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May 8, 2002Biochemical JournalOpen Access

Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-α-converting enzyme

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Authors

MLMeng‐Huee LeeVVVandana VermaKMK. Maskos

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Lee et al. (2002) studied this question.

synapsesocial.com/papers/6a930aface62e2ff0971fbaehttps://doi.org/10.1042/bj3640227
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Also Consider

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

  1. 1Different Domain Interactions Are Involved in the Binding of Tissue Inhibitors of Metalloproteinases to Stromelysin-1 and Gelatinase A1994 · 78 citations
  2. 2The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity1991 · 323 citations
  3. 3Shedding of c-Met is regulated by crosstalk between a G-protein coupled receptor and the EGF receptor and is mediated by a TIMP-3 sensitive metalloproteinase2001 · 105 citations
  4. 4Human myeloma cells shed the interleukin‐6 receptor: inhibition by tissue inhibitor of metalloproteinase‐3 and a hydroxamate‐based metalloproteinase inhibitor1998 · 91 citations