Hsp105 but not Hsp70 family proteins suppress the aggregation of heat‐denatured protein in the presence of ADP
Open Access
- 19 November 2003
- journal article
- Published by Wiley in FEBS Letters
- Vol. 555 (2) , 390-396
- https://doi.org/10.1016/s0014-5793(03)01292-4
Abstract
Hsp105α and Hsp105β are mammalian members of the Hsp105/110 family, a diverged subgroup of the Hsp70 family. Here, we show that Hsp105α and Hsp105β bind non‐native protein through the β‐sheet domain ...Keywords
This publication has 26 references indexed in Scilit:
- Protein kinase CK2 phosphorylates Hsp105alpha at Ser509 and modulates its functionBiochemical Journal, 2003
- Modulation of the Chaperone Activities of Hsc70/Hsp40 by Hsp105α and Hsp105βBiochemical and Biophysical Research Communications, 2000
- Phosphorylation of the 105-kDa Heat Shock Proteins, HSP105α and HSP105β, by Casein Kinase IIBiochemical and Biophysical Research Communications, 2000
- Association of HSP105 with HSC70 in High Molecular Mass Complexes in Mouse FM3A CellsBiochemical and Biophysical Research Communications, 1998
- Cloning and Expression of Murine High Molecular Mass Heat Shock Proteins, HSP105Journal of Biological Chemistry, 1995
- The Role of ATP in the Functional Cycle of the DnaK Chaperone SystemJournal of Molecular Biology, 1995
- The Peptide-Binding Domain of the Chaperone Protein Hsc70 Has an Unusual Secondary Structure TopologyBiochemistry, 1995
- Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate proteinNature, 1990
- HeLa cells synthesize a specific heat shock protein upon exposure to heat shock at 42°C but not at 45°CBiochemical and Biophysical Research Communications, 1986
- In Vivo Phosphorus-31 Nuclear Magnetic Resonance Reveals Lowered ATP During Heat Shock of TetrahymenaScience, 1983