Structural characterization of the D290V mutation site in hnRNPA2 low-complexity–domain polymers
Structural characterization of the D290V mutation site in hnRNPA2 low-complexity–domain polymers
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United States: National Academy of Sciences
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Language
English
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United States: National Academy of Sciences
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Contents
Human genetic studies have given evidence of familial, disease-causing mutations in the analogous amino acid residue shared by three related RNA binding proteins causative of three neurological diseases. Alteration of aspartic acid residue 290 of hnRNPA2 to valine is believed to predispose patients to multisystem proteinopathy. Mutation of aspartic...
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Full title
Structural characterization of the D290V mutation site in hnRNPA2 low-complexity–domain polymers
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6196502
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_6196502
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ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1806174115
