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. 2016 Jun 23;3(8):650–654. doi: 10.1002/acn3.329

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Published 2016. This article is a U.S. Government work and is in the public domain in the USA. Annals of Clinical and Translational Neurology published by Wiley Periodicals, Inc. on behalf of American Neurological Association

This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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Domain organization and disease mutations of the associated glycoprotein. (A) Structural domains of MAG and mutations in our patients as well as previously reported mutations. Amino acid residue numbers are indicated (single letter amino acid code). (B) Family pedigree, with affected individuals harboring homozygous p.Arg118His mutations identified by black‐filled squares. Alignments of the residues surrounding Arg118, showing conservation among species (C) and across other human sialoproteins (D). Amino acid residue numbers are indicated for human MAG.