Pathways & interactions
Literature: Clp ATPase, C-terminal (IPR019489)
References used in this entry
The following publications were referred to in the abstract:
The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state.
Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT.
Cell 115 229-40 2003
PMID: 14567920 Related citations
A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases.
Mol. Microbiol. 61 1094-100 2006
PMID: 16879409 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects.
Wang J, Rho SH, Park HH, Eom SH.
Acta Crystallogr. D Biol. Crystallogr. 61 932-41 2005
PMID: 15983416 Related citations
Crystal structure of ClpX molecular chaperone from Helicobacter pylori.
Kim DY, Kim KK.
J. Biol. Chem. 278 50664-70 2003
PMID: 14514695 Related citations
Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone.
Xia D, Esser L, Singh SK, Guo F, Maurizi MR.
J. Struct. Biol. 146 166-79 2004
PMID: 15037248 Related citations
Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome.
Kwon AR, Kessler BM, Overkleeft HS, McKay DB.
J. Mol. Biol. 330 185-95 2003
PMID: 12823960 Related citations