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 *

121 related articles for article (PubMed ID: 14556748)

  • 21. Reversible oligomerization and denaturation of the chaperonin GroES.
    Seale JW; Gorovits BM; Ybarra J; Horowitz PM
    Biochemistry; 1996 Apr; 35(13):4079-83. PubMed ID: 8672442
    [TBL] [Abstract][Full Text] [Related]  

  • 22. The C-terminal sequence of the chaperonin GroES is required for oligomerization.
    Seale JW; Horowitz PM
    J Biol Chem; 1995 Dec; 270(51):30268-70. PubMed ID: 8530444
    [TBL] [Abstract][Full Text] [Related]  

  • 23. [Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy].
    Ryabova NA; Selivanova OM; Semisotnov GV
    Mol Biol (Mosk); 2018; 52(1):120-124. PubMed ID: 29512644
    [TBL] [Abstract][Full Text] [Related]  

  • 24. Productive folding of a tethered protein in the chaperonin GroEL-GroES cage.
    Motojima F; Yoshida M
    Biochem Biophys Res Commun; 2015 Oct; 466(1):72-5. PubMed ID: 26325470
    [TBL] [Abstract][Full Text] [Related]  

  • 25. 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]  

  • 26. Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.
    Illingworth M; Salisbury J; Li W; Lin D; Chen L
    Biochem Biophys Res Commun; 2015 Oct; 466(1):15-20. PubMed ID: 26271593
    [TBL] [Abstract][Full Text] [Related]  

  • 27. The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding.
    Weber F; Keppel F; Georgopoulos C; Hayer-Hartl MK; Hartl FU
    Nat Struct Biol; 1998 Nov; 5(11):977-85. PubMed ID: 9808043
    [TBL] [Abstract][Full Text] [Related]  

  • 28. Purification and characterization of Chromatium vinosum GroEL and GroES proteins overexpressed in Escherichia coli cells lacking the endogenous groESL operon.
    Dionisi HM; Viale AM
    Protein Expr Purif; 1998 Nov; 14(2):275-82. PubMed ID: 9790891
    [TBL] [Abstract][Full Text] [Related]  

  • 29. The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/GroES-assisted folding.
    Paul S; Singh C; Mishra S; Chaudhuri TK
    FASEB J; 2007 Sep; 21(11):2874-85. PubMed ID: 17494995
    [TBL] [Abstract][Full Text] [Related]  

  • 30. Kinetics and thermodynamics of the unfolding and refolding of the three-stranded alpha-helical coiled coil, Lpp-56.
    Dragan AI; Potekhin SA; Sivolob A; Lu M; Privalov PL
    Biochemistry; 2004 Nov; 43(47):14891-900. PubMed ID: 15554696
    [TBL] [Abstract][Full Text] [Related]  

  • 31. Prying open single GroES ring complexes by force reveals cooperativity across domains.
    Ikeda-Kobayashi A; Taniguchi Y; Brockwell DJ; Paci E; Kawakami M
    Biophys J; 2012 Apr; 102(8):1961-8. PubMed ID: 22768953
    [TBL] [Abstract][Full Text] [Related]  

  • 32. Folding and assembly pathways of co-chaperonin proteins 10: Origin of bacterial thermostability.
    Luke K; Wittung-Stafshede P
    Arch Biochem Biophys; 2006 Dec; 456(1):8-18. PubMed ID: 17084377
    [TBL] [Abstract][Full Text] [Related]  

  • 33. Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins.
    Machida K; Fujiwara R; Tanaka T; Sakane I; Hongo K; Mizobata T; Kawata Y
    Biochim Biophys Acta; 2009 Sep; 1794(9):1344-54. PubMed ID: 19130907
    [TBL] [Abstract][Full Text] [Related]  

  • 34. 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]  

  • 35. GroEL/GroES-mediated folding of a protein too large to be encapsulated.
    Chaudhuri TK; Farr GW; Fenton WA; Rospert S; Horwich AL
    Cell; 2001 Oct; 107(2):235-46. PubMed ID: 11672530
    [TBL] [Abstract][Full Text] [Related]  

  • 36. Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR.
    Nieba-Axmann SE; Ottiger M; Wüthrich K; Plückthun A
    J Mol Biol; 1997 Sep; 271(5):803-18. PubMed ID: 9299328
    [TBL] [Abstract][Full Text] [Related]  

  • 37. GroEL/ES chaperonins protect interferon-gamma against physicochemical stress--study of tertiary structure formation by alpha-casein quenching and ELISA.
    Vandenbroeck K; Martens E; Billiau A
    Eur J Biochem; 1998 Jan; 251(1-2):181-8. PubMed ID: 9492282
    [TBL] [Abstract][Full Text] [Related]  

  • 38. Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings.
    Koike-Takeshita A; Arakawa T; Taguchi H; Shimamura T
    J Mol Biol; 2014 Oct; 426(21):3634-41. PubMed ID: 25174333
    [TBL] [Abstract][Full Text] [Related]  

  • 39. Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin.
    Yoshida T; Kawaguchi R; Taguchi H; Yoshida M; Yasunaga T; Wakabayashi T; Yohda M; Maruyama T
    J Mol Biol; 2002 Jan; 315(1):73-85. PubMed ID: 11771967
    [TBL] [Abstract][Full Text] [Related]  

  • 40. Comparison of refolding activities between nanogel artificial chaperone and GroEL systems.
    Asayama W; Sawada S; Taguchi H; Akiyoshi K
    Int J Biol Macromol; 2008 Apr; 42(3):241-6. PubMed ID: 18179818
    [TBL] [Abstract][Full Text] [Related]  

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