BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

164 related articles for article (PubMed ID: 8095267)

  • 1. Chaperonin-mediated reconstitution of the phytochrome photoreceptor.
    Grimm R; Donaldson GK; van der Vies SM; Schäfer E; Gatenby AA
    J Biol Chem; 1993 Mar; 268(7):5220-6. PubMed ID: 8095267
    [TBL] [Abstract][Full Text] [Related]  

  • 2. In vivo suppression of phytochrome aggregation by the GroE chaperonins in Escherichia coli.
    Edgerton MD; Santos MO; Jones AM
    Plant Mol Biol; 1993 Mar; 21(6):1191-4. PubMed ID: 8490138
    [TBL] [Abstract][Full Text] [Related]  

  • 3. The effect of groES on the groEL-dependent assembly of dodecameric glutamine synthetase in the presence of ATP and ADP.
    Fisher MT
    J Biol Chem; 1994 May; 269(18):13629-36. PubMed ID: 7909810
    [TBL] [Abstract][Full Text] [Related]  

  • 4. GroE facilitates refolding of citrate synthase by suppressing aggregation.
    Buchner J; Schmidt M; Fuchs M; Jaenicke R; Rudolph R; Schmid FX; Kiefhaber T
    Biochemistry; 1991 Feb; 30(6):1586-91. PubMed ID: 1671555
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Refolding of yeast enolase in the presence of the chaperonin GroE. The nucleotide specificity of GroE and the role of GroES.
    Kubo T; Mizobata T; Kawata Y
    J Biol Chem; 1993 Sep; 268(26):19346-51. PubMed ID: 8103517
    [TBL] [Abstract][Full Text] [Related]  

  • 6. A monomeric variant of GroEL binds nucleotides but is inactive as a molecular chaperone.
    White ZW; Fisher KE; Eisenstein E
    J Biol Chem; 1995 Sep; 270(35):20404-9. PubMed ID: 7657615
    [TBL] [Abstract][Full Text] [Related]  

  • 7. A TCP1-related molecular chaperone from plants refolds phytochrome to its photoreversible form.
    Mummert E; Grimm R; Speth V; Eckerskorn C; Schiltz E; Gatenby AA; Schäfer E
    Nature; 1993 Jun; 363(6430):644-8. PubMed ID: 8099715
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase.
    Ayling A; Baneyx F
    Protein Sci; 1996 Mar; 5(3):478-87. PubMed ID: 8868484
    [TBL] [Abstract][Full Text] [Related]  

  • 9. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation.
    Landry SJ; Gierasch LM
    Biochemistry; 1991 Jul; 30(30):7359-62. PubMed ID: 1677268
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. Refolding is enhanced in the presence of ADP.
    Mizobata T; Akiyama Y; Ito K; Yumoto N; Kawata Y
    J Biol Chem; 1992 Sep; 267(25):17773-9. PubMed ID: 1355477
    [TBL] [Abstract][Full Text] [Related]  

  • 11. A polypeptide bound by the chaperonin groEL is localized within a central cavity.
    Braig K; Simon M; Furuya F; Hainfeld JF; Horwich AL
    Proc Natl Acad Sci U S A; 1993 May; 90(9):3978-82. PubMed ID: 8097882
    [TBL] [Abstract][Full Text] [Related]  

  • 12. GroEL, GroES, and ATP-dependent folding and spontaneous assembly of ornithine transcarbamylase.
    Zheng X; Rosenberg LE; Kalousek F; Fenton WA
    J Biol Chem; 1993 Apr; 268(10):7489-93. PubMed ID: 8096512
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent.
    Viitanen PV; Lubben TH; Reed J; Goloubinoff P; O'Keefe DP; Lorimer GH
    Biochemistry; 1990 Jun; 29(24):5665-71. PubMed ID: 1974461
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Interaction of GroE with an all-beta-protein.
    Schmidt M; Buchner J
    J Biol Chem; 1992 Aug; 267(24):16829-33. PubMed ID: 1355088
    [TBL] [Abstract][Full Text] [Related]  

  • 15. GroE chaperonin-assisted folding and assembly of dodecameric glutamine synthetase.
    Fisher MT
    Biochemistry (Mosc); 1998 Apr; 63(4):382-98. PubMed ID: 9556521
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese.
    Mendoza JA; Rogers E; Lorimer GH; Horowitz PM
    J Biol Chem; 1991 Jul; 266(20):13044-9. PubMed ID: 1677004
    [TBL] [Abstract][Full Text] [Related]  

  • 17. The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network.
    Veinger L; Diamant S; Buchner J; Goloubinoff P
    J Biol Chem; 1998 May; 273(18):11032-7. PubMed ID: 9556585
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Glycosylation inhibits the interaction of invertase with the chaperone GroEL.
    Kern G; Schmidt M; Buchner J; Jaenicke R
    FEBS Lett; 1992 Jul; 305(3):203-5. PubMed ID: 1363729
    [TBL] [Abstract][Full Text] [Related]  

  • 19. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
    Martin J; Mayhew M; Langer T; Hartl FU
    Nature; 1993 Nov; 366(6452):228-33. PubMed ID: 7901770
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Efficient Catalysis of Protein Folding by GroEL/ES of the Obligate Chaperonin Substrate MetF.
    Singh AK; Balchin D; Imamoglu R; Hayer-Hartl M; Hartl FU
    J Mol Biol; 2020 Mar; 432(7):2304-2318. PubMed ID: 32135190
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 9.