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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...

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書誌詳細
主要な著者: Nordlund, Anna, Leinartaitė, Lina, Saraboji, Kadhirvel, Aisenbrey, Christopher, Gröbner, Gerhard, Zetterström, Per, Danielsson, Jens, Logan, Derek T., Oliveberg, Mikael
フォーマット: Artigo
言語:Inglês
出版事項: National Academy of Sciences 2009
主題:
オンライン・アクセス: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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