The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state
Open accessAbstract
More than 100 point mutations of the superoxide scavenger Cu/Zn superoxide dismutase (SOD; EC ) have been associated with the neurodegenerative disease amyotrophic lateral sclerosis (ALS). However, these mutations are scattered throughout the protein and provide no clear functional or structural clues to the underlying disease mechanism. Therefore, we undertook to look for folding-related defects by comparing the unfolding behavior of five ALS-associated mutants with distinct structural characteristics: A4V at the interface between the N and C termini, C6F in the hydrophobic core, D90A at the protein surface, and G93A and G93C, which decrease backbone flexibility. With the exception of the disruptive replacements A4V and C6F, the mutations only marginally affect the stability of the native protein, yet all mutants share a pronounced destabilization of the metal-free apo state: the higher the stability loss, the lower the mean survival time for ALS patients carrying the mutation. Thus organism-level pathology may be directly related to the properties of the immature state of a protein rather than to those of the native species.
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Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Conversion of α-lactalbumin to a protein inducing apoptosis.
Svensson, M., Håkansson, A., Mossberg, A.-K., Linse, S., & Svanborg, C. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.8.4221 · Cited by 355
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Superoxide dismutases and superoxide reductases
Sheng, Y., Abreu, I. A., Cabelli, D. E., Maroney, M. J., Miller, A.-F., Teixeira, M., & Valentine, J. S. (2014) · Chemical Reviews · doi:10.1021/cr4005296 · Cited by 1,081
Aggregation of Copper–Zinc Superoxide Dismutase in Familial and Sporadic ALS
Chattopadhyay, M., & Valentine, J. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2536 · Cited by 163
AlphaFold and the amyloid landscape
Pinheiro, F., Santos, J., & Ventura, S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167059 · Cited by 88
Metadata
- Authors
- Lindberg, M. J., Tibell, L., & Oliveberg, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-12-13
- Volume
- 99
- Issue
- 26
- Pages
- 16607-16612
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2096678032
- Cited by
- 193
- References
- 4
- FWCI
- 9.00
- Type
- journal article
- Language
- en
- Open access
- green
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- Lindberg, M. J., Tibell, L., & Oliveberg, M. (2002). Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: Decreased stability of the apo state. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.262527099
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