP‐1 subunits in the human keratinocyte two‐dimensional protein database: Further characterisation of antibodies to individual subunitsElectrophoresis, 1996
- Peptide mass fingerprinting of chaperonin‐containing TCP‐1 (CCT) and copurifying proteinsThe FASEB Journal, 1996
- Antibody characterisation of two distinct conformations of the chaperonin‐containing TCP‐1 from mouse testisFEBS Letters, 1995
- Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo.Proceedings of the National Academy of Sciences of the United States of America, 1994
- A cytoplasmic chaperonin that catalyzes β-actin foldingCell, 1992