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10.1002/cmdc.201700620

http://scihub22266oqcxt.onion/10.1002/cmdc.201700620
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C5895483!5895483 !29160016
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suck abstract from ncbi


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pmid29160016
      ChemMedChem 2018 ; 13 (7 ): 648-661
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  • Synthetic Oligosaccharide Libraries and Microarray Technology: A Powerful Combination for the Success of Current Glycosaminoglycan Interactomics #MMPMID29160016
  • Pomin VH ; Wang X
  • ChemMedChem 2018[Apr]; 13 (7 ): 648-661 PMID29160016 show ga
  • Glycosaminoglycans (GAGs) are extracellular matrix and/or cell-surface sulfated glycans crucial to the regulation of various signaling proteins, the functions of which are essential in many pathophysiological systems. Because structural heterogeneity is high in GAG chains and purification is difficult, the use of structurally defined GAG oligosaccharides from natural sources as molecular models in both biophysical and pharmacological assays is limited. To overcome this obstacle, GAG-like oligosaccharides of well-defined structures are currently being synthesized by chemical and/or enzymatic means in many research groups around the world. These synthetic GAG oligosaccharides serve as useful molecular tools in studies of GAG-protein interactions. In this review, besides discussing the commonest routes used for the synthesis of GAG oligosaccharides, we also survey some libraries of these synthetic models currently available for research and discuss their activities in interaction studies with functional proteins, especially through the microarray approach.
  • |Carbohydrate Sequence [MESH]
  • |Glycomics/*methods [MESH]
  • |Glycosaminoglycans/*metabolism [MESH]
  • |Humans [MESH]
  • |Microarray Analysis/methods [MESH]
  • |Oligosaccharides/chemical synthesis/*metabolism [MESH]
  • |Protein Binding [MESH]
  • |Proteins/*metabolism [MESH]
  • |Proteomics/*methods [MESH]


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