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4. A thermophilic mini-chaperonin contains a conserved polypeptide-binding surface: combined crystallographic and NMR studies of the GroEL apical domain with implications for substrate interactions. Hua Q, Dementieva IS, Walsh MA, Hallenga K, Weiss MA, Joachimiak A. J Mol Biol; 2001 Feb 23; 306(3):513-25. PubMed ID: 11178910 [Abstract] [Full Text] [Related]
5. From minichaperone to GroEL 2: importance of avidity of the multisite ring structure. Chatellier J, Hill F, Fersht AR. J Mol Biol; 2000 Dec 15; 304(5):883-96. PubMed ID: 11124034 [Abstract] [Full Text] [Related]
8. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL. Cliff MJ, Kad NM, Hay N, Lund PA, Webb MR, Burston SG, Clarke AR. J Mol Biol; 1999 Oct 29; 293(3):667-84. PubMed ID: 10543958 [Abstract] [Full Text] [Related]
17. The structural stability of the co-chaperonin GroES. Boudker O, Todd MJ, Freire E. J Mol Biol; 1997 Oct 10; 272(5):770-9. PubMed ID: 9368656 [Abstract] [Full Text] [Related]
20. Effect of hydrogen peroxide on the activity and structure of Escherichia coli chaperone GroEL. Wang F, Ou WB, Li S, Zhou HM. Biochemistry (Mosc); 2002 May 10; 67(5):547-52. PubMed ID: 12059774 [Abstract] [Full Text] [Related] Page: [Next] [New Search]