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Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

226 related items for PubMed ID: 15522085

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  • 24. Design of a molecular chaperone-assisted protein folding bioreactor.
    Kohler RJ, Preuss M, Miller AD.
    Biotechnol Prog; 2000; 16(4):671-5. PubMed ID: 10933845
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  • 26. Bacteriophage p22 portal vertex formation in vivo.
    Moore SD, Prevelige PE.
    J Mol Biol; 2002 Feb 01; 315(5):975-94. PubMed ID: 11827470
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  • 27. Molecular genetics of bacteriophage P22 scaffolding protein's functional domains.
    Weigele PR, Sampson L, Winn-Stapley D, Casjens SR.
    J Mol Biol; 2005 May 13; 348(4):831-44. PubMed ID: 15843016
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  • 28. The mechanism of GroEL/GroES folding/refolding of protein substrates revisited.
    Jones H, Preuss M, Wright M, Miller AD.
    Org Biomol Chem; 2006 Apr 07; 4(7):1223-35. PubMed ID: 16557310
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  • 29. Structural roles of subunit cysteines in the folding and assembly of the DNA packaging machine (portal) of bacteriophage P22.
    Rodríguez-Casado A, Thomas GJ.
    Biochemistry; 2003 Apr 01; 42(12):3437-45. PubMed ID: 12653547
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  • 30. Contextual Role of a Salt Bridge in the Phage P22 Coat Protein I-Domain.
    Harprecht C, Okifo O, Robbins KJ, Motwani T, Alexandrescu AT, Teschke CM.
    J Biol Chem; 2016 May 20; 291(21):11359-72. PubMed ID: 27006399
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  • 31. The folding of nascent mitochondrial aspartate aminotransferase synthesized in a cell-free extract can be assisted by GroEL and GroES.
    Mattingly JR, Yañez AJ, Martinez-Carrion M.
    Arch Biochem Biophys; 2000 Oct 01; 382(1):113-22. PubMed ID: 11051104
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  • 32. Domain-specific chaperone-induced expansion is required for beta-actin folding: a comparison of beta-actin conformations upon interactions with GroEL and tail-less complex polypeptide 1 ring complex (TRiC).
    Villebeck L, Moparthi SB, Lindgren M, Hammarström P, Jonsson BH.
    Biochemistry; 2007 Nov 06; 46(44):12639-47. PubMed ID: 17939680
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  • 33. Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties.
    Anderson E, Teschke CM.
    Virology; 2003 Aug 15; 313(1):184-97. PubMed ID: 12951032
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  • 34. 'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants.
    Teschke CM, Parent KN.
    Virology; 2010 Jun 05; 401(2):119-30. PubMed ID: 20236676
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  • 37. Chaperomics: in vivo GroEL function defined.
    Ellis RJ.
    Curr Biol; 2005 Sep 06; 15(17):R661-3. PubMed ID: 16139196
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  • 38. Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli.
    Rinas U, Hoffmann F, Betiku E, Estapé D, Marten S.
    J Biotechnol; 2007 Jan 01; 127(2):244-57. PubMed ID: 16945443
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  • 39.
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  • 40. 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
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