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PUBMED FOR HANDHELDS

Journal Abstract Search


175 related items for PubMed ID: 28683915

  • 1. Collagenolytic Matrix Metalloproteinase Structure-Function Relationships: Insights From Molecular Dynamics Studies.
    Karabencheva-Christova TG, Christov CZ, Fields GB.
    Adv Protein Chem Struct Biol; 2017; 109():1-24. PubMed ID: 28683915
    [Abstract] [Full Text] [Related]

  • 2. Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis.
    Bertini I, Fragai M, Luchinat C, Melikian M, Toccafondi M, Lauer JL, Fields GB.
    J Am Chem Soc; 2012 Feb 01; 134(4):2100-10. PubMed ID: 22239621
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  • 3. Effects of Mutations on Structure-Function Relationships of Matrix Metalloproteinase-1.
    Singh W, Fields GB, Christov CZ, Karabencheva-Christova TG.
    Int J Mol Sci; 2016 Oct 14; 17(10):. PubMed ID: 27754420
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  • 5. Biophysical studies of matrix metalloproteinase/triple-helix complexes.
    Fields GB.
    Adv Protein Chem Struct Biol; 2014 Oct 14; 97():37-48. PubMed ID: 25458354
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  • 6. Collagenolytic Matrix Metalloproteinase Activities toward Peptomeric Triple-Helical Substrates.
    Stawikowski MJ, Stawikowska R, Fields GB.
    Biochemistry; 2015 May 19; 54(19):3110-21. PubMed ID: 25897652
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  • 7. Molecular dynamics simulation study on the interaction of collagen-like peptides with gelatinase-A (MMP-2).
    Azhagiya Singam ER, Rajapandian V, Subramanian V.
    Biopolymers; 2014 Jul 19; 101(7):779-94. PubMed ID: 24374600
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  • 8. A synergy between the catalytic and structural Zn(II) ions and the enzyme and substrate dynamics underlies the structure-function relationships of matrix metalloproteinase collagenolysis.
    Varghese A, Chaturvedi SS, Fields GB, Karabencheva-Christova TG.
    J Biol Inorg Chem; 2021 Aug 19; 26(5):583-597. PubMed ID: 34228191
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  • 9. Examination of matrix metalloproteinase-1 in solution: a preference for the pre-collagenolysis state.
    Cerofolini L, Fields GB, Fragai M, Geraldes CFGC, Luchinat C, Parigi G, Ravera E, Svergun DI, Teixeira JMC.
    J Biol Chem; 2013 Oct 18; 288(42):30659-30671. PubMed ID: 24025334
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  • 10. Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity.
    Lauer-Fields JL, Chalmers MJ, Busby SA, Minond D, Griffin PR, Fields GB.
    J Biol Chem; 2009 Sep 04; 284(36):24017-24. PubMed ID: 19574232
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  • 11. The interface between catalytic and hemopexin domains in matrix metalloproteinase-1 conceals a collagen binding exosite.
    Arnold LH, Butt LE, Prior SH, Read CM, Fields GB, Pickford AR.
    J Biol Chem; 2011 Dec 30; 286(52):45073-82. PubMed ID: 22030392
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  • 12. Structural insights into triple-helical collagen cleavage by matrix metalloproteinase 1.
    Manka SW, Carafoli F, Visse R, Bihan D, Raynal N, Farndale RW, Murphy G, Enghild JJ, Hohenester E, Nagase H.
    Proc Natl Acad Sci U S A; 2012 Jul 31; 109(31):12461-6. PubMed ID: 22761315
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  • 13. Importance of the Linker Region in Matrix Metalloproteinase-1 Domain Interactions.
    Singh W, Fields GB, Christov CZ, Karabencheva-Christova TG.
    RSC Adv; 2016 Jan 01; 6(28):23223-23232. PubMed ID: 26998255
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  • 17. Transient collagen triple helix binding to a key metalloproteinase in invasion and development.
    Zhao Y, Marcink TC, Sanganna Gari RR, Marsh BP, King GM, Stawikowska R, Fields GB, Van Doren SR.
    Structure; 2015 Feb 03; 23(2):257-69. PubMed ID: 25651059
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  • 18. Identification of an Electrostatic Ruler Motif for Sequence-Specific Binding of Collagenase to Collagen.
    Subramanian SR, Singam ER, Berinski M, Subramanian V, Wade RC.
    J Phys Chem B; 2016 Aug 25; 120(33):8580-9. PubMed ID: 27245212
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  • 19. Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites.
    Overall CM.
    Mol Biotechnol; 2002 Sep 25; 22(1):51-86. PubMed ID: 12353914
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  • 20. Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1).
    Bertini I, Fragai M, Luchinat C, Melikian M, Mylonas E, Sarti N, Svergun DI.
    J Biol Chem; 2009 May 08; 284(19):12821-8. PubMed ID: 19282283
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