These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

113 related articles for article (PubMed ID: 9003436)

  • 41. Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.
    Corrales FJ; Fersht AR
    Proc Natl Acad Sci U S A; 1996 Apr; 93(9):4509-12. PubMed ID: 8633099
    [TBL] [Abstract][Full Text] [Related]  

  • 42. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.
    Xu Z; Horwich AL; Sigler PB
    Nature; 1997 Aug; 388(6644):741-50. PubMed ID: 9285585
    [TBL] [Abstract][Full Text] [Related]  

  • 43. Do chaperonins boost protein yields by accelerating folding or preventing aggregation?
    Jewett AI; Shea JE
    Biophys J; 2008 Apr; 94(8):2987-93. PubMed ID: 18192377
    [TBL] [Abstract][Full Text] [Related]  

  • 44. Protein folding assisted by the GroEL/GroES chaperonin system.
    Martin J
    Biochemistry (Mosc); 1998 Apr; 63(4):374-81. PubMed ID: 9556520
    [TBL] [Abstract][Full Text] [Related]  

  • 45. Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae.
    Mande SC; Mehra V; Bloom BR; Hol WG
    Science; 1996 Jan; 271(5246):203-7. PubMed ID: 8539620
    [TBL] [Abstract][Full Text] [Related]  

  • 46. Structure and function in GroEL-mediated protein folding.
    Sigler PB; Xu Z; Rye HS; Burston SG; Fenton WA; Horwich AL
    Annu Rev Biochem; 1998; 67():581-608. PubMed ID: 9759498
    [TBL] [Abstract][Full Text] [Related]  

  • 47. Characterisation of mutations in GroES that allow GroEL to function as a single ring.
    Liu H; Kovács E; Lund PA
    FEBS Lett; 2009 Jul; 583(14):2365-71. PubMed ID: 19545569
    [TBL] [Abstract][Full Text] [Related]  

  • 48. The lid that shapes the pot: structure and function of the chaperonin GroES.
    Saibil H
    Structure; 1996 Jan; 4(1):1-4. PubMed ID: 8805512
    [TBL] [Abstract][Full Text] [Related]  

  • 49. Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.
    Tang YC; Chang HC; Roeben A; Wischnewski D; Wischnewski N; Kerner MJ; Hartl FU; Hayer-Hartl M
    Cell; 2006 Jun; 125(5):903-14. PubMed ID: 16751100
    [TBL] [Abstract][Full Text] [Related]  

  • 50. 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]  

  • 51. Combined thermodynamic and kinetic analysis of GroEL interacting with CXCR4 transmembrane peptides.
    Chi H; Xu B; Liu Z; Wei J; Li S; Ren H; Xu Y; Lu X; Wang X; Wang X; Huang F
    Biochim Biophys Acta Gen Subj; 2018 Jul; 1862(7):1576-1583. PubMed ID: 29627450
    [TBL] [Abstract][Full Text] [Related]  

  • 52. Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL.
    Motojima F; Chaudhry C; Fenton WA; Farr GW; Horwich AL
    Proc Natl Acad Sci U S A; 2004 Oct; 101(42):15005-12. PubMed ID: 15479763
    [TBL] [Abstract][Full Text] [Related]  

  • 53. Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity.
    Shimamura T; Koike-Takeshita A; Yokoyama K; Masui R; Murai N; Yoshida M; Taguchi H; Iwata S
    Structure; 2004 Aug; 12(8):1471-80. PubMed ID: 15296740
    [TBL] [Abstract][Full Text] [Related]  

  • 54. Probing protein-protein interactions in real time.
    Viani MB; Pietrasanta LI; Thompson JB; Chand A; Gebeshuber IC; Kindt JH; Richter M; Hansma HG; Hansma PK
    Nat Struct Biol; 2000 Aug; 7(8):644-7. PubMed ID: 10932247
    [TBL] [Abstract][Full Text] [Related]  

  • 55. The mechanism of GroEL/GroES folding/refolding of protein substrates revisited.
    Jones H; Preuss M; Wright M; Miller AD
    Org Biomol Chem; 2006 Apr; 4(7):1223-35. PubMed ID: 16557310
    [TBL] [Abstract][Full Text] [Related]  

  • 56. Phosphofructokinase interacts with molecular chaperonins GroEL and GroES.
    Melegh B; Minami Y
    Acta Biol Hung; 1997; 48(4):399-407. PubMed ID: 9847453
    [TBL] [Abstract][Full Text] [Related]  

  • 57. Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.
    Wälti MA; Schmidt T; Murray DT; Wang H; Hinshaw JE; Clore GM
    Proc Natl Acad Sci U S A; 2017 Aug; 114(34):9104-9109. PubMed ID: 28784759
    [TBL] [Abstract][Full Text] [Related]  

  • 58. Hidden order in the GroEL-GroES-(ADP)7 chaperonin: forms, folding, and ADP-binding sites.
    Janner A
    Proteins; 2003 Apr; 51(1):126-36. PubMed ID: 12596269
    [TBL] [Abstract][Full Text] [Related]  

  • 59. Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering.
    Inobe T; Takahashi K; Maki K; Enoki S; Kamagata K; Kadooka A; Arai M; Kuwajima K
    Biophys J; 2008 Feb; 94(4):1392-402. PubMed ID: 17981896
    [TBL] [Abstract][Full Text] [Related]  

  • 60. 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]  

    [Previous]   [Next]    [New Search]
    of 6.