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 *

314 related articles for article (PubMed ID: 10512721)

  • 1. Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES.
    Makio T; Arai M; Kuwajima K
    J Mol Biol; 1999 Oct; 293(1):125-37. PubMed ID: 10512721
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Nucleotide-induced transition of GroEL from the high-affinity to the low-affinity state for a target protein: effects of ATP and ADP on the GroEL-affected refolding of alpha-lactalbumin.
    Makio T; Takasu-Ishikawa E; Kuwajima K
    J Mol Biol; 2001 Sep; 312(3):555-67. PubMed ID: 11563916
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL.
    Tsurupa GP; Ikura T; Makio T; Kuwajima K
    J Mol Biol; 1998 Apr; 277(3):733-45. PubMed ID: 9533891
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions.
    Behlke J; Ristau O; Schönfeld HJ
    Biochemistry; 1997 Apr; 36(17):5149-56. PubMed ID: 9136876
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Effect of GroEL on the re-folding kinetics of alpha-lactalbumin.
    Katsumata K; Okazaki A; Kuwajima K
    J Mol Biol; 1996 May; 258(5):827-38. PubMed ID: 8637013
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL.
    Katsumata K; Okazaki A; Tsurupa GP; Kuwajima K
    J Mol Biol; 1996 Dec; 264(4):643-9. PubMed ID: 8980675
    [TBL] [Abstract][Full Text] [Related]  

  • 7. 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]  

  • 8. GroE chaperonin-assisted folding and assembly of dodecameric glutamine synthetase.
    Fisher MT
    Biochemistry (Mosc); 1998 Apr; 63(4):382-98. PubMed ID: 9556521
    [TBL] [Abstract][Full Text] [Related]  

  • 9. 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]  

  • 10. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.
    Rye HS; Burston SG; Fenton WA; Beechem JM; Xu Z; Sigler PB; Horwich AL
    Nature; 1997 Aug; 388(6644):792-8. PubMed ID: 9285593
    [TBL] [Abstract][Full Text] [Related]  

  • 11. 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]  

  • 12. [The interaction of the GroEL chaperone with early kinetic intermediates of renaturing proteins inhibits the formation of their native structure].
    Marchenkov VV; Sokolovskiĭ IV; Kotova NV; Galzitskaya OV; Bochkareva ES; Girshovich AS; Semisotnov GV
    Biofizika; 2004; 49(6):987-94. PubMed ID: 15612537
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.
    Martin J; Geromanos S; Tempst P; Hartl FU
    Nature; 1993 Nov; 366(6452):279-82. PubMed ID: 7901771
    [TBL] [Abstract][Full Text] [Related]  

  • 14. 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]  

  • 15. 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]  

  • 16. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.
    Cliff MJ; Kad NM; Hay N; Lund PA; Webb MR; Burston SG; Clarke AR
    J Mol Biol; 1999 Oct; 293(3):667-84. PubMed ID: 10543958
    [TBL] [Abstract][Full Text] [Related]  

  • 17. GroEL-mediated folding of structurally homologous dihydrofolate reductases.
    Clark AC; Frieden C
    J Mol Biol; 1997 May; 268(2):512-25. PubMed ID: 9159487
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase.
    Ayling A; Baneyx F
    Protein Sci; 1996 Mar; 5(3):478-87. PubMed ID: 8868484
    [TBL] [Abstract][Full Text] [Related]  

  • 19. 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]  

  • 20. 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]  

    [Next]    [New Search]
    of 16.