CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS
CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS
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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
Through dominant mutations, aminoacyl-tRNA synthetases constitute the largest protein family linked to Charcot-Marie-Tooth disease (CMT). An example is CMT subtype 2N (CMT2N), caused by individual mutations spread out in AlaRS, including three in the aminoacylation domain, thereby suggesting a role for a tRNA-charging defect. However, here we found...
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Full title
CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8020758
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8020758
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ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.2012898118
