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8. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Kerner MJ; Naylor DJ; Ishihama Y; Maier T; Chang HC; Stines AP; Georgopoulos C; Frishman D; Hayer-Hartl M; Mann M; Hartl FU Cell; 2005 Jul; 122(2):209-20. PubMed ID: 16051146 [TBL] [Abstract][Full Text] [Related]
9. Catalysis, commitment and encapsulation during GroE-mediated folding. Beissinger M; Rutkat K; Buchner J J Mol Biol; 1999 Jun; 289(4):1075-92. PubMed ID: 10369783 [TBL] [Abstract][Full Text] [Related]
10. Prediction of chaperonin GroE substrates using small structural patterns of proteins. Minami S; Niwa T; Uemura E; Koike R; Taguchi H; Ota M FEBS Open Bio; 2023 Apr; 13(4):779-794. PubMed ID: 36869604 [TBL] [Abstract][Full Text] [Related]
11. A comparison of the GroE chaperonin requirements for sequentially and structurally homologous malate dehydrogenases: the importance of folding kinetics and solution environment. Tieman BC; Johnston MF; Fisher MT J Biol Chem; 2001 Nov; 276(48):44541-50. PubMed ID: 11551947 [TBL] [Abstract][Full Text] [Related]
12. 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; 95(26):15275-80. PubMed ID: 9860959 [TBL] [Abstract][Full Text] [Related]
13. Refolding of yeast enolase in the presence of the chaperonin GroE. The nucleotide specificity of GroE and the role of GroES. Kubo T; Mizobata T; Kawata Y J Biol Chem; 1993 Sep; 268(26):19346-51. PubMed ID: 8103517 [TBL] [Abstract][Full Text] [Related]
14. Filamentous morphology in GroE-depleted Escherichia coli induced by impaired folding of FtsE. Fujiwara K; Taguchi H J Bacteriol; 2007 Aug; 189(16):5860-6. PubMed ID: 17557821 [TBL] [Abstract][Full Text] [Related]
15. Structure and function of the GroE chaperone. Walter S Cell Mol Life Sci; 2002 Oct; 59(10):1589-97. PubMed ID: 12475168 [TBL] [Abstract][Full Text] [Related]
16. Error-prone DNA polymerase IV is regulated by the heat shock chaperone GroE in Escherichia coli. Layton JC; Foster PL J Bacteriol; 2005 Jan; 187(2):449-57. PubMed ID: 15629916 [TBL] [Abstract][Full Text] [Related]
17. The Escherichia coli groE chaperonins. Georgopoulos C; Ang D Semin Cell Biol; 1990 Feb; 1(1):19-25. PubMed ID: 1983267 [TBL] [Abstract][Full Text] [Related]
18. In vivo protein folding: suppressor analysis of mutations in the groES cochaperone gene of Escherichia coli. Zeilstra-Ryalls J; Fayet O; Georgopoulos C FASEB J; 1996 Jan; 10(1):148-52. PubMed ID: 8566535 [TBL] [Abstract][Full Text] [Related]
19. Two classes of extragenic suppressor mutations identify functionally distinct regions of the GroEL chaperone of Escherichia coli. Zeilstra-Ryalls J; Fayet O; Georgopoulos C J Bacteriol; 1994 Nov; 176(21):6558-65. PubMed ID: 7961406 [TBL] [Abstract][Full Text] [Related]
20. A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin. Natesh R; Clare DK; Farr GW; Horwich AL; Saibil HR Int J Biol Macromol; 2018 Oct; 118(Pt A):671-675. PubMed ID: 29959019 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]