BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

113 related articles for article (PubMed ID: 20860624)

  • 1. Stefin A displaces the occluding loop of cathepsin B only by as much as required to bind to the active site cleft.
    Renko M; Požgan U; Majera D; Turk D
    FEBS J; 2010 Oct; 277(20):4338-45. PubMed ID: 20860624
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine.
    Sivaraman J; Nägler DK; Zhang R; Ménard R; Cygler M
    J Mol Biol; 2000 Jan; 295(4):939-51. PubMed ID: 10656802
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen.
    Podobnik M; Kuhelj R; Turk V; Turk D
    J Mol Biol; 1997 Sep; 271(5):774-88. PubMed ID: 9299326
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Grafting of features of cystatins C or B into the N-terminal region or second binding loop of cystatin A (stefin A) substantially enhances inhibition of cysteine proteinases.
    Pavlova A; Björk I
    Biochemistry; 2003 Sep; 42(38):11326-33. PubMed ID: 14503883
    [TBL] [Abstract][Full Text] [Related]  

  • 5. The occluding loop in cathepsin B defines the pH dependence of inhibition by its propeptide.
    Quraishi O; Nägler DK; Fox T; Sivaraman J; Cygler M; Mort JS; Storer AC
    Biochemistry; 1999 Apr; 38(16):5017-23. PubMed ID: 10213604
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases.
    Jenko S; Dolenc I; Guncar G; Dobersek A; Podobnik M; Turk D
    J Mol Biol; 2003 Feb; 326(3):875-85. PubMed ID: 12581647
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Molecular mechanism of inhibition of cysteine proteinases by their protein inhibitors: kinetic studies with natural and recombinant variants of cystatins and stefins.
    Machleidt W; Thiele U; Assfalg-Machleidt I; Förger D; Auerswald EA
    Biomed Biochim Acta; 1991; 50(4-6):613-20. PubMed ID: 1801731
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Major increase in endopeptidase activity of human cathepsin B upon removal of occluding loop contacts.
    Nägler DK; Storer AC; Portaro FC; Carmona E; Juliano L; Ménard R
    Biochemistry; 1997 Oct; 36(41):12608-15. PubMed ID: 9376367
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Quantitative evaluation of each catalytic subsite of cathepsin B for inhibitory activity based on inhibitory activity-binding mode relationship of epoxysuccinyl inhibitors by X-ray crystal structure analyses of complexes.
    Watanabe D; Yamamoto A; Tomoo K; Matsumoto K; Murata M; Kitamura K; Ishida T
    J Mol Biol; 2006 Oct; 362(5):979-93. PubMed ID: 16950396
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Displacement of the occluding loop by the parasite protein, chagasin, results in efficient inhibition of human cathepsin B.
    Redzynia I; Ljunggren A; Abrahamson M; Mort JS; Krupa JC; Jaskolski M; Bujacz G
    J Biol Chem; 2008 Aug; 283(33):22815-25. PubMed ID: 18515357
    [TBL] [Abstract][Full Text] [Related]  

  • 11. The crystal structure of human procathepsin K.
    LaLonde JM; Zhao B; Janson CA; D'Alessio KJ; McQueney MS; Orsini MJ; Debouck CM; Smith WW
    Biochemistry; 1999 Jan; 38(3):862-9. PubMed ID: 9893980
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases.
    Pol E; Björk I
    Protein Sci; 2001 Sep; 10(9):1729-38. PubMed ID: 11514663
    [TBL] [Abstract][Full Text] [Related]  

  • 13. 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; 38(22):7339-45. PubMed ID: 10353845
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Role of the occluding loop in cathepsin B activity.
    Illy C; Quraishi O; Wang J; Purisima E; Vernet T; Mort JS
    J Biol Chem; 1997 Jan; 272(2):1197-202. PubMed ID: 8995421
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Importance of the second binding loop and the C-terminal end of cystatin B (stefin B) for inhibition of cysteine proteinases.
    Pol E; Björk I
    Biochemistry; 1999 Aug; 38(32):10519-26. PubMed ID: 10441148
    [TBL] [Abstract][Full Text] [Related]  

  • 16. The occluding loop of cathepsin B prevents its effective inhibition by human kininogens.
    Naudin C; Lecaille F; Chowdhury S; Krupa JC; Purisima E; Mort JS; Lalmanach G
    J Mol Biol; 2010 Jul; 400(5):1022-35. PubMed ID: 20538006
    [TBL] [Abstract][Full Text] [Related]  

  • 17. The role of the second binding loop of the cysteine protease inhibitor, cystatin A (stefin A), in stabilizing complexes with target proteases is exerted predominantly by Leu73.
    Pavlova A; Björk I
    Eur J Biochem; 2002 Nov; 269(22):5649-58. PubMed ID: 12423365
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Distinct properties of prohormone thiol protease (PTP) compared to cathepsins B, L, and H: evidence for PTP as a novel cysteine protease.
    Azaryan AV; Hook VY
    Arch Biochem Biophys; 1994 Oct; 314(1):171-7. PubMed ID: 7944391
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Regulation of cathepsin B activity by 2A2 monoclonal antibody.
    Mirković B; Premzl A; Hodnik V; Doljak B; Jevnikar Z; Anderluh G; Kos J
    FEBS J; 2009 Sep; 276(17):4739-51. PubMed ID: 19656187
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Crystal structure of the parasite protease inhibitor chagasin in complex with a host target cysteine protease.
    Ljunggren A; Redzynia I; Alvarez-Fernandez M; Abrahamson M; Mort JS; Krupa JC; Jaskolski M; Bujacz G
    J Mol Biol; 2007 Aug; 371(1):137-53. PubMed ID: 17561110
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 6.