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Systematically pert...
Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants
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- Lindberg, Mikael J (författare)
- Umeå universitet,Kemiska institutionen
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- Byström, Roberth, 1971- (författare)
- Umeå universitet,Kemiska institutionen
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- Boknäs, Niklas (författare)
- Umeå universitet,Kemiska institutionen
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- Andersen, Peter Munch, 1962- (författare)
- Umeå universitet,Neurologi
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- Oliveberg, Mikael (författare)
- Umeå universitet,Kemiska institutionen
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(creator_code:org_t)
- 2005-06-29
- 2005
- Engelska.
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : National Academy of Sciences. - 0027-8424. ; 102:28, s. 9754-9
- Relaterad länk:
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http://www.pnas.org/...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Amyotrophic lateral sclerosis is a neurodegenerative syndrome associated with 114 mutations in the gene encoding the cytosolic homodimeric enzyme Cu/Zn superoxide dismutase (SOD). In this article, we report that amyotrophic lateral sclerosis-associated SOD mutations with distinctly different disease progression can be rationalized in terms of their folding patterns. The mutations are found to perturb the protein in multiple ways; they destabilize the precursor monomers (class 1), weaken the dimer interface (class 2), or both at the same time (class 1 + 2). A shared feature of the mutational perturbations is a shift of the folding equilibrium toward poorly structured SOD monomers. We observed a link, coupled to the altered folding patterns, between protein stability, net charge, and survival time for the patients carrying the mutations.
Nyckelord
- neurodegenerative disease
- protein stability
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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