92 related articles for article (PubMed ID: 18261461)
1. Divalent cations stabilize GroEL under conditions of oxidative stress.
Melkani GC; Sielaff RL; Zardeneta G; Mendoza JA
Biochem Biophys Res Commun; 2008 Apr; 368(3):625-30. PubMed ID: 18261461
[TBL] [Abstract][Full Text] [Related]
2. GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation.
Melkani GC; Zardeneta G; Mendoza JA
Biochem Biophys Res Commun; 2002 Jun; 294(4):893-9. PubMed ID: 12061791
[TBL] [Abstract][Full Text] [Related]
3. On the chaperonin activity of GroEL at heat-shock temperature.
Melkani GC; Zardeneta G; Mendoza JA
Int J Biochem Cell Biol; 2005 Jul; 37(7):1375-85. PubMed ID: 15833270
[TBL] [Abstract][Full Text] [Related]
4. Oxidized GroEL can function as a chaperonin.
Melkani GC; Zardeneta G; Mendoza JA
Front Biosci; 2004 Jan; 9():724-31. PubMed ID: 14766403
[TBL] [Abstract][Full Text] [Related]
5. Interaction of oxidized chaperonin GroEL with an unfolded protein at low temperatures.
Melkani GC; Sielaff R; Zardeneta G; Mendoza JA
Biosci Rep; 2012 Jun; 32(3):299-303. PubMed ID: 22273181
[TBL] [Abstract][Full Text] [Related]
6. Hydrogen peroxide induces the dissociation of GroEL into monomers that can facilitate the reactivation of oxidatively inactivated rhodanese.
Melkani GC; McNamara C; Zardeneta G; Mendoza JA
Int J Biochem Cell Biol; 2004 Mar; 36(3):505-18. PubMed ID: 14687928
[TBL] [Abstract][Full Text] [Related]
7. Effects of divalent cations on encapsulation and release in the GroEL-assisted folding.
Okuda H; Sakuhana C; Yamamoto R; Kawai R; Mizukami Y; Matsuda K
Biometals; 2007 Dec; 20(6):903-10. PubMed ID: 17242865
[TBL] [Abstract][Full Text] [Related]
8. Ligand-induced conformational changes in the apical domain of the chaperonin GroEL.
Gibbons DL; Horowitz PM
J Biol Chem; 1996 Jan; 271(1):238-43. PubMed ID: 8550566
[TBL] [Abstract][Full Text] [Related]
9. Protection of GroEL by its methionine residues against oxidation by hydrogen peroxide.
Melkani GC; Kestetter J; Sielaff R; Zardeneta G; Mendoza JA
Biochem Biophys Res Commun; 2006 Aug; 347(2):534-9. PubMed ID: 16828704
[TBL] [Abstract][Full Text] [Related]
10. The ATPase activity of GroEL is supported at high temperatures by divalent cations that stabilize its structure.
Melkani GC; Zardeneta G; Mendoza JA
Biometals; 2003 Sep; 16(3):479-84. PubMed ID: 12680712
[TBL] [Abstract][Full Text] [Related]
11. Partitioning of rhodanese onto GroEL. Chaperonin binds a reversibly oxidized form derived from the native protein.
Smith KE; Voziyan PA; Fisher MT
J Biol Chem; 1998 Oct; 273(44):28677-81. PubMed ID: 9786862
[TBL] [Abstract][Full Text] [Related]
12. Divalent cations can induce the exposure of GroEL hydrophobic surfaces and strengthen GroEL hydrophobic binding interactions. Novel effects of Zn2+ GroEL interactions.
Brazil BT; Ybarra J; Horowitz PM
J Biol Chem; 1998 Feb; 273(6):3257-63. PubMed ID: 9452440
[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. Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones.
Park ES; Fenton WA; Horwich AL
Proc Natl Acad Sci U S A; 2007 Feb; 104(7):2145-50. PubMed ID: 17283341
[TBL] [Abstract][Full Text] [Related]
15. A tubular biocontainer: metal ion-induced 1D assembly of a molecularly engineered chaperonin.
Biswas S; Kinbara K; Oya N; Ishii N; Taguchi H; Aida T
J Am Chem Soc; 2009 Jun; 131(22):7556-7. PubMed ID: 19489642
[TBL] [Abstract][Full Text] [Related]
16. alpha-Crystallin facilitates the reactivation of hydrogen peroxide-inactivated rhodanese.
Del Fierro D; Zardeneta G; Mendoza JA
Biochem Biophys Res Commun; 2000 Aug; 274(2):461-6. PubMed ID: 10913360
[TBL] [Abstract][Full Text] [Related]
17. Probing dynamics and conformational change of the GroEL-GroES complex by 13C NMR spectroscopy.
Nishida N; Motojima F; Idota M; Fujikawa H; Yoshida M; Shimada I; Kato K
J Biochem; 2006 Oct; 140(4):591-8. PubMed ID: 16963786
[TBL] [Abstract][Full Text] [Related]
18. Effect of hydrogen peroxide on the activity and structure of Escherichia coli chaperone GroEL.
Wang F; Ou WB; Li S; Zhou HM
Biochemistry (Mosc); 2002 May; 67(5):547-52. PubMed ID: 12059774
[TBL] [Abstract][Full Text] [Related]
19. Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner.
Kipnis Y; Papo N; Haran G; Horovitz A
Proc Natl Acad Sci U S A; 2007 Feb; 104(9):3119-24. PubMed ID: 17360617
[TBL] [Abstract][Full Text] [Related]
20. 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]
[Next] [New Search]