Protein folding
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- PROTEIN FOLDING in the CELL: the Role of Molecular Chaperones Hsp70 and Hsp60
- Crystal Structures of the Atpase Domains of Four Human Hsp70 Isoforms: HSPA1L/Hsp70-Hom, HSPA2/Hsp70-2, HSPA6/Hsp70b’, and HSPA5/Bip/GRP78
- Residual Structure of Unfolded Ubiquitin As Revealed by Hydrogen/Deuterium-Exchange 2D NMR
- Review of Protein Structure / Folding Post-Translational Modification
- The Nature of Protein Folding Pathways S
- An Emerging Role for the Ubiquitin-Proteasome System in the Breakdown of Transient Protein Inclusions
- SAXS and Collapse in Protein Folding
- CHIP: a Co-Chaperone for Degradation by the Proteasome
- Groel-Assisted Protein Folding: Groes Binding-Induced Displacement of Denatured Proteins from Groel to Bulk Solution
- Atomic-Level Description of Ubiquitin Folding SEE COMMENTARY
- Racemization in Post-Translational Modifications Relevance To
- University of Groningen Hsp70 Machinery Vs Protein Aggregation
- Inhibition of Immunoglobulin Folding and Secretion by Dominant
- Current Status of Endoplasmic Reticulum Stress in Type II Diabetes
- Molecular Chaperones in Cellular Protein Folding: the Birth of a Field
- Study of Protein Folding Under Native Conditions by Rapidly Switching the Hydrostatic Pressure Inside an NMR Sample Cell
- Heat Shock Proteins: Dynamic Biomolecules to Counter Plant Biotic and Abiotic Stresses
- Co-Translational Protein Folding and Sorting in Chloroplasts