Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. [electronic resource]
Producer: 20060207Description: 41252-61 p. digitalISSN:- 0021-9258
- Adenosine Triphosphate -- chemistry
- Cell Proliferation
- Chromatography, Gel
- Chromosomes -- metabolism
- Cytosol -- metabolism
- Electrophoresis, Polyacrylamide Gel
- HSP110 Heat-Shock Proteins -- metabolism
- HSP70 Heat-Shock Proteins -- metabolism
- Hydrolysis
- Immunoprecipitation
- Kinetics
- Mass Spectrometry
- Models, Biological
- Models, Genetic
- Molecular Chaperones -- metabolism
- Molecular Weight
- Peptides -- chemistry
- Plasmids -- metabolism
- Protein Binding
- Protein Biosynthesis
- Protein Folding
- Protein Structure, Tertiary
- Saccharomyces cerevisiae -- metabolism
- Saccharomyces cerevisiae Proteins -- metabolism
- Silver Staining
- Time Factors
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Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
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