High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70 1 1Edited by P. E. Wright
- 1 June 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 289 (5) , 1387-1403
- https://doi.org/10.1006/jmbi.1999.2776
Abstract
No abstract availableKeywords
This publication has 61 references indexed in Scilit:
- Mutations in the substrate binding domain of the Escherichia coli 70 kda molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling 1 1Edited by M. GottesmanJournal of Molecular Biology, 1999
- Kinetic Evidence for Peptide-Induced Oligomerization of the Molecular Chaperone DnaK at Heat Shock TemperaturesBiochemistry, 1997
- Functional Interaction of the Auxilin J Domain with the Nucleotide- and Substrate-binding Modules of Hsc70Journal of Biological Chemistry, 1997
- The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system 1 1Edited by J.KarnJournal of Molecular Biology, 1997
- Chaperone-assisted protein foldingCurrent Opinion in Structural Biology, 1997
- Solution small-angle x-ray scattering study of the molecular chaperone Hsc70 and its subfragmentsBiochemistry, 1995
- Specificity of DnaK-peptide BindingJournal of Molecular Biology, 1994
- A triple-resonance pulse scheme for selectively correlating amide1HN and15N nuclei with the1Hα proton of the preceding residueJournal of Biomolecular NMR, 1992
- A proton-detected heteronuclear chemical-shift correlation experiment with improved resolution and sensitivityJournal of Magnetic Resonance (1969), 1990
- Accounting for spin diffusion in the analysis of 2D NOE dataJournal of Magnetic Resonance (1969), 1986