Differential heparin sensitivity of alpha-dystroglycan binding to laminins expressed in normal and dy/dy mouse skeletal muscle (Q77195610)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9727035%20AND%20SRC:MED&resulttype=core&format=json

3 December 2019

title

Differential heparin sensitivity of alpha-dystroglycan binding to laminins expressed in normal and dy/dy mouse skeletal muscle (English)

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3 December 2019

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E L McDearmon

1

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3 December 2019

A L Burwell

2

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3 December 2019

A C Combs

3

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3 December 2019

B A Renley

4

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3 December 2019

M T Sdano

5

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3 December 2019

J M Ervasti

6

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3 December 2019

language of work or name

English

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publication date

1 September 1998

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Journal of Biological Chemistry

3 December 2019

published in

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3 December 2019

volume

273

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3 December 2019

issue

37

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3 December 2019

page(s)

24139-24144

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Laminin receptors: achieving specificity through cooperation

3 December 2019

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The alpha7beta1 integrin mediates adhesion and migration of skeletal myoblasts on laminin

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Absence of integrin alpha 7 causes a novel form of muscular dystrophy

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Dystroglycan: an extracellular matrix receptor linked to the cytoskeleton.

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Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle

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Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix

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Membrane organization of the dystrophin-glycoprotein complex

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A new model for the interaction of dystrophin with F-actin

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Dystrophin-glycoprotein complex is monomeric and stabilizes actin filaments in vitro through a lateral association

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A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin.

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Dystrophin protects the sarcolemma from stresses developed during muscle contraction

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Mechanical function of dystrophin in muscle cells

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Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice

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Animal models for muscular dystrophy show different patterns of sarcolemmal disruption.

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Differential heparin inhibition of skeletal muscle alpha-dystroglycan binding to laminins

21 January 2018

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Tissue-specific heterogeneity in alpha-dystroglycan sialoglycosylation. Skeletal muscle alpha-dystroglycan is a latent receptor for Vicia villosa agglutinin b4 masked by sialic acid modification.

21 January 2018

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Electron microscopic evidence for a mucin-like region in chick muscle alpha-dystroglycan

21 January 2018

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Agrin binds to the nerve-muscle basal lamina via laminin

21 January 2018

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Presence of Laminin 5 Chain and Lack of Laminin 1 Chain during Human Muscle Development and in Muscular Dystrophies

21 January 2018

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21 January 2018

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A specific sequence of the laminin alpha 2 chain critical for the initiation of heterotrimer assembly

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Dystroglycan is a dual receptor for agrin and laminin-2 in Schwann cell membrane

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.37.24139

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9727035%20AND%20SRC:MED&resulttype=core&format=json

3 December 2019

1 reference