BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

137 related articles for article (PubMed ID: 15544816)

  • 1. Structural stability of oligomeric chaperonin 10: the role of two beta-strands at the N and C termini in structural stabilization.
    Sakane I; Ikeda M; Matsumoto C; Higurashi T; Inoue K; Hongo K; Mizobata T; Kawata Y
    J Mol Biol; 2004 Dec; 344(4):1123-33. PubMed ID: 15544816
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Structural stability of covalently linked GroES heptamer: advantages in the formation of oligomeric structure.
    Sakane I; Hongo K; Motojima F; Murayama S; Mizobata T; Kawata Y
    J Mol Biol; 2007 Apr; 367(4):1171-85. PubMed ID: 17303164
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model.
    Higurashi T; Nosaka K; Mizobata T; Nagai J; Kawata Y
    J Mol Biol; 1999 Aug; 291(3):703-13. PubMed ID: 10448048
    [TBL] [Abstract][Full Text] [Related]  

  • 4. The structural stability of the co-chaperonin GroES.
    Boudker O; Todd MJ; Freire E
    J Mol Biol; 1997 Oct; 272(5):770-9. PubMed ID: 9368656
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant.
    Guidry JJ; Moczygemba CK; Steede NK; Landry SJ; Wittung-Stafshede P
    Protein Sci; 2000 Nov; 9(11):2109-17. PubMed ID: 11152122
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Oligomeric state and mode of self-association of Thermotoga maritima ribosomal stalk protein L12 in solution.
    Moens PD; Wahl MC; Jameson DM
    Biochemistry; 2005 Mar; 44(9):3298-305. PubMed ID: 15736940
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Structural stability and solution structure of chaperonin GroES heptamer studied by synchrotron small-angle X-ray scattering.
    Higurashi T; Hiragi Y; Ichimura K; Seki Y; Soda K; Mizobata T; Kawata Y
    J Mol Biol; 2003 Oct; 333(3):605-20. PubMed ID: 14556748
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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]  

  • 9. Interface mutation in heptameric co-chaperonin protein 10 destabilizes subunits but not interfaces.
    Brown C; Liao J; Wittung-Stafshede P
    Arch Biochem Biophys; 2005 Jul; 439(2):175-83. PubMed ID: 15978542
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Fibril formation of hsp10 homologue proteins and determination of fibril core regions: differences in fibril core regions dependent on subtle differences in amino acid sequence.
    Yagi H; Sato A; Yoshida A; Hattori Y; Hara M; Shimamura J; Sakane I; Hongo K; Mizobata T; Kawata Y
    J Mol Biol; 2008 Apr; 377(5):1593-606. PubMed ID: 18329043
    [TBL] [Abstract][Full Text] [Related]  

  • 11. First characterization of co-chaperonin protein 10 from hyper-thermophilic Aquifex aeolicus.
    Guidry J; Wittung-Stafshede P
    Biochem Biophys Res Commun; 2004 Apr; 317(1):176-80. PubMed ID: 15047164
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified.
    Guidry JJ; Shewmaker F; Maskos K; Landry S; Wittung-Stafshede P
    BMC Biochem; 2003 Oct; 4():14. PubMed ID: 14525625
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Allostery wiring diagrams in the transitions that drive the GroEL reaction cycle.
    Tehver R; Chen J; Thirumalai D
    J Mol Biol; 2009 Mar; 387(2):390-406. PubMed ID: 19121324
    [TBL] [Abstract][Full Text] [Related]  

  • 14. From minichaperone to GroEL 2: importance of avidity of the multisite ring structure.
    Chatellier J; Hill F; Fersht AR
    J Mol Biol; 2000 Dec; 304(5):883-96. PubMed ID: 11124034
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Prediction of the structure of GroES and its interaction with GroEL.
    Valencia A; Hubbard TJ; Muga A; Bañuelos S; Llorca O; Carrascosa JL; Valpuesta JM
    Proteins; 1995 Jul; 22(3):199-209. PubMed ID: 7479694
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Comparison of the conformational state and in vitro refolding of yeast chaperonin protein cpn10 with bacterial GroES.
    de Jongh HH; Rospert S; Dobson CM
    Biochem Biophys Res Commun; 1998 Mar; 244(3):884-8. PubMed ID: 9535761
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Functional consequences of single:double ring transitions in chaperonins: life in the cold.
    Ferrer M; Lünsdorf H; Chernikova TN; Yakimov M; Timmis KN; Golyshin PN
    Mol Microbiol; 2004 Jul; 53(1):167-82. PubMed ID: 15225312
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Macromolecular crowding extended to a heptameric system: the Co-chaperonin protein 10.
    Aguilar X; F Weise C; Sparrman T; Wolf-Watz M; Wittung-Stafshede P
    Biochemistry; 2011 Apr; 50(14):3034-44. PubMed ID: 21375247
    [TBL] [Abstract][Full Text] [Related]  

  • 19. 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]  

  • 20. Role of the unique peptide tail in hyperthermostable Aquifex aeolicus cochaperonin protein 10.
    Luke K; Apiyo D; Wittung-Stafshede P
    Biochemistry; 2005 Nov; 44(44):14385-95. PubMed ID: 16262239
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 7.