154 related articles for article (PubMed ID: 29037137)
1. Heterologous Expression of Chaperones from Hyperthermophilic Archaea Inhibits Aminoglycoside-Induced Protein Misfolding in Escherichia coli.
Peng S; Chu Z; Lu J; Li D; Wang Y; Yang S; Zhang Y
Biochemistry (Mosc); 2017 Oct; 82(10):1169-1175. PubMed ID: 29037137
[TBL] [Abstract][Full Text] [Related]
2. 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]
3. Chaperonins fight aminoglycoside-induced protein misfolding and promote short-term tolerance in Escherichia coli.
Goltermann L; Good L; Bentin T
J Biol Chem; 2013 Apr; 288(15):10483-9. PubMed ID: 23447537
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. GroES and GroEL are essential chaperones for refolding of recombinant human phospholipid scramblase 1 in E. coli.
Sahu SK; Rajasekharan A; Gummadi SN
Biotechnol Lett; 2009 Nov; 31(11):1745-52. PubMed ID: 19590828
[TBL] [Abstract][Full Text] [Related]
6. Coexpression of chaperonin GroEL/GroES markedly enhanced soluble and functional expression of recombinant human interferon-gamma in Escherichia coli.
Yan X; Hu S; Guan YX; Yao SJ
Appl Microbiol Biotechnol; 2012 Feb; 93(3):1065-74. PubMed ID: 21975693
[TBL] [Abstract][Full Text] [Related]
7. Molecular chaperone GroEL/ES: unfolding and refolding processes.
Ryabova NA; Marchenkov VV; Marchenkova SY; Kotova NV; Semisotnov GV
Biochemistry (Mosc); 2013 Dec; 78(13):1405-14. PubMed ID: 24490731
[TBL] [Abstract][Full Text] [Related]
8. Folding while bound to chaperones.
Horowitz S; Koldewey P; Stull F; Bardwell JC
Curr Opin Struct Biol; 2018 Feb; 48():1-5. PubMed ID: 28734135
[TBL] [Abstract][Full Text] [Related]
9. A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo.
Nielsen KL; McLennan N; Masters M; Cowan NJ
J Bacteriol; 1999 Sep; 181(18):5871-5. PubMed ID: 10482535
[TBL] [Abstract][Full Text] [Related]
10. Improvement of extracellular bacterial protein production in Pichia pastoris by co-expression of endoplasmic reticulum residing GroEL-GroES.
Summpunn P; Jomrit J; Panbangred W
J Biosci Bioeng; 2018 Mar; 125(3):268-274. PubMed ID: 29046263
[TBL] [Abstract][Full Text] [Related]
11. Consortium of fold-catalyzing proteins increases soluble expression of cyclohexanone monooxygenase in recombinant Escherichia coli.
Lee DH; Kim MD; Lee WH; Kweon DH; Seo JH
Appl Microbiol Biotechnol; 2004 Feb; 63(5):549-52. PubMed ID: 12827321
[TBL] [Abstract][Full Text] [Related]
12. Over-expression and characterization of recombinant prefoldin from hyperthermophilic archaeum Pyrococcus furiosus in E. coli.
Chen H; Yang L; Zhang Y; Yang S
Biotechnol Lett; 2010 Mar; 32(3):429-34. PubMed ID: 19898753
[TBL] [Abstract][Full Text] [Related]
13. Co-expression of chaperones from P. furiosus enhanced the soluble expression of the recombinant hyperthermophilic α-amylase in E. coli.
Peng S; Chu Z; Lu J; Li D; Wang Y; Yang S; Zhang Y
Cell Stress Chaperones; 2016 May; 21(3):477-84. PubMed ID: 26862080
[TBL] [Abstract][Full Text] [Related]
14. Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.
Illingworth M; Salisbury J; Li W; Lin D; Chen L
Biochem Biophys Res Commun; 2015 Oct; 466(1):15-20. PubMed ID: 26271593
[TBL] [Abstract][Full Text] [Related]
15. Overproduction of the Escherichia coli Chaperones GroEL-GroES in Rhodococcus ruber Improves the Activity and Stability of Cell Catalysts Harboring a Nitrile Hydratase.
Tian Y; Chen J; Yu H; Shen Z
J Microbiol Biotechnol; 2016 Feb; 26(2):337-46. PubMed ID: 26562693
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones.
de Marco A; Vigh L; Diamant S; Goloubinoff P
Cell Stress Chaperones; 2005; 10(4):329-39. PubMed ID: 16333986
[TBL] [Abstract][Full Text] [Related]
18. [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]
19. Overexpression of prefoldin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3 endowed Escherichia coli with organic solvent tolerance.
Okochi M; Kanie K; Kurimoto M; Yohda M; Honda H
Appl Microbiol Biotechnol; 2008 Jun; 79(3):443-9. PubMed ID: 18443786
[TBL] [Abstract][Full Text] [Related]
20. 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]
[Next] [New Search]