190 related articles for article (PubMed ID: 10380224)
1. Chaperonin function depends on structure and disorder in co-chaperonin mobile loops.
Landry SJ; Steede NK; Garaudy AM; Maskos K; Viitanen PV
Pac Symp Biocomput; 1999; ():520-31. PubMed ID: 10380224
[TBL] [Abstract][Full Text] [Related]
2. The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli.
Richardson A; Schwager F; Landry SJ; Georgopoulos C
J Biol Chem; 2001 Feb; 276(7):4981-7. PubMed ID: 11050098
[TBL] [Abstract][Full Text] [Related]
3. Interplay of structure and disorder in cochaperonin mobile loops.
Landry SJ; Taher A; Georgopoulos C; van der Vies SM
Proc Natl Acad Sci U S A; 1996 Oct; 93(21):11622-7. PubMed ID: 8876186
[TBL] [Abstract][Full Text] [Related]
4. Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.
Taguchi H
J Mol Biol; 2015 Sep; 427(18):2912-8. PubMed ID: 25900372
[TBL] [Abstract][Full Text] [Related]
5. Compensatory changes in GroEL/Gp31 affinity as a mechanism for allele-specific genetic interaction.
Richardson A; van der Vies SM; Keppel F; Taher A; Landry SJ; Georgopoulos C
J Biol Chem; 1999 Jan; 274(1):52-8. PubMed ID: 9867810
[TBL] [Abstract][Full Text] [Related]
6. Pseudo-T-even bacteriophage RB49 encodes CocO, a cochaperonin for GroEL, which can substitute for Escherichia coli's GroES and bacteriophage T4's Gp31.
Ang D; Richardson A; Mayer MP; Keppel F; Krisch H; Georgopoulos C
J Biol Chem; 2001 Mar; 276(12):8720-6. PubMed ID: 11104767
[TBL] [Abstract][Full Text] [Related]
7. Chaperonin-co-chaperonin interactions.
Boshoff A
Subcell Biochem; 2015; 78():153-78. PubMed ID: 25487021
[TBL] [Abstract][Full Text] [Related]
8. Flexibility of GroES mobile loop is required for efficient chaperonin function.
Nojima T; Ikegami T; Taguchi H; Yoshida M
J Mol Biol; 2012 Sep; 422(2):291-9. PubMed ID: 22634549
[TBL] [Abstract][Full Text] [Related]
9. The disordered mobile loop of GroES folds into a defined beta-hairpin upon binding GroEL.
Shewmaker F; Maskos K; Simmerling C; Landry SJ
J Biol Chem; 2001 Aug; 276(33):31257-64. PubMed ID: 11395498
[TBL] [Abstract][Full Text] [Related]
10. Chaperonin: Co-chaperonin Interactions.
Boshoff A
Subcell Biochem; 2023; 101():213-246. PubMed ID: 36520309
[TBL] [Abstract][Full Text] [Related]
11. Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae.
Mande SC; Mehra V; Bloom BR; Hol WG
Science; 1996 Jan; 271(5246):203-7. PubMed ID: 8539620
[TBL] [Abstract][Full Text] [Related]
12. Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria.
Höhfeld J; Hartl FU
J Cell Biol; 1994 Jul; 126(2):305-15. PubMed ID: 7913473
[TBL] [Abstract][Full Text] [Related]
13. A role for confined water in chaperonin function.
England JL; Lucent D; Pande VS
J Am Chem Soc; 2008 Sep; 130(36):11838-9. PubMed ID: 18710231
[TBL] [Abstract][Full Text] [Related]
14. Archaeal group II chaperonin mediates protein folding in the cis-cavity without a detachable GroES-like co-chaperonin.
Yoshida T; Kawaguchi R; Taguchi H; Yoshida M; Yasunaga T; Wakabayashi T; Yohda M; Maruyama T
J Mol Biol; 2002 Jan; 315(1):73-85. PubMed ID: 11771967
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. Role of chaperonins in protein folding. A new model of the GroEL/GroES complex architecture.
Basharov MA
Biochemistry (Mosc); 1997 Apr; 62(4):416-24. PubMed ID: 9312423
[TBL] [Abstract][Full Text] [Related]
17. A mobile loop order-disorder transition modulates the speed of chaperonin cycling.
Shewmaker F; Kerner MJ; Hayer-Hartl M; Klein G; Georgopoulos C; Landry SJ
Protein Sci; 2004 Aug; 13(8):2139-48. PubMed ID: 15238634
[TBL] [Abstract][Full Text] [Related]
18. The lid that shapes the pot: structure and function of the chaperonin GroES.
Saibil H
Structure; 1996 Jan; 4(1):1-4. PubMed ID: 8805512
[TBL] [Abstract][Full Text] [Related]
19. Chaperonin-mediated protein folding.
Thirumalai D; Lorimer GH
Annu Rev Biophys Biomol Struct; 2001; 30():245-69. PubMed ID: 11340060
[TBL] [Abstract][Full Text] [Related]
20. MgATP binding to the nucleotide-binding domains of the eukaryotic cytoplasmic chaperonin induces conformational changes in the putative substrate-binding domains.
Szpikowska BK; Swiderek KM; Sherman MA; Mas MT
Protein Sci; 1998 Jul; 7(7):1524-30. PubMed ID: 9684884
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
