BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

134 related articles for article (PubMed ID: 10318804)

  • 21. 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]  

  • 22. An additional serine residue at the C terminus of rhodanese destabilizes the enzyme.
    Kramer G; Ramachandiran V; Horowitz P; Hardesty B
    Arch Biochem Biophys; 2001 Jan; 385(2):332-7. PubMed ID: 11368014
    [TBL] [Abstract][Full Text] [Related]  

  • 23. Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering.
    Thiyagarajan P; Henderson SJ; Joachimiak A
    Structure; 1996 Jan; 4(1):79-88. PubMed ID: 8805508
    [TBL] [Abstract][Full Text] [Related]  

  • 24. Release of both native and non-native proteins from a cis-only GroEL ternary complex.
    Burston SG; Weissman JS; Farr GW; Fenton WA; Horwich AL
    Nature; 1996 Sep; 383(6595):96-9. PubMed ID: 8779722
    [TBL] [Abstract][Full Text] [Related]  

  • 25. 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]  

  • 26. Chaperonin-assisted protein folding of the enzyme rhodanese by GroEL/GroES.
    Horowitz PM
    Methods Mol Biol; 1995; 40():361-8. PubMed ID: 7633531
    [No Abstract]   [Full Text] [Related]  

  • 27. Chaperone activity and structure of monomeric polypeptide binding domains of GroEL.
    Zahn R; Buckle AM; Perrett S; Johnson CM; Corrales FJ; Golbik R; Fersht AR
    Proc Natl Acad Sci U S A; 1996 Dec; 93(26):15024-9. PubMed ID: 8986757
    [TBL] [Abstract][Full Text] [Related]  

  • 28. 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]  

  • 29. Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action.
    Mendoza JA; Demeler B; Horowitz PM
    J Biol Chem; 1994 Jan; 269(4):2447-51. PubMed ID: 7905478
    [TBL] [Abstract][Full Text] [Related]  

  • 30. Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings.
    Llorca O; Marco S; Carrascosa JL; Valpuesta JM
    FEBS Lett; 1997 Mar; 405(2):195-9. PubMed ID: 9089290
    [TBL] [Abstract][Full Text] [Related]  

  • 31. 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]  

  • 32. Preformed GroES oligomers are not required as functional cochaperonins.
    Seale JW; Chirgwin JM; Demeler B; Horowitz PM
    J Protein Chem; 1997 Oct; 16(7):661-8. PubMed ID: 9330224
    [TBL] [Abstract][Full Text] [Related]  

  • 33. Structural plasticity and noncovalent substrate binding in the GroEL apical domain. A study using electrospay ionization mass spectrometry and fluorescence binding studies.
    Ashcroft AE; Brinker A; Coyle JE; Weber F; Kaiser M; Moroder L; Parsons MR; Jager J; Hartl UF; Hayer-Hartl M; Radford SE
    J Biol Chem; 2002 Sep; 277(36):33115-26. PubMed ID: 12065585
    [TBL] [Abstract][Full Text] [Related]  

  • 34. Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics.
    Chaudhry C; Farr GW; Todd MJ; Rye HS; Brunger AT; Adams PD; Horwich AL; Sigler PB
    EMBO J; 2003 Oct; 22(19):4877-87. PubMed ID: 14517228
    [TBL] [Abstract][Full Text] [Related]  

  • 35. GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle.
    Miyazaki T; Yoshimi T; Furutsu Y; Hongo K; Mizobata T; Kanemori M; Kawata Y
    J Biol Chem; 2002 Dec; 277(52):50621-8. PubMed ID: 12377767
    [TBL] [Abstract][Full Text] [Related]  

  • 36. The unfolding action of GroEL on a protein substrate.
    van der Vaart A; Ma J; Karplus M
    Biophys J; 2004 Jul; 87(1):562-73. PubMed ID: 15240489
    [TBL] [Abstract][Full Text] [Related]  

  • 37. Acid pH-induced conformational changes in bovine liver rhodanese.
    Horowitz PM; Xu R
    J Biol Chem; 1992 Sep; 267(27):19464-9. PubMed ID: 1527067
    [TBL] [Abstract][Full Text] [Related]  

  • 38. Protein folding in the central cavity of the GroEL-GroES chaperonin complex.
    Mayhew M; da Silva AC; Martin J; Erdjument-Bromage H; Tempst P; Hartl FU
    Nature; 1996 Feb; 379(6564):420-6. PubMed ID: 8559246
    [TBL] [Abstract][Full Text] [Related]  

  • 39. The stability of the molecular chaperonin cpn60 is affected by site-directed replacement of cysteine 518.
    Luo GX; Horowitz PM
    J Biol Chem; 1994 Dec; 269(51):32151-4. PubMed ID: 7798211
    [TBL] [Abstract][Full Text] [Related]  

  • 40. Analysis of the perturbation of phospholipid model membranes by rhodanese and its presequence.
    Zardeneta G; Horowitz PM
    J Biol Chem; 1992 Dec; 267(34):24193-8. PubMed ID: 1447169
    [TBL] [Abstract][Full Text] [Related]  

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