Protein folding in the cell
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Summary
Folding and assembly of polypeptides in vivo involves other proteins, many of which belong to families that have been highly conserved during evolution.
- Type
- review
- Published
- 1992-01-02
- Cited by
- 4,083
- References
- 190
- OpenAlex
- https://openalex.org/W2051793369
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:4330003
Keywords
Protein folding, In vitro, Folding (DSP implementation), Sequence (biology), Macromolecule
References
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- Biochemical characterization of the 94- and 78-kilodalton glucose-regulated proteins in hamster fibroblasts.
- Localization of the 90-kDa heat shock protein-binding site within the hormone-binding domain of the glucocorticoid receptor by peptide competition.
- Heavy chain-producing variants of a mouse myeloma cell line.
- Catalysis of protein folding by cyclophilins from different species.
Cited by
- The use of stress proteins in Mytilus edulis as indicators of chlorinated effluent pollution
- Disulphide bridge formation in the periplasm of Escherichia coli: β‐lactamase::human lgG3 hinge fusions as a model system
- Rat liver BiP/GRP78 is down‐regulated by a peroxisome‐proliferator, clofibrate
- Models of Alzheimer's disease: cellular and molecular aspects.
- Effect of nitrate on human cell lines in culture
- Molecular chaperones and cancer immunotherapy.
- Physiological characterization of Ashbya gossypii and strain development for recombinant protein production
- Chaperoning a pathogen
- Soluble constituents of the ER lumen are required for GPI anchoring of a model protein.
- Plant Storage Proteins
- ELEVATION OF GRP‐78 AND LOSS OF HSP‐70 FOLLOWING PHOTODYNAMIC TREATMENT OF V79 CELLS: SENSITIZATION BY NIGERICIN
- Hsp70: anti-apoptotic and tumorigenic protein.
- Defective protein folding as a cause of disease
- Eukaryotic translation elongation factor 1γ contains a glutathione transferase domain—Study of a diverse, ancient protein super family using motif search and structural modeling
- The cellular response to unfolded proteins: intercompartmental signaling.
- Effect of Nucleotide on the Binding of Peptides to 70-kDa Heat Shock Protein (*)
- The molecular chaperone TF55
- Enhancing CHO cell productivity through the stable depletion of microRNA-23
- Protein folding and the regulation of signaling pathways.
- Heterogeneities in ferritin dimers as characterized by gel filtration, nuclear magnetic resonance, electrophoresis, transmission electron microscopy, and gene engineering techniques.
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