Associated Papers
Base editing corrects the common Salla disease SLC17A5 c.115C>T variant.
Harb JF et al.
Molecular Therapy. Nucleic Acids, 2023
The molecular mechanism of sialic acid transport mediated by Sialin.
Hu W et al.
Science Advances, 2023
Ion transport and regulation in a synaptic vesicle glutamate transporter.
Li F et al.
Science (new York, N.y.), 2020
Functional characterization of vesicular excitatory amino acid transport by human sialin.
Miyaji T et al.
Journal of Neurochemistry, 2011
Structure-function studies of the SLC17 transporter sialin identify crucial residues and substrate-induced conformational changes.
Courville P et al.
The Journal of Biological Chemistry, 2010
A vesicular transporter that mediates aspartate and glutamate neurotransmission.
Miyaji T et al.
Biological & Pharmaceutical Bulletin, 2010
Molecular and cellular basis of lysosomal transmembrane protein dysfunction.
Ruivo R et al.
Biochimica Et Biophysica Acta, 2009
Identification of a vesicular aspartate transporter.
Miyaji T et al.
Proceedings of the National Academy of Sciences of the United States of America, 2008
Homozygosity for the p.K136E mutation in the SLC17A5 gene as cause of an Italian severe Salla disease.
Biancheri R et al.
Neurogenetics, 2005
Varied mechanisms underlie the free sialic acid storage disorders.
Wreden CC et al.
The Journal of Biological Chemistry, 2005
Functional characterization of wild-type and mutant human sialin.
Morin P et al.
The Embo Journal, 2004
The spectrum of SLC17A5-gene mutations resulting in free sialic acid-storage diseases indicates some genotype-phenotype correlation.
Aula N et al.
American Journal of Human Genetics, 2000
A new gene, encoding an anion transporter, is mutated in sialic acid storage diseases.
Verheijen FW et al.
Nature Genetics, 1999
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