These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
218 related articles for article (PubMed ID: 9037009)
1. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Goldberg MS; Zhang J; Sondek S; Matthews CR; Fox RO; Horwich AL Proc Natl Acad Sci U S A; 1997 Feb; 94(4):1080-5. PubMed ID: 9037009 [TBL] [Abstract][Full Text] [Related]
2. GroEL-mediated folding of structurally homologous dihydrofolate reductases. Clark AC; Frieden C J Mol Biol; 1997 May; 268(2):512-25. PubMed ID: 9159487 [TBL] [Abstract][Full Text] [Related]
3. Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL. Clark AC; Hugo E; Frieden C Biochemistry; 1996 May; 35(18):5893-901. PubMed ID: 8639551 [TBL] [Abstract][Full Text] [Related]
4. Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR. Nieba-Axmann SE; Ottiger M; Wüthrich K; Plückthun A J Mol Biol; 1997 Sep; 271(5):803-18. PubMed ID: 9299328 [TBL] [Abstract][Full Text] [Related]
5. Conditions of forming protein complexes with GroEL can influence the mechanism of chaperonin-assisted refolding. Gorovits BM; Horowitz PM J Biol Chem; 1997 Jan; 272(1):32-5. PubMed ID: 8995221 [TBL] [Abstract][Full Text] [Related]
6. Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity. Zahn R; Perrett S; Fersht AR J Mol Biol; 1996 Aug; 261(1):43-61. PubMed ID: 8760501 [TBL] [Abstract][Full Text] [Related]
7. The chaperonin GroEL binds to late-folding non-native conformations present in native Escherichia coli and murine dihydrofolate reductases. Clark AC; Frieden C J Mol Biol; 1999 Jan; 285(4):1777-88. PubMed ID: 9917411 [TBL] [Abstract][Full Text] [Related]
8. Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution. Horst R; Fenton WA; Englander SW; Wüthrich K; Horwich AL Proc Natl Acad Sci U S A; 2007 Dec; 104(52):20788-92. PubMed ID: 18093916 [TBL] [Abstract][Full Text] [Related]
9. Direct NMR observation of a substrate protein bound to the chaperonin GroEL. Horst R; Bertelsen EB; Fiaux J; Wider G; Horwich AL; Wüthrich K Proc Natl Acad Sci U S A; 2005 Sep; 102(36):12748-53. PubMed ID: 16116078 [TBL] [Abstract][Full Text] [Related]
10. Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling. Gross M; Robinson CV; Mayhew M; Hartl FU; Radford SE Protein Sci; 1996 Dec; 5(12):2506-13. PubMed ID: 8976559 [TBL] [Abstract][Full Text] [Related]
11. The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form. von Ahsen O; Tropschug M; Pfanner N; Rassow J EMBO J; 1997 Aug; 16(15):4568-78. PubMed ID: 9303301 [TBL] [Abstract][Full Text] [Related]
12. Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Mayhew M; da Silva AC; Martin J; Erdjument-Bromage H; Tempst P; Hartl FU Nature; 1996 Feb; 379(6564):420-6. PubMed ID: 8559246 [TBL] [Abstract][Full Text] [Related]
13. Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage. Corrales FJ; Fersht AR Proc Natl Acad Sci U S A; 1996 Apr; 93(9):4509-12. PubMed ID: 8633099 [TBL] [Abstract][Full Text] [Related]
14. A polypeptide bound by the chaperonin groEL is localized within a central cavity. Braig K; Simon M; Furuya F; Hainfeld JF; Horwich AL Proc Natl Acad Sci U S A; 1993 May; 90(9):3978-82. PubMed ID: 8097882 [TBL] [Abstract][Full Text] [Related]
15. Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Zahn R; Perrett S; Stenberg G; Fersht AR Science; 1996 Feb; 271(5249):642-5. PubMed ID: 8571125 [TBL] [Abstract][Full Text] [Related]
16. Kinetics and thermodynamics of the thermal inactivation and chaperone assisted folding of zebrafish dihydrofolate reductase. Thapliyal C; Jain N; Rashid N; Chaudhuri Chattopadhyay P Arch Biochem Biophys; 2018 Jan; 637():21-30. PubMed ID: 29138095 [TBL] [Abstract][Full Text] [Related]
17. 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]
18. Folding of malate dehydrogenase inside the GroEL-GroES cavity. Chen J; Walter S; Horwich AL; Smith DL Nat Struct Biol; 2001 Aug; 8(8):721-8. PubMed ID: 11473265 [TBL] [Abstract][Full Text] [Related]
19. GroEL-assisted dehydrogenase folding mediated by coenzyme is ATP-independent. Zhang S; Li J; Wang CC Biochem Biophys Res Commun; 2001 Jul; 285(2):277-82. PubMed ID: 11444838 [TBL] [Abstract][Full Text] [Related]
20. Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones. Park ES; Fenton WA; Horwich AL Proc Natl Acad Sci U S A; 2007 Feb; 104(7):2145-50. PubMed ID: 17283341 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]