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Journal Abstract Search

189 related items for PubMed ID: 1977163

  • 1. 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; 87(19):7683-7. PubMed ID: 1977163
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  • 2. 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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  • 3. Asymmetric functional interaction between chaperonin and its plastidic cofactors.
    Guo P, Jiang S, Bai C, Zhang W, Zhao Q, Liu C.
    FEBS J; 2015 Oct 01; 282(20):3959-70. PubMed ID: 26237751
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  • 4. Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring.
    Viitanen PV, Lorimer GH, Seetharam R, Gupta RS, Oppenheim J, Thomas JO, Cowan NJ.
    J Biol Chem; 1992 Jan 15; 267(2):695-8. PubMed ID: 1346131
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  • 8. Functional analysis of isolated cpn10 domains and conserved amino acid residues in spinach chloroplast co-chaperonin by site-directed mutagenesis.
    Bertsch U, Soll J.
    Plant Mol Biol; 1995 Dec 15; 29(5):1039-55. PubMed ID: 8555447
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  • 9. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.
    Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH.
    Nature; 1995 Dec 15; 342(6252):884-9. PubMed ID: 10532860
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  • 10. Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES) do not catalyse the refolding of mitochondrial malate dehydrogenase.
    Miller AD, Maghlaoui K, Albanese G, Kleinjan DA, Smith C.
    Biochem J; 1993 Apr 01; 291 ( Pt 1)(Pt 1):139-44. PubMed ID: 8097086
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  • 11. 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
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  • 12. Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding.
    van der Vies SM, Gatenby AA, Georgopoulos C.
    Nature; 1994 Apr 14; 368(6472):654-6. PubMed ID: 7908418
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  • 13. 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 14; 3(3):200-7. PubMed ID: 9764760
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  • 14. Identification of a mammalian 10-kDa heat shock protein, a mitochondrial chaperonin 10 homologue essential for assisted folding of trimeric ornithine transcarbamoylase in vitro.
    Hartman DJ, Hoogenraad NJ, Condron R, Høj PB.
    Proc Natl Acad Sci U S A; 1992 Apr 15; 89(8):3394-8. PubMed ID: 1348860
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  • 17. 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
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  • 19. Expansion and compression of a protein folding intermediate by GroEL.
    Lin Z, Rye HS.
    Mol Cell; 2004 Oct 08; 16(1):23-34. PubMed ID: 15469819
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  • 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
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