These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
122 related articles for article (PubMed ID: 22177460)
1. What distinguishes GroEL substrates from other Escherichia coli proteins? Azia A; Unger R; Horovitz A FEBS J; 2012 Feb; 279(4):543-50. PubMed ID: 22177460 [TBL] [Abstract][Full Text] [Related]
2. 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]
3. The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis. Mogk A; Homuth G; Scholz C; Kim L; Schmid FX; Schumann W EMBO J; 1997 Aug; 16(15):4579-90. PubMed ID: 9303302 [TBL] [Abstract][Full Text] [Related]
4. Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase. Ayling A; Baneyx F Protein Sci; 1996 Mar; 5(3):478-87. PubMed ID: 8868484 [TBL] [Abstract][Full Text] [Related]
5. Identification of novel in vivo obligate GroEL/ES substrates based on data from a cell-free proteomics approach. Niwa T; Fujiwara K; Taguchi H FEBS Lett; 2016 Jan; 590(2):251-7. PubMed ID: 26762164 [TBL] [Abstract][Full Text] [Related]
7. 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]
8. Conversion of a chaperonin GroEL-independent protein into an obligate substrate. Ishimoto T; Fujiwara K; Niwa T; Taguchi H J Biol Chem; 2014 Nov; 289(46):32073-32080. PubMed ID: 25288795 [TBL] [Abstract][Full Text] [Related]
9. Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli. Rinas U; Hoffmann F; Betiku E; Estapé D; Marten S J Biotechnol; 2007 Jan; 127(2):244-57. PubMed ID: 16945443 [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 systematic survey of in vivo obligate chaperonin-dependent substrates. Fujiwara K; Ishihama Y; Nakahigashi K; Soga T; Taguchi H EMBO J; 2010 May; 29(9):1552-64. PubMed ID: 20360681 [TBL] [Abstract][Full Text] [Related]
12. Protein folding in Escherichia coli: the chaperonin GroE and its substrates. Masters M; Blakely G; Coulson A; McLennan N; Yerko V; Acord J Res Microbiol; 2009 May; 160(4):267-77. PubMed ID: 19393741 [TBL] [Abstract][Full Text] [Related]
13. 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]
14. GroEL assisted folding of large polypeptide substrates in Escherichia coli: Present scenario and assignments for the future. Chaudhuri TK; Verma VK; Maheshwari A Prog Biophys Mol Biol; 2009 Jan; 99(1):42-50. PubMed ID: 19027782 [TBL] [Abstract][Full Text] [Related]
15. Shotgun Proteomics Revealed Preferential Degradation of Misfolded In Vivo Obligate GroE Substrates by Lon Protease in Niwa T; Chadani Y; Taguchi H Molecules; 2022 Jun; 27(12):. PubMed ID: 35744894 [TBL] [Abstract][Full Text] [Related]
16. Reconciling the controversy regarding the functional importance of bullet- and football-shaped GroE complexes. Bigman LS; Horovitz A J Biol Chem; 2019 Sep; 294(37):13527-13529. PubMed ID: 31371450 [TBL] [Abstract][Full Text] [Related]
17. The 69 kDa Escherichia coli maltodextrin glucosidase does not get encapsulated underneath GroES and folds through trans mechanism during GroEL/GroES-assisted folding. Paul S; Singh C; Mishra S; Chaudhuri TK FASEB J; 2007 Sep; 21(11):2874-85. PubMed ID: 17494995 [TBL] [Abstract][Full Text] [Related]
18. Low folding propensity and high translation efficiency distinguish in vivo substrates of GroEL from other Escherichia coli proteins. Noivirt-Brik O; Unger R; Horovitz A Bioinformatics; 2007 Dec; 23(24):3276-9. PubMed ID: 18006553 [TBL] [Abstract][Full Text] [Related]
19. Chaperonin-catalyzed rescue of kinetically trapped states in protein folding. Chakraborty K; Chatila M; Sinha J; Shi Q; Poschner BC; Sikor M; Jiang G; Lamb DC; Hartl FU; Hayer-Hartl M Cell; 2010 Jul; 142(1):112-22. PubMed ID: 20603018 [TBL] [Abstract][Full Text] [Related]
20. [Role of GroEL/GroES chaperonin system and Lon protease in regulation of expression Vibrio fischeri lux genes in Escherichia coli cells]. Manukhov IV; Kotova VIu; Zavil'genskiĭ GB Mol Biol (Mosk); 2006; 40(2):277-83. PubMed ID: 16637268 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]