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156 related items for PubMed ID: 7952654

  • 1. Structure-function relationships in the tissue inhibitors of metalloproteinases.
    Willenbrock F, Murphy G.
    Am J Respir Crit Care Med; 1994 Dec; 150(6 Pt 2):S165-70. PubMed ID: 7952654
    [Abstract] [Full Text] [Related]

  • 2. Different domain interactions are involved in the binding of tissue inhibitors of metalloproteinases to stromelysin-1 and gelatinase A.
    Nguyen Q, Willenbrock F, Cockett MI, O'Shea M, Docherty AJ, Murphy G.
    Biochemistry; 1994 Mar 01; 33(8):2089-95. PubMed ID: 8117665
    [Abstract] [Full Text] [Related]

  • 3. Tissue inhibitor of metalloproteinases-4 inhibits but does not support the activation of gelatinase A via efficient inhibition of membrane type 1-matrix metalloproteinase.
    Bigg HF, Morrison CJ, Butler GS, Bogoyevitch MA, Wang Z, Soloway PD, Overall CM.
    Cancer Res; 2001 May 01; 61(9):3610-8. PubMed ID: 11325829
    [Abstract] [Full Text] [Related]

  • 4. The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A.
    Willenbrock F, Crabbe T, Slocombe PM, Sutton CW, Docherty AJ, Cockett MI, O'Shea M, Brocklehurst K, Phillips IR, Murphy G.
    Biochemistry; 1993 Apr 27; 32(16):4330-7. PubMed ID: 8476862
    [Abstract] [Full Text] [Related]

  • 5. Inhibition of human stromelysin by peptides based on the N-terminal domain of tissue inhibitor of metalloproteinases-1.
    Hanglow AC, Lugo A, Walsky R, Visnick M, Coffey JW, Fotouhi N.
    Biochem Biophys Res Commun; 1994 Dec 15; 205(2):1156-63. PubMed ID: 7802645
    [Abstract] [Full Text] [Related]

  • 6. Human tissue inhibitor of metalloproteinases 3 interacts with both the N- and C-terminal domains of gelatinases A and B. Regulation by polyanions.
    Butler GS, Apte SS, Willenbrock F, Murphy G.
    J Biol Chem; 1999 Apr 16; 274(16):10846-51. PubMed ID: 10196161
    [Abstract] [Full Text] [Related]

  • 7. Sequence motifs of tissue inhibitor of metalloproteinases 2 (TIMP-2) determining progelatinase A (proMMP-2) binding and activation by membrane-type metalloproteinase 1 (MT1-MMP).
    Worley JR, Thompkins PB, Lee MH, Hutton M, Soloway P, Edwards DR, Murphy G, Knäuper V.
    Biochem J; 2003 Jun 15; 372(Pt 3):799-809. PubMed ID: 12630911
    [Abstract] [Full Text] [Related]

  • 8. Contribution of the C-terminal domain of metalloproteinases to binding by tissue inhibitor of metalloproteinases. C-terminal truncated stromelysin and matrilysin exhibit equally compromised binding affinities as compared to full-length stromelysin.
    Baragi VM, Fliszar CJ, Conroy MC, Ye QZ, Shipley JM, Welgus HG.
    J Biol Chem; 1994 Apr 29; 269(17):12692-7. PubMed ID: 8175679
    [Abstract] [Full Text] [Related]

  • 9. Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13.
    O'Shea M, Willenbrock F, Williamson RA, Cockett MI, Freedman RB, Reynolds JJ, Docherty AJ, Murphy G.
    Biochemistry; 1992 Oct 27; 31(42):10146-52. PubMed ID: 1420137
    [Abstract] [Full Text] [Related]

  • 10. TIMP-2: identification and characterization of a new member of the metalloproteinase inhibitor family.
    Stetler-Stevenson WG, Krutzsch HC, Liotta LA.
    Matrix Suppl; 1992 Oct 27; 1():299-306. PubMed ID: 1480041
    [Abstract] [Full Text] [Related]

  • 11. The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinase complex. Demonstration of the biochemical similarities of tissue inhibitor of metalloproteinases-2 and tissue inhibitor of metalloproteinases-1.
    Ward RV, Hembry RM, Reynolds JJ, Murphy G.
    Biochem J; 1991 Aug 15; 278 ( Pt 1)(Pt 1):179-87. PubMed ID: 1909113
    [Abstract] [Full Text] [Related]

  • 12. Dynamic characterisation of the netrin-like domain of human type 1 procollagen C-proteinase enhancer and comparison to the N-terminal domain of tissue inhibitor of metalloproteinases (TIMP).
    Williamson RA, Panagiotidou P, Mott JD, Howard MJ.
    Mol Biosyst; 2008 May 15; 4(5):417-25. PubMed ID: 18414739
    [Abstract] [Full Text] [Related]

  • 13. Structural features of the reprolysin atrolysin C and tissue inhibitors of metalloproteinases (TIMPs) interaction.
    Pinto AF, Terra RM, Guimarães JA, Kashiwagi M, Nagase H, Serrano SM, Fox JW.
    Biochem Biophys Res Commun; 2006 Sep 01; 347(3):641-8. PubMed ID: 16842758
    [Abstract] [Full Text] [Related]

  • 14. Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor.
    Fernandez-Catalan C, Bode W, Huber R, Turk D, Calvete JJ, Lichte A, Tschesche H, Maskos K.
    EMBO J; 1998 Sep 01; 17(17):5238-48. PubMed ID: 9724659
    [Abstract] [Full Text] [Related]

  • 15. Secreted inhibitors of metalloproteinases (IMPs) that are distinct from TIMP.
    Banda MJ, Howard EW, Herron GS, Apodaca G.
    Matrix Suppl; 1992 Sep 01; 1():294-8. PubMed ID: 1480040
    [Abstract] [Full Text] [Related]

  • 16. 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
    [Abstract] [Full Text] [Related]

  • 17. Activation of the 92-kDa gelatinase by stromelysin and 4-aminophenylmercuric acetate. Differential processing and stabilization of the carboxyl-terminal domain by tissue inhibitor of metalloproteinases (TIMP).
    Shapiro SD, Fliszar CJ, Broekelmann TJ, Mecham RP, Senior RM, Welgus HG.
    J Biol Chem; 1995 Mar 17; 270(11):6351-6. PubMed ID: 7890773
    [Abstract] [Full Text] [Related]

  • 18. The tissue metalloproteinase family and the inhibitor TIMP: a study using cDNAs and recombinant proteins.
    Docherty AJ, Murphy G.
    Ann Rheum Dis; 1990 Jun 17; 49 Suppl 1():469-79. PubMed ID: 2197998
    [Abstract] [Full Text] [Related]

  • 19. Metalloproteinase inhibition and erythroid potentiation are independent activities of tissue inhibitor of metalloproteinases-1.
    Chesler L, Golde DW, Bersch N, Johnson MD.
    Blood; 1995 Dec 15; 86(12):4506-15. PubMed ID: 8541540
    [Abstract] [Full Text] [Related]

  • 20. Tissue inhibitor of metalloproteinases (TIMP, aka EPA): structure, control of expression and biological functions.
    Denhardt DT, Feng B, Edwards DR, Cocuzzi ET, Malyankar UM.
    Pharmacol Ther; 1993 Sep 15; 59(3):329-41. PubMed ID: 8309995
    [Abstract] [Full Text] [Related]

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