BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

222 related articles for article (PubMed ID: 2192863)

  • 1. The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor.
    Laminet AA; Ziegelhoffer T; Georgopoulos C; Plückthun A
    EMBO J; 1990 Jul; 9(7):2315-9. PubMed ID: 2192863
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor.
    Zahn R; Axmann SE; Rücknagel KP; Jaeger E; Laminet AA; Plückthun A
    J Mol Biol; 1994 Sep; 242(2):150-64. PubMed ID: 7916381
    [TBL] [Abstract][Full Text] [Related]  

  • 3. 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]  

  • 4. A newly synthesized protein interacts with GroES on the surface of chaperonin GroEL.
    Bochkareva ES; Girshovich AS
    J Biol Chem; 1992 Dec; 267(36):25672-5. PubMed ID: 1361186
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.
    Bochkareva ES; Lissin NM; Girshovich AS
    Nature; 1988 Nov; 336(6196):254-7. PubMed ID: 2904124
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature beta-lactamase.
    Zahn R; Plückthun A
    J Mol Biol; 1994 Sep; 242(2):165-74. PubMed ID: 7916382
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Folding in vitro and transport in vivo of pre-beta-lactamase are SecB independent.
    Laminet AA; Kumamoto CA; Plückthun A
    Mol Microbiol; 1991 Jan; 5(1):117-22. PubMed ID: 2013998
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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]  

  • 9. Chaperonins groEL and groES promote assembly of heterotetramers (alpha 2 beta 2) of mammalian mitochondrial branched-chain alpha-keto acid decarboxylase in Escherichia coli.
    Wynn RM; Davie JR; Cox RP; Chuang DT
    J Biol Chem; 1992 Jun; 267(18):12400-3. PubMed ID: 1352285
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli.
    Kusukawa N; Yura T; Ueguchi C; Akiyama Y; Ito K
    EMBO J; 1989 Nov; 8(11):3517-21. PubMed ID: 2573517
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Visualizing GroEL/ES in the act of encapsulating a folding protein.
    Chen DH; Madan D; Weaver J; Lin Z; Schröder GF; Chiu W; Rye HS
    Cell; 2013 Jun; 153(6):1354-65. PubMed ID: 23746846
    [TBL] [Abstract][Full Text] [Related]  

  • 12. The formation of symmetrical GroEL-GroES complexes in the presence of ATP.
    Llorca O; Marco S; Carrascosa JL; Valpuesta JM
    FEBS Lett; 1994 May; 345(2-3):181-6. PubMed ID: 7911087
    [TBL] [Abstract][Full Text] [Related]  

  • 13. 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]  

  • 14. Local energetic frustration affects the dependence of green fluorescent protein folding on the chaperonin GroEL.
    Bandyopadhyay B; Goldenzweig A; Unger T; Adato O; Fleishman SJ; Unger R; Horovitz A
    J Biol Chem; 2017 Dec; 292(50):20583-20591. PubMed ID: 29066625
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Reactivation of thermally inactivated pre-beta-lactamase by DnaK, DnaJ, and GrpE.
    McCarthy D; Kramer G; Hardesty B
    Protein Sci; 1998 May; 7(5):1164-71. PubMed ID: 9605320
    [TBL] [Abstract][Full Text] [Related]  

  • 16. GroEL assisted folding of large polypeptide substrates in Escherichia coli: Present scenario and assignments for the future.
    Chaudhuri TK; Verma VK; Maheshwari A
    Prog Biophys Mol Biol; 2009 Jan; 99(1):42-50. PubMed ID: 19027782
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.
    Langer T; Pfeifer G; Martin J; Baumeister W; Hartl FU
    EMBO J; 1992 Dec; 11(13):4757-65. PubMed ID: 1361169
    [TBL] [Abstract][Full Text] [Related]  

  • 18. 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]  

  • 19. GroEL-GroES assisted folding of multiple recombinant proteins simultaneously over-expressed in Escherichia coli.
    Goyal M; Chaudhuri TK
    Int J Biochem Cell Biol; 2015 Jul; 64():277-86. PubMed ID: 25957916
    [TBL] [Abstract][Full Text] [Related]  

  • 20. 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]  

    [Next]    [New Search]
    of 12.