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180 related items for PubMed ID: 2714443

  • 1. Stem bromelain: amino acid sequence and implications for weak binding of cystatin.
    Ritonja A, Rowan AD, Buttle DJ, Rawlings ND, Turk V, Barrett AJ.
    FEBS Lett; 1989 Apr 24; 247(2):419-24. PubMed ID: 2714443
    [Abstract] [Full Text] [Related]

  • 2. Amino acid sequences of the human kidney cathepsins H and L.
    Ritonja A, Popović T, Kotnik M, Machleidt W, Turk V.
    FEBS Lett; 1988 Feb 15; 228(2):341-5. PubMed ID: 3342889
    [Abstract] [Full Text] [Related]

  • 3. L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L.
    Barrett AJ, Kembhavi AA, Brown MA, Kirschke H, Knight CG, Tamai M, Hanada K.
    Biochem J; 1982 Jan 01; 201(1):189-98. PubMed ID: 7044372
    [Abstract] [Full Text] [Related]

  • 4. The cysteine proteinases of the pineapple plant.
    Rowan AD, Buttle DJ, Barrett AJ.
    Biochem J; 1990 Mar 15; 266(3):869-75. PubMed ID: 2327970
    [Abstract] [Full Text] [Related]

  • 5. Human cysteine proteinases and their protein inhibitors stefins, cystatins and kininogens.
    Turk V, Brzin J, Kotnik M, Lenarcic B, Popović T, Ritonja A, Trstenjak M, Begić-Odobasić L, Machleidt W.
    Biomed Biochim Acta; 1986 Mar 15; 45(11-12):1375-84. PubMed ID: 3495261
    [Abstract] [Full Text] [Related]

  • 6. Conserved cystatin segments as models for designing specific substrates and inhibitors of cysteine proteinases.
    Lalmanach G, Serveau C, Brillard-Bourdet M, Chagas JR, Mayer R, Juliano L, Gauthier F.
    J Protein Chem; 1995 Nov 15; 14(8):645-53. PubMed ID: 8747425
    [Abstract] [Full Text] [Related]

  • 7. Complete amino acid sequence of ananain and a comparison with stem bromelain and other plant cysteine proteases.
    Lee KL, Albee KL, Bernasconi RJ, Edmunds T.
    Biochem J; 1997 Oct 01; 327 ( Pt 1)(Pt 1):199-202. PubMed ID: 9355753
    [Abstract] [Full Text] [Related]

  • 8. The contribution of N-terminal region residues of cystatin A (stefin A) to the affinity and kinetics of inhibition of papain, cathepsin B, and cathepsin L.
    Estrada S, Pavlova A, Björk I.
    Biochemistry; 1999 Jun 01; 38(22):7339-45. PubMed ID: 10353845
    [Abstract] [Full Text] [Related]

  • 9. Synthetic domains of cystatins linked to enkephalins are novel inhibitors of brain cathepsins L/B.
    Marks N, Berg MJ, Makofske RC, Danho W.
    Peptides; 1990 Jun 01; 11(4):679-82. PubMed ID: 2235677
    [Abstract] [Full Text] [Related]

  • 10. Characterization by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases.
    Pol E, Olsson SL, Estrada S, Prasthofer TW, Björk I.
    Biochem J; 1995 Oct 01; 311 ( Pt 1)(Pt 1):275-82. PubMed ID: 7575465
    [Abstract] [Full Text] [Related]

  • 11. E-64 [L-trans-epoxysuccinyl-leucyl-amido(4-guanidino)butane] and related epoxides as inhibitors of cysteine proteinases.
    Barrett AJ, Kembhavi AA, Hanada K.
    Acta Biol Med Ger; 1981 Oct 01; 40(10-11):1513-7. PubMed ID: 7044005
    [Abstract] [Full Text] [Related]

  • 12. Hybrids of chicken cystatin with human kininogen domain 2 sequences exhibit novel inhibition of calpain, improved inhibition of actinidin and impaired inhibition of papain, cathepsin L and cathepsin B.
    Auerswald EA, Nägler DK, Gross S, Assfalg-Machleidt I, Stubbs MT, Eckerskorn C, Machleidt W, Fritz H.
    Eur J Biochem; 1996 Feb 01; 235(3):534-42. PubMed ID: 8654398
    [Abstract] [Full Text] [Related]

  • 13. Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases.
    Salvesen G, Parkes C, Abrahamson M, Grubb A, Barrett AJ.
    Biochem J; 1986 Mar 01; 234(2):429-34. PubMed ID: 3521586
    [Abstract] [Full Text] [Related]

  • 14. Structural basis for different inhibitory specificities of human cystatins C and D.
    Hall A, Ekiel I, Mason RW, Kasprzykowski F, Grubb A, Abrahamson M.
    Biochemistry; 1998 Mar 24; 37(12):4071-9. PubMed ID: 9521728
    [Abstract] [Full Text] [Related]

  • 15. The amino acid sequences, structure comparisons and inhibition kinetics of sheep cathepsin L and sheep stefin B.
    Ritonja A, Coetzer TH, Pike RN, Dennison C.
    Comp Biochem Physiol B Biochem Mol Biol; 1996 Jun 24; 114(2):193-8. PubMed ID: 8759291
    [Abstract] [Full Text] [Related]

  • 16. Interaction of cystatin C variants with papain and human cathepsins B, H and L.
    Cimerman N, Prebanda MT, Turk B, Popovic T, Dolenc I, Turk V.
    J Enzyme Inhib; 1999 Jun 24; 14(2):167-74. PubMed ID: 10445041
    [Abstract] [Full Text] [Related]

  • 17. Sequence homologies, hydrophobic profiles and secondary structures of cathepsins B, H and L: comparison with papain and actinidin.
    Dufour E.
    Biochimie; 1988 Oct 24; 70(10):1335-42. PubMed ID: 3148320
    [Abstract] [Full Text] [Related]

  • 18. Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C and chicken cystatin.
    Abrahamson M, Ritonja A, Brown MA, Grubb A, Machleidt W, Barrett AJ.
    J Biol Chem; 1987 Jul 15; 262(20):9688-94. PubMed ID: 3496337
    [Abstract] [Full Text] [Related]

  • 19. The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L.
    Estrada S, Nycander M, Hill NJ, Craven CJ, Waltho JP, Björk I.
    Biochemistry; 1998 May 19; 37(20):7551-60. PubMed ID: 9585570
    [Abstract] [Full Text] [Related]

  • 20. Thiol proteases. Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain.
    Kamphuis IG, Drenth J, Baker EN.
    J Mol Biol; 1985 Mar 20; 182(2):317-29. PubMed ID: 3889350
    [Abstract] [Full Text] [Related]

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