Chaperone (protein)
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- Groel-Assisted Protein Folding: Groes Binding-Induced Displacement of Denatured Proteins from Groel to Bulk Solution
- Post-Translational Modification Networks of Contractile and Cellular Stress Response Proteins in Bladder Ischemia
- Integrative Genetic, Genomic and Transcriptomic Analysis of Heat Shock Protein and Nuclear Hormone Receptor Gene Associations with Spontaneous Preterm Birth Johanna M
- Role of the HSP70 Co-Chaperone SIL1 in Health and Disease
- Crystal Structure of the Human Mitochondrial Chaperonin Symmetrical Football Complex
- Mitochondrial Hsp90 Is a Ligand-Activated Molecular Chaperone Coupling ATP Binding to Dimer Closure Through a Coiled-Coil Intermediate
- Measuring How Much Work the Chaperone Groel Can Do
- Co-Translational Protein Folding and Sorting in Chloroplasts
- Chaperone-Dependent E3 Ubiquitin Ligase CHIP Mediates a Degradative Pathway for C-Erbb2͞neu
- Ubiquitin-Like Protein Conjugation and the Ubiquitin–Proteasome System As Drug Targets
- Molecular Chaperone Groel/ES: Unfolding and Refolding Processes
- Effects of Post-Translational Modification On
- The Hsp60 Protein of Helicobacter Pylori Exhibits Chaperone and Atpase Activities at Elevated Temperatures
- The Role of Molecular Chaperones in Virus Infection and Implications for Understanding and Treating COVID-19
- Inhibition of Heat Shock Proteins HSP90 and HSP70 Induce
- Understanding Groel and Dnak Stress Response Proteins As Antigens for Bacterial Diseases
- Post-Translational Modifications of Hsp90 and Their
- HSPA1L Enhances Cancer Stem Cell-Like Properties by Activating Igf1rβ and Regulating Β-Catenin Transcription