Heterodimerization of the sialidase NEU1 with the chaperone protective protein/cathepsin A prevents its premature oligomerization. - Wikidata - wikimedia - TriplyDB

Heterodimerization of the sialidase NEU1 with the chaperone protective protein/cathepsin A prevents its premature oligomerization.

Heterodimerization of the sialidase NEU1 with the chaperone protective protein/cathepsin A prevents its premature oligomerization.

http://www.wikidata.org/entity/Q37460020

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Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity In silico identification of new putative pathogenic variants in the NEU1 sialidase gene affecting enzyme function and subcellular localization Lysosomal multienzyme complex: pros and cons of working together Molecular mechanisms of pathogenesis in a glycosphingolipid and a glycoprotein storage disease Pathogenesis, Emerging therapeutic targets and Treatment in Sialidosis.Chaperone-mediated gene therapy with recombinant AAV-PPCA in a new mouse model of type I sialidosis NEU1 sialidase regulates the sialylation state of CD31 and disrupts CD31-driven capillary-like tube formation in human lung microvascular endothelia.Galactosialidosis: historic aspects and overview of investigated and emerging treatment options.Sialylation of N-glycans: mechanism, cellular compartmentalization and function.New Insights into Molecular Organization of Human Neuraminidase-1: Transmembrane Topology and Dimerization Ability.Neuraminidase-1 mediates skeletal muscle regeneration.Neuraminidase activity mediates IL-6 production by activated lupus-prone mesangial cells.Lysosomal multienzymatic complex-related diseases: a genetic study among Portuguese patients

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P2860

Heterodimerization of the sialidase NEU1 with the chaperone protective protein/cathepsin A prevents its premature oligomerization.

http://www.wikidata.org/entity/Q37460020

description

article científic

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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 07 August 2009

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

Heterodimerization of the sial ...... its premature oligomerization.

@en

Heterodimerization of the sial ...... its premature oligomerization.

@nl

type

label

Heterodimerization of the sial ...... its premature oligomerization.

@en

Heterodimerization of the sial ...... its premature oligomerization.

@nl

prefLabel

Heterodimerization of the sial ...... its premature oligomerization.

@en

Heterodimerization of the sial ...... its premature oligomerization.

@nl

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P356

JBC.M109.031419

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Journal of Biological Chemistry

P1476

Heterodimerization of the sial ...... its premature oligomerization.

@en

P2093

Alessandra d'Azzo

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

Amanda Nourse

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Brett Waddell

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Erik J Bonten

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Garry Taylor

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Viateslav Zaitsev

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William Lewis

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Yvan Campos

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P2860

Expression of cDNA encoding the human "protective protein" associated with lysosomal beta-galactosidase and neuraminidase: homology to yeast proteases

Neu4, a novel human lysosomal lumen sialidase, confers normal phenotype to sialidosis and galactosialidosis cells

Molecular cloning and characterization of NEU4, the fourth member of the human sialidase gene family

Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis

Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits

Molecular mechanism of lysosomal sialidase deficiency in galactosialidosis involves its rapid degradation

Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A.

The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll

Three-dimensional structure of the human 'protective protein': structure of the precursor form suggests a complex activation mechanism

Coot: model-building tools for molecular graphics

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28430-28441

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scholarly article

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10.1074/JBC.M109.031419

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41

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2009-08-07T00:00:00Z

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19666471

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P921

molecular chaperones

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2788892

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