Here’s the hook: Similar substrate binding sites in the chaperone domains of Clp and Lon
- 20 July 1999
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 96 (15) , 8318-8320
- https://doi.org/10.1073/pnas.96.15.8318
Abstract
No abstract availableThis publication has 35 references indexed in Scilit:
- Recognition, Targeting, and Hydrolysis of the λ O Replication Protein by the ClpP/ClpX ProteaseJournal of Biological Chemistry, 1999
- ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway.Genes & Development, 1997
- The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasomeNature Structural & Molecular Biology, 1997
- Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ DomainsScience, 1997
- Six‐fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP‐dependent activator, ClpYFEBS Letters, 1996
- ATP-dependent Degradation of CcdA by Lon ProteaseJournal of Biological Chemistry, 1996
- Peptide–Surface Association: The Case of PDZ and PTB DomainsCell, 1996
- Disassembly of the Mu transposase tetramer by the ClpX chaperone.Genes & Development, 1995
- Homology in Structural Organization BetweenE. coliClpAP Protease and the Eukaryotic 26 S ProteasomeJournal of Molecular Biology, 1995
- The N-End Rule in BacteriaScience, 1991