272 related articles for article (PubMed ID: 12742022)
1. 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]
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. Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy.
Inobe T; Arai M; Nakao M; Ito K; Kamagata K; Makio T; Amemiya Y; Kihara H; Kuwajima K
J Mol Biol; 2003 Mar; 327(1):183-91. PubMed ID: 12614617
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. 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]
6. Transition state complexes of the Klebsiella pneumoniae nitrogenase proteins. Spectroscopic properties of aluminium fluoride-stabilized and beryllium fluoride-stabilized MgADP complexes reveal conformational differences of the Fe protein.
Miller RW; Eady RR; Fairhurst SA; Gormal CA; Smith BE
Eur J Biochem; 2001 Feb; 268(3):809-18. PubMed ID: 11168422
[TBL] [Abstract][Full Text] [Related]
7. 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]
8. 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]
9. Formation of the myosin.ADP.gallium fluoride complex and its solution structure by small-angle synchrotron X-ray scattering.
Maruta S; Uyehara Y; Homma K; Sugimoto Y; Wakabayashi K
J Biochem; 1999 Jan; 125(1):177-85. PubMed ID: 9880815
[TBL] [Abstract][Full Text] [Related]
10. Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolution.
Fei X; Yang D; LaRonde-LeBlanc N; Lorimer GH
Proc Natl Acad Sci U S A; 2013 Aug; 110(32):E2958-66. PubMed ID: 23861496
[TBL] [Abstract][Full Text] [Related]
11. 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]
12. 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]
13. Probing the mechanism of ATP hydrolysis on F-actin using vanadate and the structural analogs of phosphate BeF-3 and A1F-4.
Combeau C; Carlier MF
J Biol Chem; 1988 Nov; 263(33):17429-36. PubMed ID: 3182855
[TBL] [Abstract][Full Text] [Related]
14. A monomeric variant of GroEL binds nucleotides but is inactive as a molecular chaperone.
White ZW; Fisher KE; Eisenstein E
J Biol Chem; 1995 Sep; 270(35):20404-9. PubMed ID: 7657615
[TBL] [Abstract][Full Text] [Related]
15. Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics.
Chaudhry C; Farr GW; Todd MJ; Rye HS; Brunger AT; Adams PD; Horwich AL; Sigler PB
EMBO J; 2003 Oct; 22(19):4877-87. PubMed ID: 14517228
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. 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]
18. RecA protein-promoted cleavage of LexA repressor in the presence of ADP and structural analogues of inorganic phosphate, the fluoride complexes of aluminum and beryllium.
Moreau PL; Carlier MF
J Biol Chem; 1989 Feb; 264(4):2302-6. PubMed ID: 2521626
[TBL] [Abstract][Full Text] [Related]
19. Conformational changes in the GroEL oligomer during the functional cycle.
Llorca O; Marco S; Carrascosa JL; Valpuesta JM
J Struct Biol; 1997 Feb; 118(1):31-42. PubMed ID: 9087913
[TBL] [Abstract][Full Text] [Related]
20. The difference between ADP-beryllium fluoride and ADP-aluminium fluoride complexes of the spin-labeled myosin subfragment 1.
Ponomarev MA; Timofeev VP; Levitsky DI
FEBS Lett; 1995 Sep; 371(3):261-3. PubMed ID: 7556605
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
