Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain
- 1 March 1997
- Vol. 5 (3) , 403-414
- https://doi.org/10.1016/s0969-2126(97)00197-4
Abstract
No abstract availableKeywords
This publication has 54 references indexed in Scilit:
- The role of molecular chaperones in protein folding.The FASEB Journal, 1995
- Structure and regulation of the mouse GRP78 (BiP) promoter by glucose and calcium ionophoreGene, 1995
- How Potassium Affects the Activity of the Molecular Chaperone Hsc70Journal of Biological Chemistry, 1995
- Role of cytosolic Ca2+ and protein kinases in the induction of the hsp70 geneKidney International, 1994
- Regulation of hsp70 Synthesis Induced by Cupric Sulfate and Zinc Sulfate in Thermotolerant HeLa CellsThe Journal of Biochemistry, 1993
- The translation machinery and 70 kd heat shock protein cooperate in protein synthesisCell, 1992
- Protein folding in the cellNature, 1992
- Calcium ionophore A23187 as a regulator of gene expression in mammalian cells.The Journal of cell biology, 1986
- The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system.Proceedings of the National Academy of Sciences, 1983
- The dnaK protein modulates the heat-shock response of Escherichia coliCell, 1983