Skip to search formSkip to main contentSkip to account menu

Dystroglycans

Known as: Cranin, Dystroglycan, Dystroglycans [Chemical/Ingredient] 
Dystrophin-associated proteins that play role in the formation of a transmembrane link between laminin-2 and DYSTROPHIN. Both the alpha and the beta… 
National Institutes of Health

Related topics

Related topics

13 relations

Narrower (3)

Dystrophin-Associated Glycoprotein 1alpha-Dystroglycanbeta-Dystroglycan
Dystrophin-Associated Protein ComplexIn BloodProcess of secretionWalker-Warburg congenital muscular dystrophy

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2008
2008
Biochemical characterization of MLC1 protein in astrocytes and its association with the dystrophin–glycoprotein complex
2007
2007
The sarcoglycan complex in Schwann cells and its role in myelin stability
Highly Cited
2004
Highly Cited
2004
Podocyte flattening and disorder of glomerular basement membrane are associated with splitting of dystroglycan-matrix interaction.
The transmembrane component of the dystroglycan complex, a heterodimer of alpha- and beta-dystroglycan, was recently localized at… 
Highly Cited
2003
Highly Cited
2003
Expression of mouse agrin in normal, denervated and dystrophic muscle
2002
2002
Definition of pre- and postsynaptic forms of the CT carbohydrate antigen at the neuromuscular junction: ubiquitous expression of the CT antigens and the CT GalNAc transferase in mouse tissues.
Highly Cited
2000
Highly Cited
2000
Immunolocalization of dystrobrevin in the astrocytic endfeet and endothelial cells in the rat cerebellum
Highly Cited
1999
Highly Cited
1999
Biochemical Characterization of the Epithelial Dystroglycan Complex*
Dystroglycan is a widely expressed extracellular matrix receptor that plays a critical role in basement membrane formation… 
Review
1997
Review
1997
Peripheral nerve involvement in merosin-deficient congenital muscular dystrophy and dy mouse
1994
1994
Expression of dystrophin-associated glycoproteins during human fetal muscle development: A preliminary immunocytochemical study
1993
1993
Cranin interacts specifically with the sulfatide‐binding domain of laminin
Cranin is a 120 kDa integral membrane glycoprotein which binds laminin under conditions of physiologic ionic strength in a… 
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)