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Journal Abstract Search

215 related items for PubMed ID: 17660250

  • 1. Constraining specificity in the N-domain of tissue inhibitor of metalloproteinases-1; gelatinase-selective inhibitors.
    Hamze AB, Wei S, Bahudhanapati H, Kota S, Acharya KR, Brew K.
    Protein Sci; 2007 Sep; 16(9):1905-13. PubMed ID: 17660250
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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. Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition.
    Raeeszadeh-Sarmazdeh M, Greene KA, Sankaran B, Downey GP, Radisky DC, Radisky ES.
    J Biol Chem; 2019 Jun 14; 294(24):9476-9488. PubMed ID: 31040180
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  • 4. Protein engineering of the tissue inhibitor of metalloproteinase 1 (TIMP-1) inhibitory domain. In search of selective matrix metalloproteinase inhibitors.
    Wei S, Chen Y, Chung L, Nagase H, Brew K.
    J Biol Chem; 2003 Mar 14; 278(11):9831-4. PubMed ID: 12515831
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  • 7. 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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  • 8. 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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  • 11. Matrix metalloproteinase-10/TIMP-2 structure and analyses define conserved core interactions and diverse exosite interactions in MMP/TIMP complexes.
    Batra J, Soares AS, Mehner C, Radisky ES.
    PLoS One; 2013 Oct 10; 8(9):e75836. PubMed ID: 24073280
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  • 12. Dynamic interdomain interactions contribute to the inhibition of matrix metalloproteinases by tissue inhibitors of metalloproteinases.
    Remacle AG, Shiryaev SA, Radichev IA, Rozanov DV, Stec B, Strongin AY.
    J Biol Chem; 2011 Jun 10; 286(23):21002-12. PubMed ID: 21518756
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  • 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
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  • 17. Engineering of tissue inhibitor of metalloproteinases TIMP-1 for fine discrimination between closely related stromelysins MMP-3 and MMP-10.
    Raeeszadeh-Sarmazdeh M, Coban M, Mahajan S, Hockla A, Sankaran B, Downey GP, Radisky DC, Radisky ES.
    J Biol Chem; 2022 Mar 29; 298(3):101654. PubMed ID: 35101440
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