Goloubinoff P - Search Results

1

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

Goloubinoff P, Gatenby AA, Lorimer GH. Goloubinoff P, et al. Nature. 1989 Jan 5;337(6202):44-7. doi: 10.1038/337044a0. Nature. 1989. PMID: 2562907

2

Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH. Goloubinoff P, et al. Nature. 1989 Dec 21-28;342(6252):884-9. doi: 10.1038/342884a0. Nature. 1989. PMID: 10532860

3

Purification of mammalian mitochondrial chaperonin 60 through in vitro reconstitution of active oligomers.

Viitanen PV, Lorimer G, Bergmeier W, Weiss C, Kessel M, Goloubinoff P. Viitanen PV, et al. Among authors: goloubinoff p. Methods Enzymol. 1998;290:203-17. doi: 10.1016/s0076-6879(98)90020-9. Methods Enzymol. 1998. PMID: 9534164 No abstract available.

4

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent.

Viitanen PV, Lubben TH, Reed J, Goloubinoff P, O'Keefe DP, Lorimer GH. Viitanen PV, et al. Among authors: goloubinoff p. Biochemistry. 1990 Jun 19;29(24):5665-71. doi: 10.1021/bi00476a003. Biochemistry. 1990. PMID: 1974461

5

Minimal and optimal mechanisms for GroE-mediated protein folding.

Ben-Zvi AP, Chatellier J, Fersht AR, Goloubinoff P. Ben-Zvi AP, et al. Among authors: goloubinoff p. 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.

6

The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network.

Veinger L, Diamant S, Buchner J, Goloubinoff P. Veinger L, et al. Among authors: goloubinoff p. J Biol Chem. 1998 May 1;273(18):11032-7. doi: 10.1074/jbc.273.18.11032. J Biol Chem. 1998. PMID: 9556585

7

Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins.

Goloubinoff P, Sassi AS, Fauvet B, Barducci A, De Los Rios P. Goloubinoff P, et al. Nat Chem Biol. 2018 Apr;14(4):388-395. doi: 10.1038/s41589-018-0013-8. Epub 2018 Mar 5. Nat Chem Biol. 2018. PMID: 29507388

8

Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer.

Azem A, Kessel M, Goloubinoff P. Azem A, et al. Among authors: goloubinoff p. Science. 1994 Jul 29;265(5172):653-6. doi: 10.1126/science.7913553. Science. 1994. PMID: 7913553

9

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

10

Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones.

Ben-Zvi AP, Goloubinoff P. Ben-Zvi AP, et al. Among authors: goloubinoff p. J Struct Biol. 2001 Aug;135(2):84-93. doi: 10.1006/jsbi.2001.4352. J Struct Biol. 2001. PMID: 11580258 Review.

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