Associated Papers
Genetic Loss of Sucrase-Isomaltase Function: Mechanisms, Implications, and Future Perspectives.
Senftleber NK et al.
The Application of Clinical Genetics, 2023
Two Novel Mutations in the SI Gene Associated With Congenital Sucrase-Isomaltase Deficiency: A Case Report in China.
Zhou J et al.
Frontiers in Pediatrics, 2021
Heterozygotes Are a Potential New Entity among Homozygotes and Compound Heterozygotes in Congenital Sucrase-Isomaltase Deficiency.
Husein DM et al.
Nutrients, 2019
Congenital Sucrase-isomaltase Deficiency: A Novel Compound Heterozygous Mutation Causing Aberrant Protein Localization.
Haberman Y et al.
Journal of Pediatric Gastroenterology and Nutrition, 2017
Impaired trafficking and subcellular localization of a mutant lactase associated with congenital lactase deficiency.
Behrendt M et al.
Gastroenterology, 2009
Altered folding, turnover, and polarized sorting act in concert to define a novel pathomechanism of congenital sucrase-isomaltase deficiency.
Keiser M et al.
The Journal of Biological Chemistry, 2006
Novel mutations in the human sucrase-isomaltase gene (SI) that cause congenital carbohydrate malabsorption.
Sander P et al.
Human Mutation, 2006
A phenylalanine-based folding determinant in intestinal sucrase-isomaltase that functions in the context of a quality control mechanism beyond the endoplasmic reticulum.
Pröpsting MJ et al.
Journal of Cell Science, 2005
Congenital sucrase-isomaltase deficiency because of an accumulation of the mutant enzyme in the endoplasmic reticulum.
Ritz V et al.
Gastroenterology, 2003
A glutamine to proline exchange at amino acid residue 1098 in sucrase causes a temperature-sensitive arrest of sucrase-isomaltase in the endoplasmic reticulum and cis-Golgi.
Pröpsting MJ et al.
The Journal of Biological Chemistry, 2003
Congenital sucrase-isomaltase deficiency presenting with failure to thrive, hypercalcemia, and nephrocalcinosis.
Belmont JW et al.
Bmc Pediatrics, 2002
Analysis of a naturally occurring mutation in sucrase-isomaltase: glutamine 1098 is not essential for transport to the surface of COS-1 cells.
Ouwendijk J et al.
Biochimica Et Biophysica Acta, 1998
A mutation in a highly conserved region in brush-border sucrase-isomaltase and lysosomal alpha-glucosidase results in Golgi retention.
Moolenaar CE et al.
Journal of Cell Science, 1997
Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment.
Ouwendijk J et al.
The Journal of Clinical Investigation, 1996
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