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Journal Abstract Search

369 related items for PubMed ID: 28396349

  • 1.
    ; . PubMed ID:
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  • 2. 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 09; 466(1):15-20. PubMed ID: 26271593
    [Abstract] [Full Text] [Related]

  • 3. Functional characterization of an archaeal GroEL/GroES chaperonin system: significance of substrate encapsulation.
    Figueiredo L, Klunker D, Ang D, Naylor DJ, Kerner MJ, Georgopoulos C, Hartl FU, Hayer-Hartl M.
    J Biol Chem; 2004 Jan 09; 279(2):1090-9. PubMed ID: 14576149
    [Abstract] [Full Text] [Related]

  • 4. Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL.
    Sivinski J, Ambrose AJ, Panfilenko I, Zerio CJ, Machulis JM, Mollasalehi N, Kaneko LK, Stevens M, Ray AM, Park Y, Wu C, Hoang QQ, Johnson SM, Chapman E.
    mBio; 2021 Jan 12; 12(1):. PubMed ID: 33436430
    [Abstract] [Full Text] [Related]

  • 5. Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.
    Illingworth M, Ellis H, Chen L.
    Sci Rep; 2017 Aug 29; 7(1):9710. PubMed ID: 28852160
    [Abstract] [Full Text] [Related]

  • 6. Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.
    Dubaquié Y, Looser R, Rospert S.
    Proc Natl Acad Sci U S A; 1997 Aug 19; 94(17):9011-6. PubMed ID: 9256426
    [Abstract] [Full Text] [Related]

  • 7. Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli.
    Gupta P, Aggarwal N, Batra P, Mishra S, Chaudhuri TK.
    Int J Biochem Cell Biol; 2006 Aug 19; 38(11):1975-85. PubMed ID: 16822698
    [Abstract] [Full Text] [Related]

  • 8. Triggering protein folding within the GroEL-GroES complex.
    Madan D, Lin Z, Rye HS.
    J Biol Chem; 2008 Nov 14; 283(46):32003-13. PubMed ID: 18782766
    [Abstract] [Full Text] [Related]

  • 9. Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.
    Taguchi H.
    J Mol Biol; 2015 Sep 11; 427(18):2912-8. PubMed ID: 25900372
    [Abstract] [Full Text] [Related]

  • 10. Phosphofructokinase interacts with molecular chaperonins GroEL and GroES.
    Melegh B, Minami Y.
    Acta Biol Hung; 1997 Sep 11; 48(4):399-407. PubMed ID: 9847453
    [Abstract] [Full Text] [Related]

  • 11. ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle.
    Tyagi NK, Fenton WA, Horwich AL.
    FEBS Lett; 2010 Mar 05; 584(5):951-3. PubMed ID: 20083109
    [Abstract] [Full Text] [Related]

  • 12. Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.
    Sameshima T, Ueno T, Iizuka R, Ishii N, Terada N, Okabe K, Funatsu T.
    J Biol Chem; 2008 Aug 29; 283(35):23765-73. PubMed ID: 18567585
    [Abstract] [Full Text] [Related]

  • 13. Chlamydial GroEL autoregulates its own expression through direct interactions with the HrcA repressor protein.
    Wilson AC, Wu CC, Yates JR, Tan M.
    J Bacteriol; 2005 Nov 29; 187(21):7535-42. PubMed ID: 16237037
    [Abstract] [Full Text] [Related]

  • 14. Structure and function in GroEL-mediated protein folding.
    Sigler PB, Xu Z, Rye HS, Burston SG, Fenton WA, Horwich AL.
    Annu Rev Biochem; 1998 Nov 29; 67():581-608. PubMed ID: 9759498
    [Abstract] [Full Text] [Related]

  • 15. Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy.
    Kim SY, Semyonov AN, Twieg RJ, Horwich AL, Frydman J, Moerner WE.
    J Phys Chem B; 2005 Dec 29; 109(51):24517-25. PubMed ID: 16375456
    [Abstract] [Full Text] [Related]

  • 16. A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo.
    Nielsen KL, McLennan N, Masters M, Cowan NJ.
    J Bacteriol; 1999 Sep 29; 181(18):5871-5. PubMed ID: 10482535
    [Abstract] [Full Text] [Related]

  • 17. Asp-52 in combination with Asp-398 plays a critical role in ATP hydrolysis of chaperonin GroEL.
    Koike-Takeshita A, Mitsuoka K, Taguchi H.
    J Biol Chem; 2014 Oct 24; 289(43):30005-11. PubMed ID: 25202010
    [Abstract] [Full Text] [Related]

  • 18. Multiple gene duplication and rapid evolution in the groEL gene: functional implications.
    Goyal K, Qamra R, Mande SC.
    J Mol Evol; 2006 Dec 24; 63(6):781-7. PubMed ID: 17103057
    [Abstract] [Full Text] [Related]

  • 19. Discrimination of ATP, ADP, and AMPPNP by chaperonin GroEL: hexokinase treatment revealed the exclusive role of ATP.
    Motojima F, Yoshida M.
    J Biol Chem; 2003 Jul 18; 278(29):26648-54. PubMed ID: 12736270
    [Abstract] [Full Text] [Related]

  • 20. The role of ATP hydrolysis in the function of the chaperonin GroEL: dynamic complex formation with GroES.
    Kawata Y, Hongo K, Nosaka K, Furutsu Y, Mizobata T, Nagai J.
    FEBS Lett; 1995 Aug 07; 369(2-3):283-6. PubMed ID: 7649273
    [Abstract] [Full Text] [Related]

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