| Title | Date | PubMed ID |
|---|
| The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding. | 2016 Jan | 26422689 |
| Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system. | 2015 Oct 9 | 26271593 |
| Dynamics, flexibility, and allostery in molecular chaperonins. | 2015 Sep 14 | 26140986 |
| Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES Complexes. | 2015 Jun 19 | 25912285 |
| The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation. | 2015 | 25822285 |
| Characterization of the chaperonin GroEL in Mycoplasma gallisepticum. | 2015 Mar | 25304689 |
| Asp-52 in combination with Asp-398 plays a critical role in ATP hydrolysis of chaperonin GroEL. | 2014 Oct 24 | 25202010 |
| Structure and allostery of the chaperonin GroEL. | 2013 May 13 | 23183375 |
| Interaction of oxidized chaperonin GroEL with an unfolded protein at low temperatures. | 2012 Jun | 22273181 |
| ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin. | 2012 Mar 30 | 22445172 |