Associated Papers
Structure and inhibition of the human lysosomal transporter Sialin.
Schmiege P et al.
Nature Communications, 2024
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
Functional characterization of vesicular excitatory amino acid transport by human sialin.
Miyaji T et al.
Journal of Neurochemistry, 2011
Molecular and cellular basis of lysosomal transmembrane protein dysfunction.
Ruivo R et al.
Biochimica Et Biophysica Acta, 2009
Molecular pathogenesis of sialic acid storage diseases: insight gained from four missense mutations and a putative polymorphism of human sialin.
Ruivo R et al.
Biology of the Cell, 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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