| 1 |
28017766 | Folding and unfolding pathway of chaperonin GroEL monomer and elucidation of thermodynamic parameters. | 2017 Mar |
3 |
| 2 |
22273181 | Interaction of oxidized chaperonin GroEL with an unfolded protein at low temperatures. | 2012 Jun |
3 |
| 3 |
15710410 | No evidence for a forced-unfolding mechanism during ATP/GroES binding to substrate-bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL-bound Rubisco from tritium exchange. | 2005 Feb 14 |
1 |
| 4 |
14687928 | Hydrogen peroxide induces the dissociation of GroEL into monomers that can facilitate the reactivation of oxidatively inactivated rhodanese. | 2004 Mar |
1 |
| 5 |
12790657 | On-column refolding of recombinant human interferon-gamma with an immobilized chaperone fragment. | 2003 May-Jun |
2 |
| 6 |
11841236 | Rhodanese can partially refold in its GroEL-GroES-ADP complex and can be released to give a homogeneous product. | 2002 Feb 19 |
3 |
| 7 |
12061791 | GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation. | 2002 Jun 21 |
1 |
| 8 |
11020386 | Excluded volume effects on the refolding and assembly of an oligomeric protein. GroEL, a case study. | 2001 Jan 12 |
1 |
| 9 |
10757973 | Unfolding and disassembly of the chaperonin GroEL occurs via a tetradecameric intermediate with a folded equatorial domain. | 2000 Apr 18 |
1 |
| 10 |
11222029 | The lower hydrolysis of ATP by the stress protein GroEL is a major factor responsible for the diminished chaperonin activity at low temperature. | 2000 Dec |
2 |
| 11 |
10187830 | Mechanisms for GroEL/GroES-mediated folding of a large 86-kDa fusion polypeptide in vitro. | 1999 Apr 9 |
1 |
| 12 |
10495893 | [Monomeric form of the molecular chaperone GroEL: structure, stability, and oligomerization]. | 1999 May |
1 |
| 13 |
9452440 | Divalent cations can induce the exposure of GroEL hydrophobic surfaces and strengthen GroEL hydrophobic binding interactions. Novel effects of Zn2+ GroEL interactions. | 1998 Feb 6 |
1 |
| 14 |
9786862 | Partitioning of rhodanese onto GroEL. Chaperonin binds a reversibly oxidized form derived from the native protein. | 1998 Oct 30 |
1 |
| 15 |
8995221 | Conditions of forming protein complexes with GroEL can influence the mechanism of chaperonin-assisted refolding. | 1997 Jan 3 |
1 |
| 16 |
9330224 | Preformed GroES oligomers are not required as functional cochaperonins. | 1997 Oct |
1 |
| 17 |
7499369 | The chaperonin GroEL is destabilized by binding of ADP. | 1995 Dec 1 |
1 |
| 18 |
7577988 | Residual structure in urea-denatured chaperonin GroEL. | 1995 Oct 24 |
4 |
| 19 |
7665563 | Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding. | 1995 Sep 15 |
1 |
| 20 |
7673187 | Refolding and reassembly of active chaperonin GroEL after denaturation. | 1995 Sep 22 |
1 |
| 21 |
7696310 | Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent. | 1995 Mar 15 |
6 |
| 22 |
7706275 | Exposure of hydrophobic surfaces on the chaperonin GroEL oligomer by protonation or modification of His-401. | 1995 Mar 31 |
2 |
| 23 |
7905478 | Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action. | 1994 Jan 28 |
3 |