Posttranslational modification of alpha-dystroglycan, the cellular receptor for arenaviruses, by the glycosyltransferase LARGE is critical for virus binding. (Q34123911)

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English	Posttranslational modification of alpha-dystroglycan, the cellular receptor for arenaviruses, by the glycosyltransferase LARGE is critical for virus binding.	scientific article

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8 January 2020

Posttranslational modification of alpha-dystroglycan, the cellular receptor for arenaviruses, by the glycosyltransferase LARGE is critical for virus binding (English)

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8 January 2020

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8 January 2020

Kevin P Campbell

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8 January 2020

Christina F Spiropoulou

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Christina F Spiropoulou

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8 January 2020

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Jillian M Rojek

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8 January 2020

Motoi Kanagawa

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8 January 2020

Rita Barresi

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8 January 2020

Michael B A Oldstone

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1 November 2005

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8 January 2020

Journal of Virology

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8 January 2020

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8 January 2020

14282-14296

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8 January 2020

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8 January 2020

O Mannosylation of alpha-dystroglycan is essential for lymphocytic choriomeningitis virus receptor function

1 reference

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Characterization of the interaction of lassa fever virus with its cellular receptor alpha-dystroglycan

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Localization and functional analysis of the LARGE family of glycosyltransferases: significance for muscular dystrophy

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Structure, function and pathology of O-mannosyl glycans

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Molecular recognition by LARGE is essential for expression of functional dystroglycan

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Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity

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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

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Glycosylation defects: a new mechanism for muscular dystrophy?

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Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function.

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Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies

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Biology and pathogenesis of lymphocytic choriomeningitis virus infection.

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New World arenavirus clade C, but not clade A and B viruses, utilizes alpha-dystroglycan as its major receptor

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

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Molecular analysis of the interaction of LCMV with its cellular receptor [alpha]-dystroglycan.

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A stoichiometric complex of neurexins and dystroglycan in brain

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Mutant glycosyltransferase and altered glycosylation of alpha-dystroglycan in the myodystrophy mouse

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Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins

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

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LARGE can functionally bypass alpha-dystroglycan glycosylation defects in distinct congenital muscular dystrophies.

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1 reference

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28 October 2018

1 reference

https://pubmed.ncbi.nlm.nih.gov/16254363

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Monoclonal antibodies to lymphocytic choriomeningitis and pichinde viruses: Generation, characterization, and cross-reactivity with other arenaviruses

1 reference

https://pubmed.ncbi.nlm.nih.gov/16254363

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A role for dystroglycan in basement membrane assembly

1 reference

https://pubmed.ncbi.nlm.nih.gov/16254363

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/JVI.79.22.14282-14296.2005

1 reference

Europe PubMed Central

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8 January 2020

1 reference

Europe PubMed Central

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8 January 2020

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16254363%20AND%20SRC:MED&resulttype=core&format=json

8 January 2020

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