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Divalent cations stabilize GroEL under conditions of oxidative stress.
Biochem Biophys Res Commun. 2008 Apr 11;368(3):625-30. doi: 10.1016/j.bbrc.2008.01.126. Epub 2008 Feb 6.
Biochem Biophys Res Commun. 2008.
PMID: 18261461
On the chaperonin activity of GroEL at heat-shock temperature.
Melkani GC, Zardeneta G, Mendoza JA.
Melkani GC, et al.
Int J Biochem Cell Biol. 2005 Jul;37(7):1375-85. doi: 10.1016/j.biocel.2005.01.007.
Int J Biochem Cell Biol. 2005.
PMID: 15833270
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Oxidized GroEL can function as a chaperonin.
Melkani GC, Zardeneta G, Mendoza JA.
Melkani GC, et al.
Front Biosci. 2004 Jan 1;9:724-31. doi: 10.2741/1258.
Front Biosci. 2004.
PMID: 14766403
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The ATPase activity of GroEL is supported at high temperatures by divalent cations that stabilize its structure.
Melkani GC, Zardeneta G, Mendoza JA.
Melkani GC, et al.
Biometals. 2003 Sep;16(3):479-84. doi: 10.1023/a:1022536219800.
Biometals. 2003.
PMID: 12680712
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GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation.
Melkani GC, Zardeneta G, Mendoza JA.
Melkani GC, et al.
Biochem Biophys Res Commun. 2002 Jun 21;294(4):893-9. doi: 10.1016/S0006-291X(02)00575-2.
Biochem Biophys Res Commun. 2002.
PMID: 12061791
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alpha-Crystallin facilitates the reactivation of hydrogen peroxide-inactivated rhodanese.
Del Fierro D, Zardeneta G, Mendoza JA.
Del Fierro D, et al.
Biochem Biophys Res Commun. 2000 Aug 2;274(2):461-6. doi: 10.1006/bbrc.2000.3165.
Biochem Biophys Res Commun. 2000.
PMID: 10913360
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