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2. On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein folding. Hayer-Hartl MK, Ewalt KL, Hartl FU. Biol Chem; 1999 May; 380(5):531-40. PubMed ID: 10384959 [Abstract] [Full Text] [Related]
7. Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity. Betancourt MR, Thirumalai D. J Mol Biol; 1999 Apr 02; 287(3):627-44. PubMed ID: 10092464 [Abstract] [Full Text] [Related]
8. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings. Kad NM, Ranson NA, Cliff MJ, Clarke AR. J Mol Biol; 1998 Apr 24; 278(1):267-78. PubMed ID: 9571049 [Abstract] [Full Text] [Related]
9. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Martin J, Mayhew M, Langer T, Hartl FU. Nature; 1993 Nov 18; 366(6452):228-33. PubMed ID: 7901770 [Abstract] [Full Text] [Related]
11. Minimal and optimal mechanisms for GroE-mediated protein folding. Ben-Zvi AP, Chatellier J, Fersht AR, Goloubinoff P. Proc Natl Acad Sci U S A; 1998 Dec 22; 95(26):15275-80. PubMed ID: 9860959 [Abstract] [Full Text] [Related]
13. Design of a molecular chaperone-assisted protein folding bioreactor. Kohler RJ, Preuss M, Miller AD. Biotechnol Prog; 2000 Dec 22; 16(4):671-5. PubMed ID: 10933845 [Abstract] [Full Text] [Related]
14. Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli. Gupta P, Aggarwal N, Batra P, Mishra S, Chaudhuri TK. Int J Biochem Cell Biol; 2006 Dec 22; 38(11):1975-85. PubMed ID: 16822698 [Abstract] [Full Text] [Related]
15. Specificity in chaperonin-mediated protein folding. Tian G, Vainberg IE, Tap WD, Lewis SA, Cowan NJ. Nature; 1995 May 18; 375(6528):250-3. PubMed ID: 7746329 [Abstract] [Full Text] [Related]