The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Variation in the Biochemical/Biophysical Properties of Mutant Superoxide Dismutase 1 Enzymes and the Rate of Disease Progression in Familial Amyotrophic Lateral Sclerosis Kindreds
Open accessAbstract
Mutations in superoxide dismutase 1 (SOD1) polypeptides cause a form of familial amyotrophic lateral sclerosis (FALS). In different kindreds, harboring different mutations, the duration of illness tends to be similar for a given mutation. For example, patients inheriting a substitution of valine for alanine at position four (A4V) average a 1.5 year life expectancy after the onset of symptoms, whereas patients harboring a substitution of arginine for histidine at position 46 (H46R) average an 18 year life expectancy after disease onset. Here, we examine a number of biochemical and biophysical properties of nine different FALS variants of SOD1 polypeptides, including enzymatic activity (which relates indirectly to the affinity of the enzyme for copper), polypeptide half-life, resistance to proteolytic degradation and solubility, in an effort to determine whether a specific property of these enzymes correlates with clinical progression. We find that although all the mutants tested appear to be soluble, the different mutants show a remarkable degree of variation with respect to activity, polypeptide half-life and resistance to proteolysis. However, these variables do not stratify in a manner that correlates with clinical progression. We conclude that the basis for the different life expectancies of patients in different kindreds of sod1-linked FALS may result from an as yet unidentified property of these mutant enzymes.
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Cites
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Mattiazzi, M., D'Aurelio, M., Gajewski, C. D., Martushova, K., Kiaei, M., Beal, M. F., & Manfredi, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203065200 · Cited by 616
De Vos, K. J., Chapman, A. L., Tennant, M. E., Manser, C., Tudor, E. L., Lau, K.-F., Brownlees, J., Ackerley, S., Shaw, P. J., McLoughlin, D. M., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm226 · Cited by 420
Antisense oligonucleotides extend survival and reverse decrement in muscle response in ALS models
McCampbell, A., Cole, T., Wegener, A. J., Tomassy, G. S., Setnicka, A., Farley, B. J., Schoch, K. M., Hoye, M. L., Shabsovich, M., Sun, L., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci99081 · Cited by 279
Intermolecular transmission of superoxide dismutase 1 misfolding in living cells
Grad, L. I., Guest, W. C., Yanai, A., Pokrishevsky, E., O'Neill, M. A., Gibbs, E., Semenchenko, V., Yousefi, M., Wishart, D. S., Plotkin, S. S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102645108 · Cited by 274
Genetic epidemiology of amyotrophic lateral sclerosis
Majoor‐Krakauer, D., Willems, P., & Hofman, A. (2003) · Clinical Genetics · doi:10.1046/j.0009-9163.2002.00001.x · Cited by 147
Metadata
- Authors
- Ratovitski, T., Corson, L. B., Strain, J., Wong, P., Cleveland, D. W., Culotta, V. C., & Borchelt, D. R.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 1999-08-01
- Volume
- 8
- Issue
- 8
- Pages
- 1451-1460
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2133408527
- Cited by
- 180
- References
- 4
- FWCI
- 5.19
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Ratovitski, T., Corson, L. B., Strain, J., Wong, P., Cleveland, D. W., Culotta, V. C., & Borchelt, D. R. (1999). Variation in the Biochemical/Biophysical Properties of Mutant Superoxide Dismutase 1 Enzymes and the Rate of Disease Progression in Familial Amyotrophic Lateral Sclerosis Kindreds. Human Molecular Genetics. https://doi.org/10.1093/hmg/8.8.1451
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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).
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