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September 1, 2000Journal of Biological ChemistryOpen Access

Binding of the NG2 Proteoglycan to Kringle Domains Modulates the Functional Properties of Angiostatin and Plasmin(ogen)

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Authors

LGLothar GoretzkiScripps Research InstituteCLChristian R. LombardoUniversity of Buenos AiresWSWilliam B. StallcupSouthern Research Institute

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Goretzki et al. (2000) studied this question.

synapsesocial.com/papers/6a8bf3cbb676b7d1a2fb88c8https://doi.org/10.1074/jbc.m002290200
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Also Consider

Synapse has enriched 3 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Binding of the NG2 Proteoglycan to Type VI Collagen and Other Extracellular Matrix Molecules1996 · 194 citations
  2. 2High-affinity Binding of Basic Fibroblast Growth Factor and Platelet-derived Growth Factor-AA to the Core Protein of the NG2 Proteoglycan1999 · 208 citations
  3. 3PDGF α-receptor is unresponsive to PDGF-AA in aortic smooth muscle cells from the NG2 knockout mouse1999 · 152 citations