The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding.
Open accessAbstract
Circular dichroism and HPLC gel filtration were used to show that cytosolic hsp70 is thermally stable but undergoes a conformational transition (midpoint, 43 degrees C; 57 degrees C in the presence of ATP or ADP) leading to oligomerization. hsp70 binds to unfolded, but not to folded, proteins in a temperature-dependent manner; complex formation is significant only at physiologically relevant temperatures. hsp70 binds ADP more tightly than ATP to form a binary complex, which binds to the unfolded protein more rapidly than free hsp70. ADP also inhibits the ATP-induced dissociation of the hsp70-protein complex. A regulatory role for the hsp70-nucleotide binary complexes is proposed.
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Cites
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Cited by
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Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK
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Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
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Peptide-binding specificity of the molecular chaperone BiP
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Metadata
- Authors
- Palleros, D. R., Welch, W. J., & Fink, A. L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1991-07
- Volume
- 88
- Issue
- 13
- Pages
- 5719-5723
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1964652518
- Cited by
- 333
- References
- 20
- FWCI
- 12.56
- Type
- journal article
- Language
- en
- Open access
- green
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- Palleros, D. R., Welch, W. J., & Fink, A. L. (1991). Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.88.13.5719
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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