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9. Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions. Behlke J; Ristau O; Schönfeld HJ Biochemistry; 1997 Apr; 36(17):5149-56. PubMed ID: 9136876 [TBL] [Abstract][Full Text] [Related]
10. How to orient the functional GroEL-SR1 mutant for atomic force microscopy investigations. Schiener J; Witt S; Hayer-Hartl M; Guckenberger R Biochem Biophys Res Commun; 2005 Mar; 328(2):477-83. PubMed ID: 15694372 [TBL] [Abstract][Full Text] [Related]
11. GroEL-assisted protein folding: does it occur within the chaperonin inner cavity? Marchenkov VV; Semisotnov GV Int J Mol Sci; 2009 May; 10(5):2066-2083. PubMed ID: 19564940 [TBL] [Abstract][Full Text] [Related]
12. Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components. Moparthi SB; Carlsson U; Vincentelli R; Jonsson BH; Hammarström P; Wenger J Sci Rep; 2016 Jun; 6():28386. PubMed ID: 27328749 [TBL] [Abstract][Full Text] [Related]
13. Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL. Yokokawa M; Wada C; Ando T; Sakai N; Yagi A; Yoshimura SH; Takeyasu K EMBO J; 2006 Oct; 25(19):4567-76. PubMed ID: 16977315 [TBL] [Abstract][Full Text] [Related]
14. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. Hayer-Hartl MK; Weber F; Hartl FU EMBO J; 1996 Nov; 15(22):6111-21. PubMed ID: 8947033 [TBL] [Abstract][Full Text] [Related]
15. 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; 38(11):1975-85. PubMed ID: 16822698 [TBL] [Abstract][Full Text] [Related]
16. Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate. Taguchi H J Mol Biol; 2015 Sep; 427(18):2912-8. PubMed ID: 25900372 [TBL] [Abstract][Full Text] [Related]
17. Phosphofructokinase interacts with molecular chaperonins GroEL and GroES. Melegh B; Minami Y Acta Biol Hung; 1997; 48(4):399-407. PubMed ID: 9847453 [TBL] [Abstract][Full Text] [Related]
18. Gly192 at hinge 2 site in the chaperonin GroEL plays a pivotal role in the dynamic apical domain movement that leads to GroES binding and efficient encapsulation of substrate proteins. Machida K; Fujiwara R; Tanaka T; Sakane I; Hongo K; Mizobata T; Kawata Y Biochim Biophys Acta; 2009 Sep; 1794(9):1344-54. PubMed ID: 19130907 [TBL] [Abstract][Full Text] [Related]
19. Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings. Llorca O; Marco S; Carrascosa JL; Valpuesta JM FEBS Lett; 1997 Mar; 405(2):195-9. PubMed ID: 9089290 [TBL] [Abstract][Full Text] [Related]
20. 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; 278(1):267-78. PubMed ID: 9571049 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]