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Journal Abstract Search

131 related items for PubMed ID: 10415716

  • 1. Engineering of selective TIMPs.
    Nagase H, Meng Q, Malinovskii V, Huang W, Chung L, Bode W, Maskos K, Brew K.
    Ann N Y Acad Sci; 1999 Jun 30; 878():1-11. PubMed ID: 10415716
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  • 2. Residue 2 of TIMP-1 is a major determinant of affinity and specificity for matrix metalloproteinases but effects of substitutions do not correlate with those of the corresponding P1' residue of substrate.
    Meng Q, Malinovskii V, Huang W, Hu Y, Chung L, Nagase H, Bode W, Maskos K, Brew K.
    J Biol Chem; 1999 Apr 09; 274(15):10184-9. PubMed ID: 10187802
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  • 3. Mutational study of the amino-terminal domain of human tissue inhibitor of metalloproteinases 1 (TIMP-1) locates an inhibitory region for matrix metalloproteinases.
    Huang W, Meng Q, Suzuki K, Nagase H, Brew K.
    J Biol Chem; 1997 Aug 29; 272(35):22086-91. PubMed ID: 9268350
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  • 4. Unveiling the surface epitopes that render tissue inhibitor of metalloproteinase-1 inactive against membrane type 1-matrix metalloproteinase.
    Lee MH, Rapti M, Murphy G.
    J Biol Chem; 2003 Oct 10; 278(41):40224-30. PubMed ID: 12869573
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  • 17. Drosophila TIMP is a potent inhibitor of MMPs and TACE: similarities in structure and function to TIMP-3.
    Wei S, Xie Z, Filenova E, Brew K.
    Biochemistry; 2003 Oct 28; 42(42):12200-7. PubMed ID: 14567681
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  • 18. Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme.
    Stracke JO, Hutton M, Stewart M, Pendás AM, Smith B, López-Otin C, Murphy G, Knäuper V.
    J Biol Chem; 2000 May 19; 275(20):14809-16. PubMed ID: 10809722
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  • 20. Total conversion of tissue inhibitor of metalloproteinase (TIMP) for specific metalloproteinase targeting: fine-tuning TIMP-4 for optimal inhibition of tumor necrosis factor-{alpha}-converting enzyme.
    Lee MH, Rapti M, Murphy G.
    J Biol Chem; 2005 Apr 22; 280(16):15967-75. PubMed ID: 15713681
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