Molecular chaperones in cellular protein folding
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Summary
Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.
- Type
- review
- Published
- 1996-06-13
- Cited by
- 3,515
- References
- 152
- OpenAlex
- https://openalex.org/W2119999468
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:4347271
Keywords
Chaperonin, Co-chaperone, Protein folding, Chaperone (clinical), Folding (DSP implementation)
References
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- Evolution and replication of tobacco ringspot virus satellite RNA mutants.
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- The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein.
- hsp70-protein complexes. Complex stability and conformation of bound substrate protein.
- Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding.
- The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication.
- The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj‐1 have distinct roles in recognition of a non‐native protein and protein refolding.
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- Ecological and evolutionary physiology of heat shock proteins and the stress response in Drosophila: complementary insights from genetic engineering and natural variation.
- Structures and Functions of Chaperones and Chaperonins (Review)
- Interaction of Hsp70 chaperones with substrates
- Mechanism of the Facilitation of PC2 Maturation by 7B2: Involvement in ProPC2 Transport and Activation but Not Folding
- Modular Folding and Evidence for Phosphorylation-induced Stabilization of an hsp90-dependent Kinase*
- SBA1 Encodes a Yeast Hsp90 Cochaperone That Is Homologous to Vertebrate p23 Proteins
- ATP-dependent Proteolysis in Mitochondria
- Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease.
- Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.
- Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology.
- Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB
- Role of heat shock proteins in gastric mucosal protection
- Reversible denaturation of oligomeric human chaperonin 10: Denatured state depends on chemical denaturant
- Characterization of the dnaK Multigene Family in the Cyanobacterium Synechococcus sp. Strain PCC7942
- Ligand-independent assembly of recombinant human CD1 by using oxidative refolding chromatography
- Protein quality control, retention, and degradation at the endoplasmic reticulum.
- Molecular structure of tight junctions and their role in epithelial transport.
- Trinucleotide repeats: mechanisms and pathophysiology.
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