Results 221 to 230 of about 23,189 (236)
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Disulfide-bonded aggregates of heparan sulfate proteoglycans

Biochemistry, 1984
Heparan sulfate proteoglycans have been isolated from Swiss mouse 3T3 cells by using two nondegradative techniques: extraction with 4 M guanidine or 2.5% 1-butanol. These proteoglycans were separated from copurifying chondroitin sulfate proteoglycans by using ion-exchange chromatography on DEAE-cellulose in the presence of 2 M urea.
L J, Lowe-Krentz, J M, Keller
openaire   +2 more sources

Heparan sulfate proteoglycans and the emergence of neuronal connectivity

Current Opinion in Neurobiology, 2006
With the identification of the molecular determinants of neuronal connectivity, our understanding of the extracellular information that controls axon guidance and synapse formation has evolved from single factors towards the complexity that neurons face in a living organism.
David, Van Vactor   +2 more
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Autoantibodies to heparan sulfate proteoglycans

Autoimmunity Reviews, 2002
Yves, Renaudineau   +4 more
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Heparanases: endoglycosidases that degrade heparan sulfate proteoglycans

Glycobiology, 2001
Heparanases are endoglycosidases that cleave the heparan sulfate glycosaminoglycans from proteoglycan core proteins and degrade them to small oligosaccharides. Inside cells, these enzymes are important for the normal catabolism of heparan sulfate proteoglycans (HSPGs), generating glycosaminoglycan fragments that are then transported to lysosomes and ...
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Structural and Functional Diversity of the Heparan Sulfate Proteoglycans

1992
Several enzymes, cell adhesion molecules, growth factors, proteinase inhibitors and extracellular matrix components possess heparin-binding domains, and are profoundly affected in their reactivities with third parties in the presence of this glycosaminoglycan. Heparin, e.g.
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BIOLOGICAL SIGNIFICANCE OF HEPARAN SULFATE PROTEOGLYCANS*

Annals of the New York Academy of Sciences, 1982
V, Buonassisi, P, Colburn
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Cell surface heparan sulfate proteoglycans and lipoprotein metabolism

Cellular and Molecular Life Sciences, 1999
Svein O Kolset, M Salmivirta
exaly  

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