Loss of alpha-dystroglycan laminin binding in epithelium-derived cancers is caused by silencing of LARGE. - Wikidata - wikimedia - TriplyDB

Loss of alpha-dystroglycan laminin binding in epithelium-derived cancers is caused by silencing of LARGE.

Loss of alpha-dystroglycan laminin binding in epithelium-derived cancers is caused by silencing of LARGE.

http://www.wikidata.org/entity/Q37160880

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Human UDP-α-D-xylose synthase and Escherichia coli ArnA conserve a conformational shunt that controls whether xylose or 4-keto-xylose is produced B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan The glucuronyltransferase B4GAT1 is required for initiation of LARGE-mediated α-dystroglycan functional glycosylation Tumor suppressor function of laminin-binding alpha-dystroglycan requires a distinct beta3-N-acetylglucosaminyltransferase ISPD loss-of-function mutations disrupt dystroglycan O-mannosylation and cause Walker-Warburg syndrome Mammalian O-mannosylation: unsolved questions of structure/function O-Mannosylation and human disease Endocytic trafficking of laminin is controlled by dystroglycan and is disrupted in cancers.Fer kinase regulates cell migration through α-dystroglycan glycosylation JISTIC: identification of significant targets in cancer.The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression.Large induces functional glycans in an O-mannosylation dependent manner and targets GlcNAc terminals on alpha-dystroglycan LARGE expression augments the glycosylation of glycoproteins in addition to α-dystroglycan conferring laminin binding.DNA damage, somatic aneuploidy, and malignant sarcoma susceptibility in muscular dystrophies.Differential glycosylation of α-dystroglycan and proteins other than α-dystroglycan by like-glycosyltransferase Dystroglycan controls signaling of multiple hormones through modulation of STAT5 activity.Human natural killer-1 sulfotransferase (HNK-1ST)-induced sulfate transfer regulates laminin-binding glycans on α-dystroglycan.Sarcolemma instability during mechanical activity in Largemyd cardiac myocytes with loss of dystroglycan extracellular matrix receptor function Reduced glycosylation of α-dystroglycans on carcinoma cells contributes to formation of highly infiltrative histological patterns in prostate cancer.Synthetic, structural, and biosynthetic studies of an unusual phospho-glycopeptide derived from α-dystroglycan.Absence of post-phosphoryl modification in dystroglycanopathy mouse models and wild-type tissues expressing non-laminin binding form of α-dystroglycan.Downregulation of dystroglycan glycosyltransferases LARGE2 and ISPD associate with increased mortality in clear cell renal cell carcinoma.Loss of cell-surface laminin anchoring promotes tumor growth and is associated with poor clinical outcomes.The glycosyltransferase LARGE2 is repressed by Snail and ZEB1 in prostate cancer.Increased expression of CD133 and reduced dystroglycan expression are strong predictors of poor outcome in colon cancer patients.Polarization and myelination in myelinating glia.Loss of LARGE2 disrupts functional glycosylation of α-dystroglycan in prostate cancer.The o-mannosylation pathway: glycosyltransferases and proteins implicated in congenital muscular dystrophy.VHL-dependent regulation of a β-dystroglycan glycoform and glycogene expression in renal cancer LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans.Protein O-mannosylation in metazoan organisms.Basement membrane components are key players in specialized extracellular matrices.Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.Nuclear targeting of dystroglycan promotes the expression of androgen regulated transcription factors in prostate cancer.Dystroglycan function is a novel determinant of tumor growth and behavior in prostate cancer.Loss of dystroglycan function in oesophageal cancer.Golgi phosphoprotein 3 mediates the Golgi localization and function of protein O-linked mannose β-1,2-N-acetlyglucosaminyltransferase 1.γ-Secretase Dependent Nuclear Targeting of Dystroglycan.Recent advancements in understanding mammalian O-mannosylation.LARGE enzyme activity deciphered: a new therapeutic target for muscular dystrophies.

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P2860

Loss of alpha-dystroglycan laminin binding in epithelium-derived cancers is caused by silencing of LARGE.

http://www.wikidata.org/entity/Q37160880

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 24 February 2009

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

@cs

name

Loss of alpha-dystroglycan lam ...... caused by silencing of LARGE.

@en

Loss of alpha-dystroglycan lam ...... caused by silencing of LARGE.

@nl

type

label

Loss of alpha-dystroglycan lam ...... caused by silencing of LARGE.

@en

Loss of alpha-dystroglycan lam ...... caused by silencing of LARGE.

@nl

prefLabel

Loss of alpha-dystroglycan lam ...... caused by silencing of LARGE.

@en

Loss of alpha-dystroglycan lam ...... caused by silencing of LARGE.

@nl

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Journal of Biological Chemistry

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Loss of alpha-dystroglycan lam ...... s caused by silencing of LARGE

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P2093

Christine J Weydert

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Daniel Beltrán-Valero de Bernabé

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

Hollie A Harper

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Kei-Ichiro Inamori

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Takako Yoshida-Moriguchi

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Tobias Willer

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P2860

The human LARGE gene from 22q12.3-q13.1 is a new, distinct member of the glycosyltransferase gene family

Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1

An ancient retrotransposal insertion causes Fukuyama-type congenital muscular dystrophy

Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan.

Dystroglycan, a scaffold for the ERK-MAP kinase cascade.

Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome

POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-Warburg syndrome

A stoichiometric complex of neurexins and dystroglycan in brain

Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan

Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor

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11279-11284

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17

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284

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Michael D. Henry

Kevin P Campbell

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2009-02-24T00:00:00Z

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19244252

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