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Journal Abstract Search


160 related items for PubMed ID: 7571409

  • 1. The role of individual oligosaccharide chains in the activities of the HN glycoprotein of Newcastle disease virus.
    McGinnes LW, Morrison TG.
    Virology; 1995 Oct 01; 212(2):398-410. PubMed ID: 7571409
    [Abstract] [Full Text] [Related]

  • 2. The role of the individual cysteine residues in the formation of the mature, antigenic HN protein of Newcastle disease virus.
    McGinnes LW, Morrison TG.
    Virology; 1994 May 01; 200(2):470-83. PubMed ID: 8178436
    [Abstract] [Full Text] [Related]

  • 3. Glycosylation within an antigenic site on the HN glycoprotein of Newcastle disease virus interferes with its role in the promotion of membrane fusion.
    Deng R, Wang Z, Glickman RL, Iorio RM.
    Virology; 1994 Oct 01; 204(1):17-26. PubMed ID: 7522370
    [Abstract] [Full Text] [Related]

  • 4. Carbohydrate modifications of the NDV fusion protein heptad repeat domains influence maturation and fusion activity.
    McGinnes L, Sergel T, Reitter J, Morrison T.
    Virology; 2001 May 10; 283(2):332-42. PubMed ID: 11336558
    [Abstract] [Full Text] [Related]

  • 5. The fusion promotion activity of the NDV HN protein does not correlate with neuraminidase activity.
    Sergel T, McGinnes LW, Morrison TG.
    Virology; 1993 Oct 10; 196(2):831-4. PubMed ID: 8372451
    [Abstract] [Full Text] [Related]

  • 6. Mutations in the transmembrane domain of the HN protein of Newcastle disease virus affect the structure and activity of the protein.
    McGinnes L, Sergel T, Morrison T.
    Virology; 1993 Sep 10; 196(1):101-10. PubMed ID: 8356787
    [Abstract] [Full Text] [Related]

  • 7. Role of cotranslational disulfide bond formation in the folding of the hemagglutinin-neuraminidase protein of Newcastle disease virus.
    McGinnes LW, Morrison TG.
    Virology; 1996 Oct 15; 224(2):465-76. PubMed ID: 8874507
    [Abstract] [Full Text] [Related]

  • 8. Conformationally sensitive antigenic determinants on the HN glycoprotein of Newcastle disease virus form with different kinetics.
    McGinnes LW, Morrison TG.
    Virology; 1994 Mar 15; 199(2):255-64. PubMed ID: 7510081
    [Abstract] [Full Text] [Related]

  • 9. Importance of serine 200 for functional activities of the hemagglutinin-neuraminidase protein of Newcastle Disease Virus.
    Fournier P, Zeng J, Von Der Lieth CW, Washburn B, Ahlert T, Schirrmacher V.
    Int J Oncol; 2004 Mar 15; 24(3):623-34. PubMed ID: 14767547
    [Abstract] [Full Text] [Related]

  • 10. Role of individual oligosaccharide chains in antigenic properties, intracellular transport, and biological activities of influenza C virus hemagglutinin-esterase protein.
    Sugahara K, Hongo S, Sugawara K, Li ZN, Tsuchiya E, Muraki Y, Matsuzaki Y, Nakamura K.
    Virology; 2001 Jun 20; 285(1):153-64. PubMed ID: 11414815
    [Abstract] [Full Text] [Related]

  • 11. Role of N-linked glycosylation of the human parainfluenza virus type 3 hemagglutinin-neuraminidase protein.
    Chu FL, Wen HL, Hou GH, Lin B, Zhang WQ, Song YY, Ren GJ, Sun CX, Li ZM, Wang Z.
    Virus Res; 2013 Jun 20; 174(1-2):137-47. PubMed ID: 23562646
    [Abstract] [Full Text] [Related]

  • 12. A single amino acid substitution in the haemagglutinin-neuraminidase protein of Newcastle disease virus results in increased fusion promotion and decreased neuraminidase activities without changes in virus pathotype.
    Estevez C, King DJ, Luo M, Yu Q.
    J Gen Virol; 2011 Mar 20; 92(Pt 3):544-51. PubMed ID: 21123551
    [Abstract] [Full Text] [Related]

  • 13. Amino acid substitutions in leucine zipper motif in the F-specific domain of human parainfluenza virus 3 HN protein play important roles in the protein function.
    Zhang W, Ren G, Wu B, Liu X, Wang G, Song Y, Xu H, Wen H, Wang Z.
    Intervirology; 2008 Mar 20; 51(5):311-21. PubMed ID: 19018146
    [Abstract] [Full Text] [Related]

  • 14. The attachment function of the Newcastle disease virus hemagglutinin-neuraminidase protein can be separated from fusion promotion by mutation.
    Sergel T, McGinnes LW, Peeples ME, Morrison TG.
    Virology; 1993 Apr 20; 193(2):717-26. PubMed ID: 8384752
    [Abstract] [Full Text] [Related]

  • 15. 'a'-Position-mutated and G4-mutated hemagglutinin-neuraminidase proteins of Newcastle disease virus impair fusion and hemagglutinin-neuraminidase-fusion interaction by different mechanisms.
    Chu FL, Wen HL, Zhang WQ, Lin B, Zhang Y, Sun CX, Ren GJ, Song YY, Wang Z.
    Intervirology; 2013 Apr 20; 56(1):27-36. PubMed ID: 23038058
    [Abstract] [Full Text] [Related]

  • 16. Loss of N-linked glycosylation from the hemagglutinin-neuraminidase protein alters virulence of Newcastle disease virus.
    Panda A, Elankumaran S, Krishnamurthy S, Huang Z, Samal SK.
    J Virol; 2004 May 20; 78(10):4965-75. PubMed ID: 15113876
    [Abstract] [Full Text] [Related]

  • 17. Disulfide bond formation is a determinant of glycosylation site usage in the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.
    McGinnes LW, Morrison TG.
    J Virol; 1997 Apr 20; 71(4):3083-9. PubMed ID: 9060670
    [Abstract] [Full Text] [Related]

  • 18. [Study on functions of N-carbohydrate chains in human parainfluenza virus type 3 hemagglutinin-neuraminidase protein].
    Chu FL, Wen HL, Hou GH, Lin B, Zhang WQ, Song YY, Ren GJ, Sun CX, Li ZM, Wang ZY.
    Bing Du Xue Bao; 2013 Sep 20; 29(5):500-8. PubMed ID: 24386838
    [Abstract] [Full Text] [Related]

  • 19. High cell surface expression of Newcastle disease virus proteins via replicon vectors demonstrates syncytia forming activity of F and fusion promotion activity of HN molecules.
    Zeng J, Fournier P, Schirrmacher V.
    Int J Oncol; 2004 Aug 20; 25(2):293-302. PubMed ID: 15254725
    [Abstract] [Full Text] [Related]

  • 20. Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion.
    Deng R, Wang Z, Mahon PJ, Marinello M, Mirza A, Iorio RM.
    Virology; 1999 Jan 05; 253(1):43-54. PubMed ID: 9887317
    [Abstract] [Full Text] [Related]


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