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Journal Abstract Search

143 related items for PubMed ID: 9698543

  • 1. P22 tailspike folding mutants revisited: effects on the thermodynamic stability of the isolated beta-helix domain.
    Schuler B, Seckler R.
    J Mol Biol; 1998 Aug 14; 281(2):227-34. PubMed ID: 9698543
    [Abstract] [Full Text] [Related]

  • 2. Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein.
    Schuler B, Fürst F, Osterroth F, Steinbacher S, Huber R, Seckler R.
    Proteins; 2000 Apr 01; 39(1):89-101. PubMed ID: 10737931
    [Abstract] [Full Text] [Related]

  • 3. Mechanism of phage P22 tailspike protein folding mutations.
    Danner M, Seckler R.
    Protein Sci; 1993 Nov 01; 2(11):1869-81. PubMed ID: 8268798
    [Abstract] [Full Text] [Related]

  • 4. Mutations that stabilize folding intermediates of phage P22 tailspike protein: folding in vivo and in vitro, stability, and structural context.
    Beissinger M, Lee SC, Steinbacher S, Reinemer P, Huber R, Yu MH, Seckler R.
    J Mol Biol; 1995 May 26; 249(1):185-94. PubMed ID: 7776371
    [Abstract] [Full Text] [Related]

  • 5. Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.
    Miller S, Schuler B, Seckler R.
    Protein Sci; 1998 Oct 26; 7(10):2223-32. PubMed ID: 9792111
    [Abstract] [Full Text] [Related]

  • 6. Invivo folding efficiencies for mutants of the P22 tailspike beta-helix protein correlate with predicted stability changes.
    Reich L, Becker M, Seckler R, Weikl TR.
    Biophys Chem; 2009 May 26; 141(2-3):186-92. PubMed ID: 19254821
    [Abstract] [Full Text] [Related]

  • 7. Side-chain specificity at three temperature-sensitive folding mutation sites of P22 tailspike protein.
    Lee SC, Yu MH.
    Biochem Biophys Res Commun; 1997 Apr 28; 233(3):857-62. PubMed ID: 9168948
    [Abstract] [Full Text] [Related]

  • 8. A reversibly unfolding fragment of P22 tailspike protein with native structure: the isolated beta-helix domain.
    Miller S, Schuler B, Seckler R.
    Biochemistry; 1998 Jun 23; 37(25):9160-8. PubMed ID: 9636063
    [Abstract] [Full Text] [Related]

  • 9. The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization.
    Kreisberg JF, Betts SD, Haase-Pettingell C, King J.
    Protein Sci; 2002 Apr 23; 11(4):820-30. PubMed ID: 11910025
    [Abstract] [Full Text] [Related]

  • 10. Formation of fibrous aggregates from a non-native intermediate: the isolated P22 tailspike beta-helix domain.
    Schuler B, Rachel R, Seckler R.
    J Biol Chem; 1999 Jun 25; 274(26):18589-96. PubMed ID: 10373469
    [Abstract] [Full Text] [Related]

  • 11. Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase.
    Haase-Pettingell C, King J.
    J Mol Biol; 1997 Mar 21; 267(1):88-102. PubMed ID: 9096209
    [Abstract] [Full Text] [Related]

  • 12. Characterization of the protrimer intermediate in the folding pathway of the interdigitated beta-helix tailspike protein.
    Benton CB, King J, Clark PL.
    Biochemistry; 2002 Apr 23; 41(16):5093-103. PubMed ID: 11955057
    [Abstract] [Full Text] [Related]

  • 13. Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain.
    Danner M, Fuchs A, Miller S, Seckler R.
    Eur J Biochem; 1993 Aug 01; 215(3):653-61. PubMed ID: 8354271
    [Abstract] [Full Text] [Related]

  • 14. Stalled folding mutants in the triple beta-helix domain of the phage P22 tailspike adhesin.
    Weigele PR, Haase-Pettingell C, Campbell PG, Gossard DC, King J.
    J Mol Biol; 2005 Dec 16; 354(5):1103-17. PubMed ID: 16289113
    [Abstract] [Full Text] [Related]

  • 15. The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain.
    Freiberg A, Morona R, Van den Bosch L, Jung C, Behlke J, Carlin N, Seckler R, Baxa U.
    J Biol Chem; 2003 Jan 17; 278(3):1542-8. PubMed ID: 12424253
    [Abstract] [Full Text] [Related]

  • 16. Folding and function of repetitive structure in the homotrimeric phage P22 tailspike protein.
    Seckler R.
    J Struct Biol; 1998 Jan 17; 122(1-2):216-22. PubMed ID: 9724623
    [Abstract] [Full Text] [Related]

  • 17. Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike.
    Lefebvre BG, Comolli NK, Gage MJ, Robinson AS.
    Protein Sci; 2004 Jun 17; 13(6):1538-46. PubMed ID: 15133163
    [Abstract] [Full Text] [Related]

  • 18. Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity.
    Baxa U, Steinbacher S, Weintraub A, Huber R, Seckler R.
    J Mol Biol; 1999 Oct 29; 293(3):693-701. PubMed ID: 10543960
    [Abstract] [Full Text] [Related]

  • 19. There's a right way and a wrong way: in vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike.
    Betts S, King J.
    Structure; 1999 Jun 15; 7(6):R131-9. PubMed ID: 10404587
    [Abstract] [Full Text] [Related]

  • 20. Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation.
    Betts SD, King J.
    Protein Sci; 1998 Jul 15; 7(7):1516-23. PubMed ID: 9684883
    [Abstract] [Full Text] [Related]

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