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Journal Abstract Search

106 related items for PubMed ID: 1347504

  • 1. Structure of holo-chaperonin studied with electron microscopy. Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each.
    Ishii N, Taguchi H, Sumi M, Yoshida M.
    FEBS Lett; 1992 Mar 09; 299(2):169-74. PubMed ID: 1347504
    [Abstract] [Full Text] [Related]

  • 2. Molecular cloning, expression, and characterization of chaperonin-60 and chaperonin-10 from a thermophilic bacterium, Thermus thermophilus HB8.
    Amada K, Yohda M, Odaka M, Endo I, Ishii N, Taguchi H, Yoshida M.
    J Biochem; 1995 Aug 09; 118(2):347-54. PubMed ID: 8543569
    [Abstract] [Full Text] [Related]

  • 3. A chaperonin from a thermophilic bacterium, Thermus thermophilus.
    Yoshida M, Ishii N, Muneyuki E, Taguchi H.
    Philos Trans R Soc Lond B Biol Sci; 1993 Mar 29; 339(1289):305-12. PubMed ID: 8098535
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  • 4. Crystallization of the cpn60/cpn10 complex ('holo-chaperonin') from Thermus thermophilus.
    Lissin NM, Sedelnikova SE, Ryazantsev SN.
    FEBS Lett; 1992 Oct 12; 311(1):22-4. PubMed ID: 1356830
    [Abstract] [Full Text] [Related]

  • 5. Equatorial split of holo-chaperonin from Thermus thermophilus by ATP and K+.
    Ishii N, Taguchi H, Sasabe H, Yoshida M.
    FEBS Lett; 1995 Apr 03; 362(2):121-5. PubMed ID: 7720857
    [Abstract] [Full Text] [Related]

  • 6. Image analysis by electron microscopy of two-dimensional crystals developed on a mercury surface of chaperonin from Thermus thermophilus.
    Ishii N, Taguchi H, Yoshida M, Yoshimura H, Nagayama K.
    J Biochem; 1991 Dec 03; 110(6):905-8. PubMed ID: 1686608
    [Abstract] [Full Text] [Related]

  • 7. Purification and characterization of chaperonins 60 and 10 from Methylobacillus glycogenes.
    Kawata Y, Doi K, Omoto H, Mizobata T, Nagai J.
    Cell Stress Chaperones; 1998 Sep 03; 3(3):200-7. PubMed ID: 9764760
    [Abstract] [Full Text] [Related]

  • 8. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.
    Jackson GS, Staniforth RA, Halsall DJ, Atkinson T, Holbrook JJ, Clarke AR, Burston SG.
    Biochemistry; 1993 Mar 16; 32(10):2554-63. PubMed ID: 8095403
    [Abstract] [Full Text] [Related]

  • 9. Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria.
    Rospert S, Glick BS, Jenö P, Schatz G, Todd MJ, Lorimer GH, Viitanen PV.
    Proc Natl Acad Sci U S A; 1993 Dec 01; 90(23):10967-71. PubMed ID: 7902576
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  • 11. Identification of a groES-like chaperonin in mitochondria that facilitates protein folding.
    Lubben TH, Gatenby AA, Donaldson GK, Lorimer GH, Viitanen PV.
    Proc Natl Acad Sci U S A; 1990 Oct 01; 87(19):7683-7. PubMed ID: 1977163
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  • 13. Immunochemical localization of a region of chaperonin-60 important for productive interaction with chaperonin-10.
    Burns DL, Kessel M, Arciniega JL, Karpas A, Gould-Kostka J.
    J Biol Chem; 1992 Dec 25; 267(36):25632-5. PubMed ID: 1361184
    [Abstract] [Full Text] [Related]

  • 14. Differential effects of co-chaperonin homologs on cpn60 oligomers.
    Bonshtien AL, Parnas A, Sharkia R, Niv A, Mizrahi I, Azem A, Weiss C.
    Cell Stress Chaperones; 2009 Sep 25; 14(5):509-19. PubMed ID: 19224397
    [Abstract] [Full Text] [Related]

  • 15. Functional consequences of single:double ring transitions in chaperonins: life in the cold.
    Ferrer M, Lünsdorf H, Chernikova TN, Yakimov M, Timmis KN, Golyshin PN.
    Mol Microbiol; 2004 Jul 25; 53(1):167-82. PubMed ID: 15225312
    [Abstract] [Full Text] [Related]

  • 16. Molecular chaperones in pancreatic tissue: the presence of cpn10, cpn60 and hsp70 in distinct compartments along the secretory pathway of the acinar cells.
    Vélez-Granell CS, Arias AE, Torres-Ruíz JA, Bendayan M.
    J Cell Sci; 1994 Mar 25; 107 ( Pt 3)():539-49. PubMed ID: 7911805
    [Abstract] [Full Text] [Related]

  • 17. Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody.
    Ishii N, Taguchi H, Sasabe H, Yoshida M.
    J Mol Biol; 1994 Feb 25; 236(3):691-6. PubMed ID: 7906737
    [Abstract] [Full Text] [Related]

  • 18. Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae.
    Mande SC, Mehra V, Bloom BR, Hol WG.
    Science; 1996 Jan 12; 271(5246):203-7. PubMed ID: 8539620
    [Abstract] [Full Text] [Related]

  • 19. Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action.
    Mendoza JA, Demeler B, Horowitz PM.
    J Biol Chem; 1994 Jan 28; 269(4):2447-51. PubMed ID: 7905478
    [Abstract] [Full Text] [Related]

  • 20. Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10.
    Staniforth RA, Burston SG, Atkinson T, Clarke AR.
    Biochem J; 1994 Jun 15; 300 ( Pt 3)(Pt 3):651-8. PubMed ID: 7912068
    [Abstract] [Full Text] [Related]

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