166 related articles for article (PubMed ID: 29512644)
1. [Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy].
Ryabova NA; Selivanova OM; Semisotnov GV
Mol Biol (Mosk); 2018; 52(1):120-124. PubMed ID: 29512644
[TBL] [Abstract][Full Text] [Related]
2. [Limited Trypsinolysis of GroES: The Effect on the Interaction with GroEL and Assembly In Vitro].
Marchenkov VV; Kotova NV; Muranova TA; Semisotnov GV
Mol Biol (Mosk); 2018; 52(1):82-87. PubMed ID: 29512639
[TBL] [Abstract][Full Text] [Related]
3. 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]
4. Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes.
Engel A; Hayer-Hartl MK; Goldie KN; Pfeifer G; Hegerl R; Müller S; da Silva AC; Baumeister W; Hartl FU
Science; 1995 Aug; 269(5225):832-6. PubMed ID: 7638600
[TBL] [Abstract][Full Text] [Related]
5. TEM and STEM-EDS evaluation of metal nanoparticle encapsulation in GroEL/GroES complexes according to the reaction mechanism of chaperonin.
Yoda H; Koike-Takeshita A
Microscopy (Oxf); 2021 Jun; 70(3):289-296. PubMed ID: 33173948
[TBL] [Abstract][Full Text] [Related]
6. GroEL and the GroEL-GroES Complex.
Ishii N
Subcell Biochem; 2017; 83():483-504. PubMed ID: 28271487
[TBL] [Abstract][Full Text] [Related]
7. An expanded protein folding cage in the GroEL-gp31 complex.
Clare DK; Bakkes PJ; van Heerikhuizen H; van der Vies SM; Saibil HR
J Mol Biol; 2006 May; 358(3):905-11. PubMed ID: 16549073
[TBL] [Abstract][Full Text] [Related]
8. Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.
Sameshima T; Ueno T; Iizuka R; Ishii N; Terada N; Okabe K; Funatsu T
J Biol Chem; 2008 Aug; 283(35):23765-73. PubMed ID: 18567585
[TBL] [Abstract][Full Text] [Related]
9. Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant.
Koike-Takeshita A; Yoshida M; Taguchi H
J Biol Chem; 2008 Aug; 283(35):23774-81. PubMed ID: 18567584
[TBL] [Abstract][Full Text] [Related]
10. Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes.
Farr GW; Fenton WA; Chaudhuri TK; Clare DK; Saibil HR; Horwich AL
EMBO J; 2003 Jul; 22(13):3220-30. PubMed ID: 12839985
[TBL] [Abstract][Full Text] [Related]
11. Transmission electron microscopy of GroEL, GroES, and the symmetrical GroEL/ES complex.
Harris JR; Plückthun A; Zahn R
J Struct Biol; 1994; 112(3):216-30. PubMed ID: 7986648
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.
Lin Z; Puchalla J; Shoup D; Rye HS
J Biol Chem; 2013 Oct; 288(43):30944-55. PubMed ID: 24022487
[TBL] [Abstract][Full Text] [Related]
14. Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES Complexes.
Haldar S; Gupta AJ; Yan X; Miličić G; Hartl FU; Hayer-Hartl M
J Mol Biol; 2015 Jun; 427(12):2244-55. PubMed ID: 25912285
[TBL] [Abstract][Full Text] [Related]
15. Productive folding of a tethered protein in the chaperonin GroEL-GroES cage.
Motojima F; Yoshida M
Biochem Biophys Res Commun; 2015 Oct; 466(1):72-5. PubMed ID: 26325470
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. 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]
18. Location and flexibility of the unique C-terminal tail of Aquifex aeolicus co-chaperonin protein 10 as derived by cryo-electron microscopy and biophysical techniques.
Chen DH; Luke K; Zhang J; Chiu W; Wittung-Stafshede P
J Mol Biol; 2008 Sep; 381(3):707-17. PubMed ID: 18588898
[TBL] [Abstract][Full Text] [Related]
19. The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate protein.
Weaver J; Rye HS
J Biol Chem; 2014 Aug; 289(33):23219-23232. PubMed ID: 24970895
[TBL] [Abstract][Full Text] [Related]
20. Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8Å reveals rearrangement between two GroEL rings.
Koike-Takeshita A; Arakawa T; Taguchi H; Shimamura T
J Mol Biol; 2014 Oct; 426(21):3634-41. PubMed ID: 25174333
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]