226 related articles for article (PubMed ID: 7961406)
1. 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]
2. 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]
3. From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.
Chatellier J; Hill F; Foster NW; Goloubinoff P; Fersht AR
J Mol Biol; 2000 Dec; 304(5):897-910. PubMed ID: 11124035
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. From minichaperone to GroEL 2: importance of avidity of the multisite ring structure.
Chatellier J; Hill F; Fersht AR
J Mol Biol; 2000 Dec; 304(5):883-96. PubMed ID: 11124034
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL.
Sivinski J; Ambrose AJ; Panfilenko I; Zerio CJ; Machulis JM; Mollasalehi N; Kaneko LK; Stevens M; Ray AM; Park Y; Wu C; Hoang QQ; Johnson SM; Chapman E
mBio; 2021 Jan; 12(1):. PubMed ID: 33436430
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. Substrate mutations that bypass a specific Cpn10 chaperonin requirement for protein folding.
Andreadis JD; Black LW
J Biol Chem; 1998 Dec; 273(51):34075-86. PubMed ID: 9852065
[TBL] [Abstract][Full Text] [Related]
10. Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction.
Illingworth M; Ellis H; Chen L
Sci Rep; 2017 Aug; 7(1):9710. PubMed ID: 28852160
[TBL] [Abstract][Full Text] [Related]
11. Dissociation kinetics of the GroEL-gp31 chaperonin complex studied with Förster resonance energy transfer.
Calmat S; Hendriks J; van Heerikhuizen H; Schmidt CF; van der Vies SM; Peterman EJ
Biochemistry; 2009 Dec; 48(49):11692-8. PubMed ID: 19899806
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. 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]
14. Factors governing the substrate recognition by GroEL chaperone: a sequence correlation approach.
Chaudhuri TK; Gupta P
Cell Stress Chaperones; 2005; 10(1):24-36. PubMed ID: 15832945
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. 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]
17. GroEL-GroES-mediated protein folding requires an intact central cavity.
Wang JD; Michelitsch MD; Weissman JS
Proc Natl Acad Sci U S A; 1998 Oct; 95(21):12163-8. PubMed ID: 9770457
[TBL] [Abstract][Full Text] [Related]
18. An ORFan no more: the bacteriophage T4 39.2 gene product, NwgI, modulates GroEL chaperone function.
Ang D; Georgopoulos C
Genetics; 2012 Mar; 190(3):989-1000. PubMed ID: 22234860
[TBL] [Abstract][Full Text] [Related]
19. Cloning and characterization of the groE heat-shock operon of the marine bacterium Vibrio harveyi.
Kuchanny-Ardigò D; Lipińska B
Microbiology (Reading); 2003 Jun; 149(Pt 6):1483-1492. PubMed ID: 12777488
[TBL] [Abstract][Full Text] [Related]
20. Reversible oligomerization and denaturation of the chaperonin GroES.
Seale JW; Gorovits BM; Ybarra J; Horowitz PM
Biochemistry; 1996 Apr; 35(13):4079-83. PubMed ID: 8672442
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
