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Extended N-Sulfated Domains Reside at the Nonreducing End of Heparan Sulfate Chains
Heparan sulfate (HS) serves as a cell-surface co-receptor for growth factors, morphogens, and chemokines. These HS and protein binding events depend on the fine structure and distribution of domains along an HS chain. A given domain can vary in terms of uronic acid epimer, N- and O-sulfate, and N-ac...
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| Autori principali: | , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Biochemistry and Molecular Biology
2010
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2881759/ https://ncbi.nlm.nih.gov/pubmed/20363743 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.101592 |
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