BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

121 related articles for article (PubMed ID: 7914191)

  • 21. Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria.
    Höhfeld J; Hartl FU
    J Cell Biol; 1994 Jul; 126(2):305-15. PubMed ID: 7913473
    [TBL] [Abstract][Full Text] [Related]  

  • 22. GroE-mediated folding of bacterial luciferases in vivo.
    Escher A; Szalay AA
    Mol Gen Genet; 1993 Apr; 238(1-2):65-73. PubMed ID: 8097558
    [TBL] [Abstract][Full Text] [Related]  

  • 23. 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]  

  • 24. 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]  

  • 25. Spinach chloroplast cpn21 co-chaperonin possesses two functional domains fused together in a toroidal structure and exhibits nucleotide-dependent binding to plastid chaperonin 60.
    Baneyx F; Bertsch U; Kalbach CE; van der Vies SM; Soll J; Gatenby AA
    J Biol Chem; 1995 May; 270(18):10695-702. PubMed ID: 7738007
    [TBL] [Abstract][Full Text] [Related]  

  • 26. The N terminus of the molecular chaperonin GroEL is a crucial structural element for its assembly.
    Horovitz A; Bochkareva ES; Girshovich AS
    J Biol Chem; 1993 May; 268(14):9957-9. PubMed ID: 8098040
    [TBL] [Abstract][Full Text] [Related]  

  • 27. Chaperonins and protein folding: unity and disunity of mechanisms.
    Lorimer GH; Todd MJ; Viitanen PV
    Philos Trans R Soc Lond B Biol Sci; 1993 Mar; 339(1289):297-303; discussion 303-4. PubMed ID: 8098534
    [TBL] [Abstract][Full Text] [Related]  

  • 28. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells.
    Thomas JG; Baneyx F
    Mol Microbiol; 2000 Jun; 36(6):1360-70. PubMed ID: 10931286
    [TBL] [Abstract][Full Text] [Related]  

  • 29. On the role of groES in the chaperonin-assisted folding reaction. Three case studies.
    Schmidt M; Buchner J; Todd MJ; Lorimer GH; Viitanen PV
    J Biol Chem; 1994 Apr; 269(14):10304-11. PubMed ID: 7908292
    [TBL] [Abstract][Full Text] [Related]  

  • 30. 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]  

  • 31. Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES.
    Kandror O; Busconi L; Sherman M; Goldberg AL
    J Biol Chem; 1994 Sep; 269(38):23575-82. PubMed ID: 7916344
    [TBL] [Abstract][Full Text] [Related]  

  • 32. The Escherichia coli groE chaperonins.
    Georgopoulos C; Ang D
    Semin Cell Biol; 1990 Feb; 1(1):19-25. PubMed ID: 1983267
    [TBL] [Abstract][Full Text] [Related]  

  • 33. 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]  

  • 34. Targeting of a foreign protein to chloroplasts by fusion to the transit peptide from the small subunit of ribulose 1,5-bisphosphate carboxylase.
    Van den Broeck G; Timko MP; Kausch AP; Cashmore AR; Van Montagu M; Herrera-Estrella L
    Nature; 1985 Jan 31-Feb 6; 313(6001):358-63. PubMed ID: 3969146
    [TBL] [Abstract][Full Text] [Related]  

  • 35. Refolding and recognition of mitochondrial malate dehydrogenase by Escherichia coli chaperonins cpn 60 (groEL) and cpn10 (groES).
    Hutchinson JP; el-Thaher TS; Miller AD
    Biochem J; 1994 Sep; 302 ( Pt 2)(Pt 2):405-10. PubMed ID: 7916564
    [TBL] [Abstract][Full Text] [Related]  

  • 36. 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; 32(10):2554-63. PubMed ID: 8095403
    [TBL] [Abstract][Full Text] [Related]  

  • 37. Characterization of a functionally important mobile domain of GroES.
    Landry SJ; Zeilstra-Ryalls J; Fayet O; Georgopoulos C; Gierasch LM
    Nature; 1993 Jul; 364(6434):255-8. PubMed ID: 8100614
    [TBL] [Abstract][Full Text] [Related]  

  • 38. Dual function of protein confinement in chaperonin-assisted protein folding.
    Brinker A; Pfeifer G; Kerner MJ; Naylor DJ; Hartl FU; Hayer-Hartl M
    Cell; 2001 Oct; 107(2):223-33. PubMed ID: 11672529
    [TBL] [Abstract][Full Text] [Related]  

  • 39. 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
    [TBL] [Abstract][Full Text] [Related]  

  • 40. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.
    Goloubinoff P; Gatenby AA; Lorimer GH
    Nature; 1989 Jan; 337(6202):44-7. PubMed ID: 2562907
    [TBL] [Abstract][Full Text] [Related]  

    [Previous]   [Next]    [New Search]
    of 7.