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10.1146/annurev-biochem-060713-035314

http://scihub22266oqcxt.onion/10.1146/annurev-biochem-060713-035314
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24606135!7851832!24606135
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suck abstract from ncbi

pmid24606135      Annu+Rev+Biochem 2014 ; 83 (ä): 129-57
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  • Demystifying heparan sulfate-protein interactions #MMPMID24606135
  • Xu D; Esko JD
  • Annu Rev Biochem 2014[]; 83 (ä): 129-57 PMID24606135show ga
  • Numerous proteins, including cytokines and chemokines, enzymes and enzyme inhibitors, extracellular matrix proteins, and membrane receptors, bind heparin. Although they are traditionally classified as heparin-binding proteins, under normal physiological conditions these proteins actually interact with the heparan sulfate chains of one or more membrane or extracellular proteoglycans. Thus, they are more appropriately classified as heparan sulfate-binding proteins (HSBPs). This review provides an overview of the various modes of interaction between heparan sulfate and HSBPs, emphasizing biochemical and structural insights that improve our understanding of the many biological functions of heparan sulfate.
  • |Animals[MESH]
  • |Binding Sites[MESH]
  • |Carbohydrates/chemistry[MESH]
  • |Extracellular Matrix/metabolism[MESH]
  • |Glucuronidase/chemistry[MESH]
  • |Heparitin Sulfate/*chemistry[MESH]
  • |Humans[MESH]
  • |Hydrogen Bonding[MESH]
  • |Ligands[MESH]
  • |Macromolecular Substances[MESH]
  • |Oligosaccharides/chemistry[MESH]
  • |Protein Binding[MESH]
  • |Protein Interaction Mapping[MESH]
  • |Protein Structure, Secondary[MESH]
  • |Proteins/*chemistry[MESH]


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