Old World and clade C New World arenaviruses mimic the molecular mechanism of receptor recognition used by alpha-dystroglycan's host-derived ligands (Q35857739)

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scientific article published on 14 March 2007

Language	Label	Description	Also known as
English	Old World and clade C New World arenaviruses mimic the molecular mechanism of receptor recognition used by alpha-dystroglycan's host-derived ligands	scientific article published on 14 March 2007

Statements

scholarly article

1 reference

Europe PubMed Central

10 August 2017

Old World and clade C New World arenaviruses mimic the molecular mechanism of receptor recognition used by alpha-dystroglycan's host-derived ligands (English)

1 reference

Europe PubMed Central

10 August 2017

4

object named as

Stefan Kunz

1 reference

Europe PubMed Central

10 August 2017

Christina F Spiropoulou

2

object named as

Christina F Spiropoulou

1 reference

Europe PubMed Central

10 August 2017

author name string

Jillian M Rojek

1

1 reference

Europe PubMed Central

10 August 2017

Kevin P Campbell

3

1 reference

Europe PubMed Central

10 August 2017

language of work or name

0 references

publication date

14 March 2007

1 reference

Europe PubMed Central

10 August 2017

Journal of Virology

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Europe PubMed Central

10 August 2017

81

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Europe PubMed Central

10 August 2017

5685-5695

1 reference

Europe PubMed Central

10 August 2017

11

1 reference

Europe PubMed Central

10 August 2017

The genetic and molecular basis of muscular dystrophy: roles of cell-matrix linkage in the pathogenesis

1 reference

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Glycosylation in cellular mechanisms of health and disease

1 reference

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Nothing in glycobiology makes sense, except in the light of evolution

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Transmission of lymphocytic choriomeningitis virus by organ transplantation

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Dystroglycan: from biosynthesis to pathogenesis of human disease.

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

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

1 reference

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Glycoconjugate glycans as viral receptors

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Enhanced laminin binding by alpha-dystroglycan after enzymatic deglycosylation

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Mouse large can modify complex N- and mucin O-glycans on alpha-dystroglycan to induce laminin binding

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Dystroglycan: important player in skeletal muscle and beyond

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Exotic emerging viral diseases: progress and challenges

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Structure, function and pathology of O-mannosyl glycans

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Proteolytic enzymes and altered glycosylation modulate dystroglycan function in carcinoma cells.

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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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Core 1 glycans on alpha-dystroglycan mediate laminin-induced acetylcholine receptor clustering but not laminin binding

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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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Differences in affinity of binding of lymphocytic choriomeningitis virus strains to the cellular receptor alpha-dystroglycan correlate with viral tropism and disease kinetics

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The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin

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Identifiers

10.1128/JVI.02574-06

1 reference

Europe PubMed Central

10 August 2017

1 reference

Europe PubMed Central

10 August 2017

1 reference

Europe PubMed Central

10 August 2017

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