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GroES binding regulates GroEL chaperonin activity under heat shock.
Goloubinoff P, Diamant S, Weiss C, Azem A. Goloubinoff P, et al. FEBS Lett. 1997 Apr 28;407(2):215-9. doi: 10.1016/s0014-5793(97)00348-7. FEBS Lett. 1997. PMID: 9166902
From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.
Chatellier J, Hill F, Foster NW, Goloubinoff P, Fersht AR. Chatellier J, et al. J Mol Biol. 2000 Dec 15;304(5):897-910. doi: 10.1006/jmbi.2000.4278. J Mol Biol. 2000. PMID: 11124035
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.
Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B. Goloubinoff P, et al. Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13732-7. doi: 10.1073/pnas.96.24.13732. Proc Natl Acad Sci U S A. 1999. PMID: 10570141 Free PMC article.
Minimal and optimal mechanisms for GroE-mediated protein folding.
Ben-Zvi AP, Chatellier J, Fersht AR, Goloubinoff P. Ben-Zvi AP, et al. Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15275-80. doi: 10.1073/pnas.95.26.15275. Proc Natl Acad Sci U S A. 1998. PMID: 9860959 Free PMC article.
Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration.
Diamant S, Goloubinoff P. Diamant S, et al. Biochemistry. 1998 Jul 7;37(27):9688-94. doi: 10.1021/bi980338u. Biochemistry. 1998. PMID: 9657681
Structural analysis of GroE chaperonin complexes using chemical cross-linking.
Azem A, Weiss C, Goloubinoff P. Azem A, et al. Methods Enzymol. 1998;290:253-68. doi: 10.1016/s0076-6879(98)90024-6. Methods Enzymol. 1998. PMID: 9534168
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