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 *

348 related articles for article (PubMed ID: 11563916)

  • 1. 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]  

  • 2. 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]  

  • 3. 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]  

  • 4. Allosteric control by ATP of non-folded protein binding to GroEL.
    Yifrach O; Horovitz A
    J Mol Biol; 1996 Jan; 255(3):356-61. PubMed ID: 8568880
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL.
    Yifrach O; Horovitz A
    Biochemistry; 1998 May; 37(20):7083-8. PubMed ID: 9585518
    [TBL] [Abstract][Full Text] [Related]  

  • 6. The allosteric transition of GroEL induced by metal fluoride-ADP complexes.
    Inobe T; Kikushima K; Makio T; Arai M; Kuwajima K
    J Mol Biol; 2003 May; 329(1):121-34. PubMed ID: 12742022
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Phi value analysis of an allosteric transition of GroEL based on a single-pathway model.
    Inobe T; Kuwajima K
    J Mol Biol; 2004 May; 339(1):199-205. PubMed ID: 15123431
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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]  

  • 9. A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL.
    Poso D; Clarke AR; Burston SG
    J Mol Biol; 2004 May; 338(5):969-77. PubMed ID: 15111060
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings.
    Kad NM; Ranson NA; Cliff MJ; Clarke AR
    J Mol Biol; 1998 Apr; 278(1):267-78. PubMed ID: 9571049
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196-->Ala.
    Yifrach O; Horovitz A
    J Mol Biol; 1994 Oct; 243(3):397-401. PubMed ID: 7966268
    [TBL] [Abstract][Full Text] [Related]  

  • 12. GroES promotes the T to R transition of the GroEL ring distal to GroES in the GroEL-GroES complex.
    Inbar E; Horovitz A
    Biochemistry; 1997 Oct; 36(40):12276-81. PubMed ID: 9315866
    [TBL] [Abstract][Full Text] [Related]  

  • 13. [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]  

  • 14. 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]  

  • 15. 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]  

  • 16. Kinetic analysis of ATP-dependent inter-ring communication in GroEL.
    Amir A; Horovitz A
    J Mol Biol; 2004 May; 338(5):979-88. PubMed ID: 15111061
    [TBL] [Abstract][Full Text] [Related]  

  • 17. The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites.
    Schlee S; Groemping Y; Herde P; Seidel R; Reinstein J
    J Mol Biol; 2001 Mar; 306(4):889-99. PubMed ID: 11243796
    [TBL] [Abstract][Full Text] [Related]  

  • 18. From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.
    Chatellier J; Hill F; Foster NW; Goloubinoff P; Fersht AR
    J Mol Biol; 2000 Dec; 304(5):897-910. PubMed ID: 11124035
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP.
    Inobe T; Makio T; Takasu-Ishikawa E; Terada TP; Kuwajima K
    Biochim Biophys Acta; 2001 Feb; 1545(1-2):160-73. PubMed ID: 11342042
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Coupling between protein folding and allostery in the GroE chaperonin system.
    Yifrach O; Horovitz A
    Proc Natl Acad Sci U S A; 2000 Feb; 97(4):1521-4. PubMed ID: 10677493
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 18.