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156 related items for PubMed ID: 7917003

  • 1.
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  • 2. Secretion of active recombinant human tissue plasminogen activator derivatives in Escherichia coli.
    Manosroi J, Tayapiwatana C, Götz F, Werner RG, Manosroi A.
    Appl Environ Microbiol; 2001 Jun; 67(6):2657-64. PubMed ID: 11375177
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  • 3. Recombinant gene expression and 1H NMR characteristics of the kringle (2 + 3) supermodule: spectroscopic/functional individuality of plasminogen kringle domains.
    Söhndel S, Hu CK, Marti D, Affolter M, Schaller J, Llinás M, Rickli EE.
    Biochemistry; 1996 Feb 20; 35(7):2357-64. PubMed ID: 8652577
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  • 4. Domain-domain interactions in hybrids of tissue-type plasminogen activator and urokinase-type plasminogen activator.
    Bakker AH, Nieuwenbroek NM, Verheijen JH.
    Protein Eng; 1995 Dec 20; 8(12):1295-1302. PubMed ID: 8869642
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  • 5. The effector roles of kringle 1 and kringle 2 in the enzymatic properties of recombinant tissue-type plasminogen activator as revealed by generation of recombinant molecules containing each kringle linked to the protease domain.
    Rydzewski A, Castellino FJ.
    Arch Biochem Biophys; 1993 Jan 20; 300(1):472-82. PubMed ID: 8424682
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  • 6. Soluble expression of active recombinant human tissue plasminogen activator derivative (K2S) in Escherichia coli.
    Luo XG, Tian WJ, Ni M, Jing XL, Lv LH, Wang N, Jiang Y, Zhang TC.
    Pharm Biol; 2011 Jun 20; 49(6):653-7. PubMed ID: 21554008
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  • 7. A kringle-containing protease with plasminogen-like activity in the basal chordate Branchiostoma belcheri.
    Liu M, Zhang S.
    Biosci Rep; 2009 Sep 02; 29(6):385-95. PubMed ID: 19193194
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  • 8. Purification and characterization of tissue plasminogen activator kringle-2 domain expressed in Escherichia coli.
    Cleary S, Mulkerrin MG, Kelley RF.
    Biochemistry; 1989 Feb 21; 28(4):1884-91. PubMed ID: 2497771
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  • 9. The construction and expression of chimeric urokinase-type plasminogen activator genes containing kringle domains of human plasminogen.
    Boutaud A, Castellino FJ.
    Arch Biochem Biophys; 1993 Jun 21; 303(2):222-30. PubMed ID: 8512311
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  • 10. Role of tryptophan-63 of the kringle 2 domain of tissue-type plasminogen activator in its thermal stability, folding, and ligand binding properties.
    Chang Y, Zajicek J, Castellino FJ.
    Biochemistry; 1997 Jun 24; 36(25):7652-63. PubMed ID: 9201906
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  • 11. Recombinant variants of tissue-type plasminogen activator containing amino acid substitutions in the fibronectin finger-like domain and the kringle 1 domain.
    Yahara H, Matsumoto K, Maruyama H, Nagaoka T, Ikenaka Y, Yajima K, Fukao H, Ueshima S, Matsuo O.
    Thromb Haemost; 1994 Dec 24; 72(6):893-9. PubMed ID: 7740460
    [Abstract] [Full Text] [Related]

  • 12. Expression, purification, and characterization of the recombinant kringle 1 domain from tissue-type plasminogen activator.
    DeSerrano VS, Menhart N, Castellino FJ.
    Arch Biochem Biophys; 1992 Apr 24; 294(1):282-90. PubMed ID: 1550352
    [Abstract] [Full Text] [Related]

  • 13. High level expression of kringle 5 fragment of plasminogen in Pichia pastoris.
    Zhou Y, Zheng Q, Gao J, Gu J.
    Biotechnol Lett; 2005 Feb 24; 27(3):167-71. PubMed ID: 15717125
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  • 17. High-level secretion in Pichia pastoris and biochemical characterization of the recombinant kringle 2 domain of tissue-type plasminogen activator.
    Nilsen SL, DeFord ME, Prorok M, Chibber BA, Bretthauer RK, Castellino FJ.
    Biotechnol Appl Biochem; 1997 Feb 24; 25(1):63-74. PubMed ID: 9032937
    [Abstract] [Full Text] [Related]

  • 18. Lekteplase--a secreted tissue plasminogen activator derivative from Escherichia coli.
    Manosroi J, Tayapiwatana C, Manosroi A, Beer J, Bergemann K, Werner RG.
    Arzneimittelforschung; 2002 Feb 24; 52(1):60-6. PubMed ID: 11838275
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  • 19. Spatial orientation of tissue-type plasminogen activator bound at the melanoma cell surface.
    Bizik J, Trancikova D, Felnerova D, Verheijen JH, Vaheri A.
    Biochem Biophys Res Commun; 1997 Oct 09; 239(1):322-8. PubMed ID: 9345318
    [Abstract] [Full Text] [Related]

  • 20. Purification and characterization of a recombinant anti-angiogenic kringle fragment expressed in Escherichia coli: Purification and characterization of a tri-kringle fragment from human apolipoprotein (a) (kringle IV (9)-kringle IV (10)-kringle V).
    Kang KY, Kim SG, Kim WK, You HK, Kim YJ, Lee JH, Jung KH, Kim CW.
    Protein Expr Purif; 2006 Jan 09; 45(1):216-25. PubMed ID: 16260151
    [Abstract] [Full Text] [Related]

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