Functional features cause misfolding of the ALS-provoking enzyme SOD1

The structural integrity of the ubiquitous enzyme superoxide dismutase (SOD1) relies critically on the correct coordination of Cu and Zn. Loss of these cofactors not only promotes SOD1 aggregation in vitro but also seems to be a key prerequisite for pathogenic misfolding in the neurodegenerative dis...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Päätekijät: Nordlund, Anna, Leinartaitė, Lina, Saraboji, Kadhirvel, Aisenbrey, Christopher, Gröbner, Gerhard, Zetterström, Per, Danielsson, Jens, Logan, Derek T., Oliveberg, Mikael
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: National Academy of Sciences 2009
Aiheet:
Biological Sciences
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC2701049/
https://ncbi.nlm.nih.gov/pubmed/19497878
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0812046106
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