Effect of inhibitors of glycoprotein processing on integrin and the adhesion of myoblasts to extracellular matrix proteins
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference20 articles.
1. Inhibition of myoblast fusion by tunicamycin and pantomycin
2. Inhibition of fusion of embryonic muscle cells in culture by tunicamycin is prevented by leupeptin.
3. Possible involvement of a cell surface glycoprotein in the differentiation of skeletal myoblasts.
4. Changes in cell surface glycoproteins on non-differentiating L6 rat myoblasts selected for resistance to concanavalin A
5. Inhibition of myoblast fusion by the glucosidase inhibitor N-methyl-1-deoxynojirimycin, but not by the mannosidase inhibitor 1-deoxymannojirimycin
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1. Inhibitory Activity of Corn-Derived Bisamide Compounds against α-Glucosidase;Journal of Agricultural and Food Chemistry;2002-11-23
2. Molecular architecture of the lens fiber cell basal membrane complex;Journal of Cell Science;1999-07-01
3. Inhibitors of N-linked oligosaccharide processing glucosidases interfere with oligodendrocyte differentiation in culture;Journal of Neuroscience Research;1994-09-01
4. Differential expression of an endogenous mannose-binding protein R1 during muscle development and regeneration delineating its role in myoblast fusion;Glycobiology;1994
5. The importance of N-linked glycoproteins and dolichyl phosphate synthesis for fusion of L6 myoblasts;Biochemistry and Cell Biology;1992-06-01
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