Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ. - Wikidata - awgldk - TriplyDB

Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.

Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.

http://www.wikidata.org/entity/Q37627989

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Analysis of mucolipidosis II/III GNPTAB missense mutations identifies domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase involved in catalytic function and lysosomal enzyme recognition Analyses of disease-related GNPTAB mutations define a novel GlcNAc-1-phosphotransferase interaction domain and an alternative site-1 protease cleavage site Mammalian O-mannosylation of cadherins and plexins is independent of protein O-mannosyltransferases 1 and 2.The lysosomal enzyme receptor protein (LERP) is not essential, but is implicated in lysosomal function in Drosophila melanogaster.Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival Mucolipidosis III GNPTG Missense Mutations Cause Misfolding of the γ Subunit of GlcNAc-1-Phosphotransferase.Tuberous sclerosis, polycystic kidney disease and mucolipidosis III gamma caused by a microdeletion unmasking a recessive mutation.

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Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.

http://www.wikidata.org/entity/Q37627989

description

article científic

@ca

article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 18 February 2014

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vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.

@en

Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.

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type

label

Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.

@en

Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.

@nl

prefLabel

Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.

@en

Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.

@nl

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PNAS.1401417111

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Proceedings of the National Academy of Sciences of the United States of America

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Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.

@en

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Eline van Meel

http://www.w3.org/2001/XMLSchema#string

Stuart A Kornfeld

http://www.w3.org/2001/XMLSchema#string

Yi Qian

http://www.w3.org/2001/XMLSchema#string

P2860

The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a substrate recognition module

Golgi phosphoprotein 3 determines cell binding properties under dynamic flow by controlling Golgi localization of core 2 N-acetylglucosaminyltransferase 1.

A key enzyme in the biogenesis of lysosomes is a protease that regulates cholesterol metabolism

Mucolipidosis II-related mutations inhibit the exit from the endoplasmic reticulum and proteolytic cleavage of GlcNAc-1-phosphotransferase precursor protein (GNPTAB)

Golgi localization of glycosyltransferases requires a Vps74p oligomer

Functions of the alpha, beta, and gamma subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase

Mutation of the COG complex subunit gene COG7 causes a lethal congenital disorder

Signal-mediated dynamic retention of glycosyltransferases in the Golgi.

When Mucolipidosis III meets Mucolipidosis II: GNPTA gene mutations in 24 patients

The alpha- and beta-subunits of the human UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase [corrected] are encoded by a single cDNA.

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3532-3537

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scholarly article

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10.1073/PNAS.1401417111

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9

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111

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2014-02-18T00:00:00Z

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260254087

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24550498

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3948257

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