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July 1, 1991Journal of Biological ChemistryOpen Access

Five type I modules of fibronectin form a functional unit that binds to fibroblasts and Staphylococcus aureus

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Authors

JSJane SottileAlbany State UniversityJSJean E. SchwarzbauerPrinceton UniversityJSJane E. SelegueUniversity of Wisconsin–Madison

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Sottile et al. (1991) studied this question.

synapsesocial.com/papers/6a78ea6eb9c8f88091f9a76bhttps://doi.org/10.1016/s0021-9258(18)98769-7
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Binding of soluble form of fibroblast surface protein, fibronectin, to collagen1977 · 1,955 citations
  2. 2On the interaction of the finger and the kringle-2 domain of tissue-type plasminogen activator with fibrin. Inhibition of kringle-2 binding to fibrin by epsilon-amino caproic acid.1986 · 242 citations
  3. 3DNA sequencing with chain-terminating inhibitors1977 · 69,501 citations
  4. 4Interaction of the 70,000-mol-wt amino-terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts.1985 · 341 citations