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125 related items for PubMed ID: 8182052

  • 1. Two distinct types of cardiotoxin as revealed by the structure and activity relationship of their interaction with zwitterionic phospholipid dispersions.
    Chien KY, Chiang CM, Hseu YC, Vyas AA, Rule GS, Wu W.
    J Biol Chem; 1994 May 20; 269(20):14473-83. PubMed ID: 8182052
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  • 2. Fusion of sphingomyelin vesicles induced by proteins from Taiwan cobra (Naja naja atra) venom. Interactions of zwitterionic phospholipids with cardiotoxin analogues.
    Chien KY, Huang WN, Jean JH, Wu WG.
    J Biol Chem; 1991 Feb 15; 266(5):3252-9. PubMed ID: 1993698
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  • 3. Elucidation of the solution structure of cardiotoxin analogue V from the Taiwan cobra (Naja naja atra)--identification of structural features important for the lethal action of snake venom cardiotoxins.
    Jayaraman G, Kumar TK, Tsai CC, Srisailam S, Chou SH, Ho CL, Yu C.
    Protein Sci; 2000 Apr 15; 9(4):637-46. PubMed ID: 10794406
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  • 4. Conformational change and inactivation of membrane phospholipid-related activity of cardiotoxin V from Taiwan cobra venom at acidic pH.
    Chiang CM, Chien KY, Lin HJ, Lin JF, Yeh HC, Ho PL, Wu WG.
    Biochemistry; 1996 Jul 16; 35(28):9167-76. PubMed ID: 8703922
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  • 5. Delineating residues for haemolytic activities of snake venom cardiotoxin 1 from Naja naja as probed by molecular dynamics simulations and in vitro validations.
    Gorai B, Sivaraman T.
    Int J Biol Macromol; 2017 Feb 16; 95():1022-1036. PubMed ID: 27984143
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  • 7. Structures of heparin-derived tetrasaccharide bound to cobra cardiotoxins: heparin binding at a single protein site with diverse side chain interactions.
    Tjong SC, Chen TS, Huang WN, Wu WG.
    Biochemistry; 2007 Sep 04; 46(35):9941-52. PubMed ID: 17685633
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  • 8. Separation and structure-function studies of Taiwan cobra cardiotoxins.
    Lin SR, Chang LS, Chang KL.
    J Protein Chem; 2002 Feb 04; 21(2):81-6. PubMed ID: 11934278
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  • 9. Role of cationic residues in cytolytic activity: modification of lysine residues in the cardiotoxin from Naja nigricollis venom and correlation between cytolytic and antiplatelet activity.
    Kini RM, Evans HJ.
    Biochemistry; 1989 Nov 14; 28(23):9209-15. PubMed ID: 2513886
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  • 10. Differential binding to phospholipid bilayers modulates membrane-damaging activity of Naja naja atra cardiotoxins.
    Kao PH, Lin SR, Chang LS.
    Toxicon; 2009 Sep 01; 54(3):321-8. PubMed ID: 19450618
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  • 12. Interactions in red blood cells between fatty acids and either snake venom cardiotoxin or halothane.
    Fletcher JE, Jiang MS, Tripolitis L, Smith LA, Beech J.
    Toxicon; 1990 Sep 01; 28(6):657-67. PubMed ID: 2402762
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  • 13. Comparison of the hemolytic activity and solution structures of two snake venom cardiotoxin analogues which only differ in their N-terminal amino acid.
    Jang JY, Krishnaswamy T, Kumar S, Jayaraman G, Yang PW, Yu C.
    Biochemistry; 1997 Dec 02; 36(48):14635-41. PubMed ID: 9398182
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  • 16. Structural basis of membrane-induced cardiotoxin A3 oligomerization.
    Forouhar F, Huang WN, Liu JH, Chien KY, Wu WG, Hsiao CD.
    J Biol Chem; 2003 Jun 13; 278(24):21980-8. PubMed ID: 12660250
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  • 18. Membrane-bound conformation and phospholipid components modulate membrane-damaging activity of Taiwan cobra cardiotoxins.
    Kao PH, Lin SR, Wu MJ, Chang LS.
    Toxicon; 2009 Apr 13; 53(5):512-8. PubMed ID: 19673097
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  • 20. The role of the N-terminal leucine residue in snake venom cardiotoxin II (Naja naja atra).
    Wu CY, Chen WC, Ho CL, Chen ST, Wang KT.
    Biochem Biophys Res Commun; 1997 Apr 28; 233(3):713-6. PubMed ID: 9168920
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