Dystroglycan inside and out

Current Opinion in Cell Biology

Volumn 11, Issue 5, 1999, Pages 602-607

  Henry, Michael D ^a   Campbell, Kevin P ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; DYSTROGLYCAN; PERLECAN; SCLEROPROTEIN;

BACTERIAL INFECTION; BASEMENT MEMBRANE; CELL SURFACE; CYTOSKELETON; EXTRACELLULAR MATRIX; MUSCULAR DYSTROPHY; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; REVIEW;

BACTERIA (MICROORGANISMS);

EID: 0032822661     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)00024-1     Document Type: Review

References (55)

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23. ••], provides mechanistic insight to differential salt and heparin sensitivities of laminin-1 and laminin-2 binding to α-dystroglycan. Sets the stage for future studies aimed at comparing the dystroglycan-binding properties of the various members of the laminin family.
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25. ••] above. The work reported by the authors of this paper also demonstrates direct binding between α-dystroglycan and perlecan, which is, quite interestingly, of higher affinity than that between α-dystroglycan and the laminin α1 G domains.
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28. ••]. This paper clearly provides a basis by which heparin sulfate proteoglycans could regulate dystroglycan ligand binding.
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