The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Activity-Stability Relationships in Extremophilic Enzymes
Open accessAbstract
Psychrophilic, mesophilic, and thermophilic alpha-amylases have been studied as regards their conformational stability, heat inactivation, irreversible unfolding, activation parameters of the reaction, properties of the enzyme in complex with a transition state analog, and structural permeability. These data allowed us to propose an energy landscape for a family of extremophilic enzymes based on the folding funnel model, integrating the main differences in conformational energy, cooperativity of protein unfolding, and temperature dependence of the activity. In particular, the shape of the funnel bottom, which depicts the stability of the native state ensemble, also accounts for the thermodynamic parameters of activation that characterize these extremophilic enzymes, therefore providing a rational basis for stability-activity relationships in protein adaptation to extreme temperatures.
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Cited by
Psychrophilic enzymes: hot topics in cold adaptation
Feller, G., & Gerday, C. (2003) · Nature Reviews Microbiology · doi:10.1038/nrmicro773 · Cited by 1,155
Self-citationBiotechnological uses of enzymes from psychrophiles
Cavicchioli, R., Charlton, T., Ertan, H., Omar, S. M., Siddiqui, K. S., & Williams, T. J. (2011) · Microbial Biotechnology · doi:10.1111/j.1751-7915.2011.00258.x · Cited by 355
Protein stability and enzyme activity at extreme biological temperatures
Feller, G. (2010) · Journal of Physics: Condensed Matter · doi:10.1088/0953-8984/22/32/323101 · Cited by 337
Self-citationPsychrophilic Enzymes: From Folding to Function and Biotechnology
Feller, G. (2013) · Scientifica · doi:10.1155/2013/512840 · Cited by 323
Self-citationProtein Design: From the Aspect of Water Solubility and Stability
Qing, R., Hao, S., Smorodina, E., Jin, D., Zalevsky, A., & Zhang, S. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00757 · Cited by 312
Metadata
- Authors
- D'Amico, S., Marx, J.-C., Gerday, C., & Feller, G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-03
- Volume
- 278
- Issue
- 10
- Pages
- 7891-7896
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2157826157
- Cited by
- 455
- References
- 46
- FWCI
- 7.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
