BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

307 related articles for article (PubMed ID: 1677004)

  • 1. 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]  

  • 2. Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures.
    Mendoza JA; Lorimer GH; Horowitz PM
    J Biol Chem; 1992 Sep; 267(25):17631-4. PubMed ID: 1355476
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding.
    Smith KE; Fisher MT
    J Biol Chem; 1995 Sep; 270(37):21517-23. PubMed ID: 7665563
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry.
    Mendoza JA; Lorimer GH; Horowitz PM
    J Biol Chem; 1991 Sep; 266(26):16973-6. PubMed ID: 1680127
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Refolding of bovine mitochondrial rhodanese by chaperonins GroEL and GroES.
    Weber F; Hayer-Hartl M
    Methods Mol Biol; 2000; 140():117-26. PubMed ID: 11484478
    [No Abstract]   [Full Text] [Related]  

  • 6. The chaperonin assisted and unassisted refolding of rhodanese can be modulated by its N-terminal peptide.
    Mendoza JA; Horowitz PM
    J Protein Chem; 1994 Jan; 13(1):15-22. PubMed ID: 8011067
    [TBL] [Abstract][Full Text] [Related]  

  • 7. 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]  

  • 8. Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP.
    Makino Y; Taguchi H; Yoshida M
    FEBS Lett; 1993 Dec; 336(2):363-7. PubMed ID: 7903258
    [TBL] [Abstract][Full Text] [Related]  

  • 9. The lower hydrolysis of ATP by the stress protein GroEL is a major factor responsible for the diminished chaperonin activity at low temperature.
    Mendoza JA; Dulin P; Warren T
    Cryobiology; 2000 Dec; 41(4):319-23. PubMed ID: 11222029
    [TBL] [Abstract][Full Text] [Related]  

  • 10. GroEL and GroES increase the specific enzymatic activity of newly-synthesized rhodanese if present during in vitro transcription/translation.
    Tsalkova T; Zardeneta G; Kudlicki W; Kramer G; Horowitz PM; Hardesty B
    Biochemistry; 1993 Apr; 32(13):3377-80. PubMed ID: 8096394
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Rhodanese folding is controlled by the partitioning of its folding intermediates.
    Gorovits BM; McGee WA; Horowitz PM
    Biochim Biophys Acta; 1998 Jan; 1382(1):120-8. PubMed ID: 9507086
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese.
    Mendoza JA; Butler MC; Horowitz PM
    J Biol Chem; 1992 Dec; 267(34):24648-54. PubMed ID: 1360012
    [TBL] [Abstract][Full Text] [Related]  

  • 13. The aggregation state of rhodanese during folding influences the ability of GroEL to assist reactivation.
    Bhattacharyya AM; Horowitz PM
    J Biol Chem; 2001 Aug; 276(31):28739-43. PubMed ID: 11397797
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Rhodanese can partially refold in its GroEL-GroES-ADP complex and can be released to give a homogeneous product.
    Bhattacharyya AM; Horowitz PM
    Biochemistry; 2002 Feb; 41(7):2421-8. PubMed ID: 11841236
    [TBL] [Abstract][Full Text] [Related]  

  • 15. 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]  

  • 16. Sulfhydryl modification of E. coli Cpn60 leads to loss of its ability to support refolding of rhodanese but not to form a binary complex.
    Mendoza JA; Horowitz PM
    J Protein Chem; 1992 Dec; 11(6):589-94. PubMed ID: 1361328
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides.
    Ybarra J; Horowitz PM
    J Biol Chem; 1995 Sep; 270(39):22962-7. PubMed ID: 7559433
    [TBL] [Abstract][Full Text] [Related]  

  • 18. The rates of commitment to renaturation of rhodanese and glutamine synthetase in the presence of the groE chaperonins.
    Fisher MT; Yuan X
    J Biol Chem; 1994 Nov; 269(47):29598-601. PubMed ID: 7961947
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Minimal and optimal mechanisms for GroE-mediated protein folding.
    Ben-Zvi AP; Chatellier J; Fersht AR; Goloubinoff P
    Proc Natl Acad Sci U S A; 1998 Dec; 95(26):15275-80. PubMed ID: 9860959
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.
    Hayer-Hartl MK; Weber F; Hartl FU
    EMBO J; 1996 Nov; 15(22):6111-21. PubMed ID: 8947033
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 16.