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7. Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP. Makino Y; Taguchi H; Yoshida M FEBS Lett; 1993 Dec; 336(2):363-7. PubMed ID: 7903258 [TBL] [Abstract][Full Text] [Related]
8. GroEL walks the fine line: the subtle balance of substrate and co-chaperonin binding by GroEL. A combinatorial investigation by design, selection and screening. Kawe M; Plückthun A J Mol Biol; 2006 Mar; 357(2):411-26. PubMed ID: 16427651 [TBL] [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; 267(3):842-9. PubMed ID: 10673379 [TBL] [Abstract][Full Text] [Related]
10. On the chaperonin activity of GroEL at heat-shock temperature. Melkani GC; Zardeneta G; Mendoza JA Int J Biochem Cell Biol; 2005 Jul; 37(7):1375-85. PubMed ID: 15833270 [TBL] [Abstract][Full Text] [Related]
11. Characterisation of mutations in GroES that allow GroEL to function as a single ring. Liu H; Kovács E; Lund PA FEBS Lett; 2009 Jul; 583(14):2365-71. PubMed ID: 19545569 [TBL] [Abstract][Full Text] [Related]
12. Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure. Aharoni A; Horovitz A J Mol Biol; 1996 May; 258(5):732-5. PubMed ID: 8637005 [TBL] [Abstract][Full Text] [Related]
13. Functional consequences of single:double ring transitions in chaperonins: life in the cold. Ferrer M; Lünsdorf H; Chernikova TN; Yakimov M; Timmis KN; Golyshin PN Mol Microbiol; 2004 Jul; 53(1):167-82. PubMed ID: 15225312 [TBL] [Abstract][Full Text] [Related]
14. Identification of a GroES (CPN10)-related sequence motif in the GroEL (CPN60) chaperonins. Gupta RS Biochem Mol Biol Int; 1994 Jun; 33(3):591-5. PubMed ID: 7951076 [TBL] [Abstract][Full Text] [Related]
15. Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL. Clark AC; Hugo E; Frieden C Biochemistry; 1996 May; 35(18):5893-901. PubMed ID: 8639551 [TBL] [Abstract][Full Text] [Related]
16. The chaperonin GroEL binds a polypeptide in an alpha-helical conformation. Landry SJ; Gierasch LM Biochemistry; 1991 Jul; 30(30):7359-62. PubMed ID: 1677268 [TBL] [Abstract][Full Text] [Related]
17. Release of both native and non-native proteins from a cis-only GroEL ternary complex. Burston SG; Weissman JS; Farr GW; Fenton WA; Horwich AL Nature; 1996 Sep; 383(6595):96-9. PubMed ID: 8779722 [TBL] [Abstract][Full Text] [Related]
18. The lower hydrolysis of ATP by the stress protein GroEL is a major factor responsible for the diminished chaperonin activity at low temperature. Mendoza JA; Dulin P; Warren T Cryobiology; 2000 Dec; 41(4):319-23. PubMed ID: 11222029 [TBL] [Abstract][Full Text] [Related]
19. An arginine residue (Arg101), which is conserved in many GroEL homologues, is required for interactions between the two heptameric rings. Jones S; Wallington EJ; George R; Lund PA J Mol Biol; 1998 Oct; 282(4):789-800. PubMed ID: 9743627 [TBL] [Abstract][Full Text] [Related]
20. An additional serine residue at the C terminus of rhodanese destabilizes the enzyme. Kramer G; Ramachandiran V; Horowitz P; Hardesty B Arch Biochem Biophys; 2001 Jan; 385(2):332-7. PubMed ID: 11368014 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]