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Journal Abstract Search

163 related items for PubMed ID: 19193644

  • 21. The substrate specificities of endo-beta-N-acetylglucosaminidases CII and H.
    Tai T, Yamashita K, Kobata A.
    Biochem Biophys Res Commun; 1977 Sep 09; 78(1):434-41. PubMed ID: 199169
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  • 22. Sialidases From Clostridium perfringens and Their Inhibitors.
    Wang YH.
    Front Cell Infect Microbiol; 2019 Sep 09; 9():462. PubMed ID: 31998664
    [Abstract] [Full Text] [Related]

  • 23. Endo-beta-N-acetylglucosaminidases acting on carbohydrate moieties of glycoproteins: purification and properties of the two enzymes with different specificities from Clostridium perfringens.
    Ito S, Muramatsu T, Kobata A.
    Arch Biochem Biophys; 1975 Nov 09; 171(1):78-86. PubMed ID: 242275
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  • 24. Diverse modes of galacto-specific carbohydrate recognition by a family 31 glycoside hydrolase from Clostridium perfringens.
    Grondin JM, Duan D, Kirlin AC, Abe KT, Chitayat S, Spencer HL, Spencer C, Campigotto A, Houliston S, Arrowsmith CH, Allingham JS, Boraston AB, Smith SP.
    PLoS One; 2017 Nov 09; 12(2):e0171606. PubMed ID: 28158290
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  • 27. Mechanical Stability of a High-Affinity Toxin Anchor from the Pathogen Clostridium perfringens.
    Milles LF, Bayer EA, Nash MA, Gaub HE.
    J Phys Chem B; 2017 Apr 20; 121(15):3620-3625. PubMed ID: 27991799
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  • 29. Molecular genetic analysis of the nagH gene encoding a hyaluronidase of Clostridium perfringens.
    Canard B, Garnier T, Saint-Joanis B, Cole ST.
    Mol Gen Genet; 1994 Apr 20; 243(2):215-24. PubMed ID: 8177218
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  • 30. Structural basis of cellulosome efficiency explored by small angle X-ray scattering.
    Hammel M, Fierobe HP, Czjzek M, Kurkal V, Smith JC, Bayer EA, Finet S, Receveur-Bréchot V.
    J Biol Chem; 2005 Nov 18; 280(46):38562-8. PubMed ID: 16157599
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  • 32. Clostridium perfringens iota-toxin, ADP-ribosyltransferase: structure and mechanism of action.
    Sakurai J, Nagahama M, Hisatsune J, Katunuma N, Tsuge H.
    Adv Enzyme Regul; 2003 Nov 18; 43():361-77. PubMed ID: 12791397
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  • 35. Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens iota-toxin.
    Tsuge H, Nagahama M, Nishimura H, Hisatsune J, Sakaguchi Y, Itogawa Y, Katunuma N, Sakurai J.
    J Mol Biol; 2003 Jan 17; 325(3):471-83. PubMed ID: 12498797
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  • 36. Crystal structure of the catalytic domain of Clostridium perfringens neuraminidase in complex with a non-carbohydrate-based inhibitor, 2-(cyclohexylamino)ethanesulfonic acid.
    Lee Y, Youn HS, Lee JG, An JY, Park KR, Kang JY, Ryu YB, Jin MS, Park KH, Eom SH.
    Biochem Biophys Res Commun; 2017 Apr 29; 486(2):470-475. PubMed ID: 28315686
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  • 37. The structure of hyperthermophilic β-N-acetylglucosaminidase reveals a novel dimer architecture associated with the active site.
    Mine S, Kado Y, Watanabe M, Fukuda Y, Abe Y, Ueda T, Kawarabayasi Y, Inoue T, Ishikawa K.
    FEBS J; 2014 Nov 29; 281(22):5092-103. PubMed ID: 25227262
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  • 39. X-ray structure of Clostridium perfringens sortase B cysteine transpeptidase.
    Tamai E, Sekiya H, Maki J, Nariya H, Yoshida H, Kamitori S.
    Biochem Biophys Res Commun; 2017 Nov 25; 493(3):1267-1272. PubMed ID: 28962862
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  • 40. Structural and biochemical characterization of the Clostridium perfringens autolysin catalytic domain.
    Tamai E, Sekiya H, Goda E, Makihata N, Maki J, Yoshida H, Kamitori S.
    FEBS Lett; 2017 Jan 25; 591(1):231-239. PubMed ID: 27926788
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