Transport to cell surface of intestinal sucrase-isomaltase is blocked in the Golgi apparatus in a patient with congenital sucrase-isomaltase deficiency.
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Naturally occurring mutations in intestinal sucrase-isomaltase provide evidence for the existence of an intracellular sorting signal in the isomaltase subunitStudies on the expression of intestinal lactase in different individuals.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-GolgiRotavirus infection reduces sucrase-isomaltase expression in human intestinal epithelial cells by perturbing protein targeting and organization of microvillar cytoskeleton.Molecular cloning of sucrase-isomaltase cDNA in the house musk shrew Suncus murinus and identification of a mutation responsible for isolated sucrase deficiency.Sucrase-isomaltase deficiency in humans. Different mutations disrupt intracellular transport, processing, and function of an intestinal brush border enzyme.Congenital sucrase-isomaltase deficiency arising from cleavage and secretion of a mutant form of the enzyme.The posttranslational processing of sucrase-isomaltase in HT-29 cells is a function of their state of enterocytic differentiation.A novel marker glycoprotein for the microvillus membrane of surface colonocytes of rat large intestine and its presence in small-intestinal crypt cells.Dissection of the asynchronous transport of intestinal microvillar hydrolases to the cell surface.Sucrase is an intramolecular chaperone located at the C-terminal end of the sucrase-isomaltase enzyme complex.The clinical consequences of sucrase-isomaltase deficiency.Molecular basis of aberrant apical protein transport in an intestinal enzyme disorder.Morphological and biochemical analysis of the secretory pathway in melanoma cells with distinct metastatic potential.Involvement of CRF2 signaling in enterocyte differentiation.Long term differential consequences of miglustat therapy on intestinal disaccharidases.Polyamine participation in the maturation of glycoprotein fucosylation, but not sialylation, in rat small intestine.Pharmacoperones as Novel Therapeutics for Diverse Protein Conformational Diseases.
P2860
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P2860
Transport to cell surface of intestinal sucrase-isomaltase is blocked in the Golgi apparatus in a patient with congenital sucrase-isomaltase deficiency.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on July 1985
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Transport to cell surface of i ...... sucrase-isomaltase deficiency.
@en
Transport to cell surface of i ...... sucrase-isomaltase deficiency.
@nl
type
label
Transport to cell surface of i ...... sucrase-isomaltase deficiency.
@en
Transport to cell surface of i ...... sucrase-isomaltase deficiency.
@nl
prefLabel
Transport to cell surface of i ...... sucrase-isomaltase deficiency.
@en
Transport to cell surface of i ...... sucrase-isomaltase deficiency.
@nl
P2093
P2860
P921
P356
P1476
Transport to cell surface of i ...... sucrase-isomaltase deficiency.
@en
P2093
P2860
P304
P356
10.1073/PNAS.82.13.4423
P407
P577
1985-07-01T00:00:00Z