The N Terminus of the Head Protein of T4 Bacteriophage Directs Proteins to the GroEL Chaperonin
- 14 January 2005
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 345 (2), 375-386
- https://doi.org/10.1016/j.jmb.2004.10.052
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0Å ResolutionJournal of Molecular Biology, 2003
- Review: Cellular Substrates of the Eukaryotic Chaperonin TRiC/CCTJournal of Structural Biology, 2001
- Identification of in vivo substrates of the chaperonin GroELNature, 1999
- Trigger factor and DnaK cooperate in folding of newly synthesized proteinsNature, 1999
- Polypeptide Flux through Bacterial Hsp70Cell, 1999
- STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDINGAnnual Review of Biochemistry, 1998
- The Hsp70 and Hsp60 Chaperone MachinesCell, 1998
- The crystal structure of the GroES co-chaperonin at 2.8 Å resolutionNature, 1996
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- A cytoplasmic chaperonin that catalyzes β-actin foldingCell, 1992