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Journal Abstract Search

716 related items for PubMed ID: 9169027

  • 1. Conformational preferences of a peptide corresponding to the major antigenic determinant of foot-and-mouth disease virus: implications for peptide-vaccine approaches.
    de Prat-Gay G.
    Arch Biochem Biophys; 1997 May 15; 341(2):360-9. PubMed ID: 9169027
    [Abstract] [Full Text] [Related]

  • 2. A CD strategy for the study of polypeptide folding/unfolding. A synthetic foot-and-mouth disease virus immunogenic peptide.
    Siligardi G, Drake AF, Mascagni P, Rowlands DJ, Brown F, Gibbons WA.
    Int J Pept Protein Res; 1991 Dec 15; 38(6):519-27. PubMed ID: 1726426
    [Abstract] [Full Text] [Related]

  • 3. Conformational flexibility in a highly mobile protein loop of foot-and-mouth disease virus: distinct structural requirements for integrin and antibody binding.
    Feliu JX, Benito A, Oliva B, Avilés FX, Villaverde A.
    J Mol Biol; 1998 Oct 23; 283(2):331-8. PubMed ID: 9769208
    [Abstract] [Full Text] [Related]

  • 4. Structural comparison between retro-inverso and parent peptides: molecular basis for the biological activity of a retro-inverso analogue of the immunodominant fragment of VP1 coat protein from foot-and-mouth disease virus.
    Carver JA, Esposito G, Viglino P, Fogolari F, Guichard G, Briand JP, Van Regenmortel MH, Brown F, Mascagni P.
    Biopolymers; 1997 Apr 15; 41(5):569-90. PubMed ID: 9095678
    [Abstract] [Full Text] [Related]

  • 5. Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop.
    Hewat EA, Verdaguer N, Fita I, Blakemore W, Brookes S, King A, Newman J, Domingo E, Mateu MG, Stuart DI.
    EMBO J; 1997 Apr 01; 16(7):1492-500. PubMed ID: 9130694
    [Abstract] [Full Text] [Related]

  • 6. [Synthesis and immunogenic properties of peptides--fragments of the immunodominant regions of the VP1 protein of the Asia-1 type of foot- and-mouth disease virus].
    Petrov VN, Rybakov SS, Petrova ON, Chepurkin AV, Gulenkin VM.
    Bioorg Khim; 1998 Dec 01; 24(12):899-905. PubMed ID: 10079947
    [Abstract] [Full Text] [Related]

  • 7. Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2.
    Itzhaki LS, Neira JL, Ruiz-Sanz J, de Prat Gay G, Fersht AR.
    J Mol Biol; 1995 Nov 24; 254(2):289-304. PubMed ID: 7490749
    [Abstract] [Full Text] [Related]

  • 8. Formation of immunogenic virus-like particles by inserting epitopes into surface-exposed regions of hamster polyomavirus major capsid protein.
    Gedvilaite A, Frömmel C, Sasnauskas K, Micheel B, Ozel M, Behrsing O, Staniulis J, Jandrig B, Scherneck S, Ulrich R.
    Virology; 2000 Jul 20; 273(1):21-35. PubMed ID: 10891404
    [Abstract] [Full Text] [Related]

  • 9. Flexibility of the major antigenic loop of foot-and-mouth disease virus bound to a Fab fragment of a neutralising antibody: structure and neutralisation.
    Verdaguer N, Schoehn G, Ochoa WF, Fita I, Brookes S, King A, Domingo E, Mateu MG, Stuart D, Hewat EA.
    Virology; 1999 Mar 15; 255(2):260-8. PubMed ID: 10069951
    [Abstract] [Full Text] [Related]

  • 10. Two peptide fragments G55-I72 and K97-A109 from staphylococcal nuclease exhibit different behaviors in conformational preferences for helix formation.
    Wang M, Shan L, Wang J.
    Biopolymers; 2006 Oct 15; 83(3):268-79. PubMed ID: 16767771
    [Abstract] [Full Text] [Related]

  • 11. [Antigenic structure of the foot-and-mouth virus. VI. Functional segments of the immunodominant region of the VP1 protein of foot-and-mouth virus strains O1K and A22].
    Gel'famov VM, Grechaninova LA, Kan ES, Iarov AV, Surovoĭ AIu, Vol'pina OM, Chepurkin AV, Ivanov VT.
    Bioorg Khim; 1991 May 15; 17(5):596-605. PubMed ID: 1722673
    [Abstract] [Full Text] [Related]

  • 12. Conformations of peptide fragments from the FK506 binding protein: comparison with the native and urea-unfolded states.
    Callihan DE, Logan TM.
    J Mol Biol; 1999 Feb 05; 285(5):2161-75. PubMed ID: 9925792
    [Abstract] [Full Text] [Related]

  • 13. Contribution of increased length and intact capping sequences to the conformational preference for helix in a 31-residue peptide from the C terminus of myohemerythrin.
    Reymond MT, Huo S, Duggan B, Wright PE, Dyson HJ.
    Biochemistry; 1997 Apr 29; 36(17):5234-44. PubMed ID: 9136885
    [Abstract] [Full Text] [Related]

  • 14. Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: evidence for stable native-like secondary structure in the unfolded state.
    Luisi DL, Wu WJ, Raleigh DP.
    J Mol Biol; 1999 Mar 26; 287(2):395-407. PubMed ID: 10080901
    [Abstract] [Full Text] [Related]

  • 15. Circular dichroism, molecular modeling, and serology indicate that the structural basis of antigenic variation in foot-and-mouth disease virus is alpha-helix formation.
    France LL, Piatti PG, Newman JF, Toth I, Gibbons WA, Brown F.
    Proc Natl Acad Sci U S A; 1994 Aug 30; 91(18):8442-6. PubMed ID: 8078900
    [Abstract] [Full Text] [Related]

  • 16. Native-like cyclic peptide models of a viral antigenic site: finding a balance between rigidity and flexibility.
    Valero ML, Camarero JA, Haack T, Mateu MG, Domingo E, Giralt E, Andreu D.
    J Mol Recognit; 2000 Aug 30; 13(1):5-13. PubMed ID: 10679891
    [Abstract] [Full Text] [Related]

  • 17. Conformational properties of five peptides corresponding to the entire sequence of glutathione transferase domain II.
    Dragani B, Cocco R, Principe DR, Paludi D, Aceto A.
    Arch Biochem Biophys; 2001 May 01; 389(1):15-21. PubMed ID: 11370666
    [Abstract] [Full Text] [Related]

  • 18. Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide.
    Petit MC, Benkirane N, Guichard G, Du AP, Marraud M, Cung MT, Briand JP, Muller S.
    J Biol Chem; 1999 Feb 05; 274(6):3686-92. PubMed ID: 9920919
    [Abstract] [Full Text] [Related]

  • 19. Local interactions drive the formation of nonnative structure in the denatured state of human alpha-lactalbumin: a high resolution structural characterization of a peptide model in aqueous solution.
    Demarest SJ, Hua Y, Raleigh DP.
    Biochemistry; 1999 Jun 01; 38(22):7380-7. PubMed ID: 10353850
    [Abstract] [Full Text] [Related]

  • 20. Mimicry of viral epitopes with retro-inverso peptides of increased stability.
    Benkirane N, Guichard G, Briand JP, Muller S, Brown F, Van Regenmortel MH.
    Dev Biol Stand; 1996 Jun 01; 87():283-91. PubMed ID: 8854029
    [Abstract] [Full Text] [Related]

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