These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Journal Abstract Search
317 related items for PubMed ID: 9312423
1. Role of chaperonins in protein folding. A new model of the GroEL/GroES complex architecture. Basharov MA. Biochemistry (Mosc); 1997 Apr; 62(4):416-24. PubMed ID: 9312423 [Abstract] [Full Text] [Related]
8. Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. Shimamura T, Koike-Takeshita A, Yokoyama K, Masui R, Murai N, Yoshida M, Taguchi H, Iwata S. Structure; 2004 Aug 29; 12(8):1471-80. PubMed ID: 15296740 [Abstract] [Full Text] [Related]
9. Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding. Motojima F, Makio T, Aoki K, Makino Y, Kuwajima K, Yoshida M. Biochem Biophys Res Commun; 2000 Jan 27; 267(3):842-9. PubMed ID: 10673379 [Abstract] [Full Text] [Related]
14. Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Tang YC, Chang HC, Roeben A, Wischnewski D, Wischnewski N, Kerner MJ, Hartl FU, Hayer-Hartl M. Cell; 2006 Jun 02; 125(5):903-14. PubMed ID: 16751100 [Abstract] [Full Text] [Related]
15. Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES Complexes. Haldar S, Gupta AJ, Yan X, Miličić G, Hartl FU, Hayer-Hartl M. J Mol Biol; 2015 Jun 19; 427(12):2244-55. PubMed ID: 25912285 [Abstract] [Full Text] [Related]
16. The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding. Weber F, Keppel F, Georgopoulos C, Hayer-Hartl MK, Hartl FU. Nat Struct Biol; 1998 Nov 19; 5(11):977-85. PubMed ID: 9808043 [Abstract] [Full Text] [Related]