Clp ATPases and their role in protein unfolding and degradation
- 1 January 2001
- book chapter
- Published by Elsevier in Advances in Protein Chemistry
- Vol. 59, 413-429
- https://doi.org/10.1016/s0065-3233(01)59013-0
Abstract
No abstract availableKeywords
This publication has 83 references indexed in Scilit:
- Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coliJournal of Molecular Biology, 2000
- Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpBThe EMBO Journal, 1999
- The solution structure of VAT-N reveals a ‘missing link’ in the evolution of complex enzymes from a simple βαββ elementCurrent Biology, 1999
- Recognition, Targeting, and Hydrolysis of the λ O Replication Protein by the ClpP/ClpX ProteaseJournal of Biological Chemistry, 1999
- Communication of ClpXP protease hypersensitivity to bacteriophage mu repressor isoformsJournal of Molecular Biology, 1997
- Structure of 20S proteasome from yeast at 2.4Å resolutionNature, 1997
- Six‐fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP‐dependent activator, ClpYFEBS Letters, 1996
- Homology in Structural Organization BetweenE. coliClpAP Protease and the Eukaryotic 26 S ProteasomeJournal of Molecular Biology, 1995
- Molecular Chaperones: Resurrection or destruction?Current Biology, 1995
- Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivationCurrent Biology, 1995