131 related articles for article (PubMed ID: 1361186)
1. A newly synthesized protein interacts with GroES on the surface of chaperonin GroEL.
Bochkareva ES; Girshovich AS
J Biol Chem; 1992 Dec; 267(36):25672-5. PubMed ID: 1361186
[TBL] [Abstract][Full Text] [Related]
2. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
Martin J; Mayhew M; Langer T; Hartl FU
Nature; 1993 Nov; 366(6452):228-33. PubMed ID: 7901770
[TBL] [Abstract][Full Text] [Related]
3. Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.
Martin J; Geromanos S; Tempst P; Hartl FU
Nature; 1993 Nov; 366(6452):279-82. PubMed ID: 7901771
[TBL] [Abstract][Full Text] [Related]
4. Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.
Bochkareva ES; Lissin NM; Girshovich AS
Nature; 1988 Nov; 336(6196):254-7. PubMed ID: 2904124
[TBL] [Abstract][Full Text] [Related]
5. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.
Langer T; Pfeifer G; Martin J; Baumeister W; Hartl FU
EMBO J; 1992 Dec; 11(13):4757-65. PubMed ID: 1361169
[TBL] [Abstract][Full Text] [Related]
6. Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli.
Kusukawa N; Yura T; Ueguchi C; Akiyama Y; Ito K
EMBO J; 1989 Nov; 8(11):3517-21. PubMed ID: 2573517
[TBL] [Abstract][Full Text] [Related]
7. Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.
Gragerov A; Nudler E; Komissarova N; Gaitanaris GA; Gottesman ME; Nikiforov V
Proc Natl Acad Sci U S A; 1992 Nov; 89(21):10341-4. PubMed ID: 1359538
[TBL] [Abstract][Full Text] [Related]
8. Positive cooperativity in the functioning of molecular chaperone GroEL.
Bochkareva ES; Lissin NM; Flynn GC; Rothman JE; Girshovich AS
J Biol Chem; 1992 Apr; 267(10):6796-800. PubMed ID: 1348056
[TBL] [Abstract][Full Text] [Related]
9. The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor.
Laminet AA; Ziegelhoffer T; Georgopoulos C; Plückthun A
EMBO J; 1990 Jul; 9(7):2315-9. PubMed ID: 2192863
[TBL] [Abstract][Full Text] [Related]
10. Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity.
Ziemienowicz A; Skowyra D; Zeilstra-Ryalls J; Fayet O; Georgopoulos C; Zylicz M
J Biol Chem; 1993 Dec; 268(34):25425-31. PubMed ID: 7902351
[TBL] [Abstract][Full Text] [Related]
11. Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivation.
Kawata Y; Nosaka K; Hongo K; Mizobata T; Nagai J
FEBS Lett; 1994 May; 345(2-3):229-32. PubMed ID: 7911090
[TBL] [Abstract][Full Text] [Related]
12. The formation of symmetrical GroEL-GroES complexes in the presence of ATP.
Llorca O; Marco S; Carrascosa JL; Valpuesta JM
FEBS Lett; 1994 May; 345(2-3):181-6. PubMed ID: 7911087
[TBL] [Abstract][Full Text] [Related]
13. 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]
14. 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]
15. Chaperonins groEL and groES promote assembly of heterotetramers (alpha 2 beta 2) of mammalian mitochondrial branched-chain alpha-keto acid decarboxylase in Escherichia coli.
Wynn RM; Davie JR; Cox RP; Chuang DT
J Biol Chem; 1992 Jun; 267(18):12400-3. PubMed ID: 1352285
[TBL] [Abstract][Full Text] [Related]
16. The effect of groES on the groEL-dependent assembly of dodecameric glutamine synthetase in the presence of ATP and ADP.
Fisher MT
J Biol Chem; 1994 May; 269(18):13629-36. PubMed ID: 7909810
[TBL] [Abstract][Full Text] [Related]
17. GroEL and the GroEL-GroES Complex.
Ishii N
Subcell Biochem; 2017; 83():483-504. PubMed ID: 28271487
[TBL] [Abstract][Full Text] [Related]
18. Characterization of a functionally important mobile domain of GroES.
Landry SJ; Zeilstra-Ryalls J; Fayet O; Georgopoulos C; Gierasch LM
Nature; 1993 Jul; 364(6434):255-8. PubMed ID: 8100614
[TBL] [Abstract][Full Text] [Related]
19. 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]
20. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells.
Thomas JG; Baneyx F
Mol Microbiol; 2000 Jun; 36(6):1360-70. PubMed ID: 10931286
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]