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Journal Abstract Search

165 related items for PubMed ID: 17202148

  • 1. Identification of the extracellular matrix (ECM) binding motifs of tissue inhibitor of metalloproteinases (TIMP)-3 and effective transfer to TIMP-1.
    Lee MH, Atkinson S, Murphy G.
    J Biol Chem; 2007 Mar 02; 282(9):6887-98. PubMed ID: 17202148
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  • 2. Threonine 98, the pivotal residue of tissue inhibitor of metalloproteinases (TIMP)-1 in metalloproteinase recognition.
    Lee MH, Rapti M, Knaüper V, Murphy G.
    J Biol Chem; 2004 Apr 23; 279(17):17562-9. PubMed ID: 14734567
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  • 3. Structural and functional insights into the interaction of sulfated glycosaminoglycans with tissue inhibitor of metalloproteinase-3 - A possible regulatory role on extracellular matrix homeostasis.
    Rother S, Samsonov SA, Hofmann T, Blaszkiewicz J, Köhling S, Moeller S, Schnabelrauch M, Rademann J, Kalkhof S, von Bergen M, Pisabarro MT, Scharnweber D, Hintze V.
    Acta Biomater; 2016 Nov 23; 45():143-154. PubMed ID: 27545813
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  • 4. Dissecting the interaction between tissue inhibitor of metalloproteinases-3 (TIMP-3) and low density lipoprotein receptor-related protein-1 (LRP-1): Development of a "TRAP" to increase levels of TIMP-3 in the tissue.
    Scilabra SD, Yamamoto K, Pigoni M, Sakamoto K, Müller SA, Papadopoulou A, Lichtenthaler SF, Troeberg L, Nagase H, Kadomatsu K.
    Matrix Biol; 2017 May 23; 59():69-79. PubMed ID: 27476612
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  • 5. 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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  • 8. TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2.
    Wang WM, Ge G, Lim NH, Nagase H, Greenspan DS.
    Biochem J; 2006 Sep 15; 398(3):515-9. PubMed ID: 16771712
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  • 9. Tissue inhibitors of metalloproteinases (TIMP) in invasion and proliferation.
    Henriet P, Blavier L, Declerck YA.
    APMIS; 1999 Jan 15; 107(1):111-9. PubMed ID: 10190287
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  • 10. The role of TIMPs in regulation of extracellular matrix proteolysis.
    Arpino V, Brock M, Gill SE.
    Matrix Biol; 2015 Jan 15; 44-46():247-54. PubMed ID: 25805621
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  • 13. 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
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  • 15. TIMP-3 facilitates binding of target metalloproteinases to the endocytic receptor LRP-1 and promotes scavenging of MMP-1.
    Carreca AP, Pravatà VM, Markham M, Bonelli S, Murphy G, Nagase H, Troeberg L, Scilabra SD.
    Sci Rep; 2020 Jul 21; 10(1):12067. PubMed ID: 32694578
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  • 18. TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5).
    Kashiwagi M, Tortorella M, Nagase H, Brew K.
    J Biol Chem; 2001 Apr 20; 276(16):12501-4. PubMed ID: 11278243
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  • 19. Functional characterization of tissue inhibitor of metalloproteinase-1 (TIMP-1) N- and C-terminal domains during Xenopus laevis development.
    Nieuwesteeg MA, Willson JA, Cepeda M, Fox MA, Damjanovski S.
    ScientificWorldJournal; 2014 Apr 20; 2014():467907. PubMed ID: 24616631
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  • 20. TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix.
    Yu WH, Yu S, Meng Q, Brew K, Woessner JF.
    J Biol Chem; 2000 Oct 06; 275(40):31226-32. PubMed ID: 10900194
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