119 related articles for article (PubMed ID: 9534169)
1. Molecular chaperones and their interactions investigated by analytical ultracentrifugation and other methodologies.
Schönfeld HJ; Behlke J
Methods Enzymol; 1998; 290():269-96. PubMed ID: 9534169
[No Abstract] [Full Text] [Related]
2. Capturing the misfolds: chaperone-peptide-binding motifs.
Joachimiak A
Nat Struct Biol; 1997 Jun; 4(6):430-4. PubMed ID: 9187647
[No Abstract] [Full Text] [Related]
3. Limits of protein folding inside GroE complexes.
Grallert H; Rutkat K; Buchner J
J Biol Chem; 2000 Jul; 275(27):20424-30. PubMed ID: 10779510
[TBL] [Abstract][Full Text] [Related]
4. [Reaction mechanism of mammalian molecular chaperones].
Itoh H
Seikagaku; 2005 Sep; 77(9):1137-51. PubMed ID: 16241001
[No Abstract] [Full Text] [Related]
5. Chaperones keep a high profile on the beach.
Freedman RB
Trends Biotechnol; 1995 Dec; 13(12):501-2. PubMed ID: 8595134
[No Abstract] [Full Text] [Related]
6. Immediate response of the DnaK molecular chaperone system to heat shock.
Siegenthaler RK; Grimshaw JP; Christen P
FEBS Lett; 2004 Mar; 562(1-3):105-10. PubMed ID: 15044009
[TBL] [Abstract][Full Text] [Related]
7. Substrate Interaction Networks of the Escherichia coli Chaperones: Trigger Factor, DnaK and GroEL.
Bhandari V; Houry WA
Adv Exp Med Biol; 2015; 883():271-94. PubMed ID: 26621473
[TBL] [Abstract][Full Text] [Related]
8. Molecular chaperones in biology and medicine at Obernai.
Bergeron JJ; Craig EA; Horwich AL; Langer T; Multhoff G; Smith DF; Hightower LE
Cell Stress Chaperones; 1997 Dec; 2(4):220-8. PubMed ID: 9495279
[TBL] [Abstract][Full Text] [Related]
9. Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration.
Diamant S; Goloubinoff P
Biochemistry; 1998 Jul; 37(27):9688-94. PubMed ID: 9657681
[TBL] [Abstract][Full Text] [Related]
10. Molecular chaperone function of mammalian Hsp70 and Hsp40--a review.
Ohtsuka K; Hata M
Int J Hyperthermia; 2000; 16(3):231-45. PubMed ID: 10830586
[TBL] [Abstract][Full Text] [Related]
11. Machinery of protein folding and unfolding.
Zhang X; Beuron F; Freemont PS
Curr Opin Struct Biol; 2002 Apr; 12(2):231-8. PubMed ID: 11959502
[TBL] [Abstract][Full Text] [Related]
12. Principles of chaperone-mediated protein folding.
Hartl FU
Philos Trans R Soc Lond B Biol Sci; 1995 Apr; 348(1323):107-12. PubMed ID: 7770479
[TBL] [Abstract][Full Text] [Related]
13. Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins.
Saibil H
Curr Opin Struct Biol; 2000 Apr; 10(2):251-8. PubMed ID: 10753820
[TBL] [Abstract][Full Text] [Related]
14. NMR disentangles a dynamic disaggregase machinery.
Saio T; Kalodimos CG
Nat Struct Mol Biol; 2013 Apr; 20(4):409-10. PubMed ID: 23552291
[No Abstract] [Full Text] [Related]
15. Folding while bound to chaperones.
Horowitz S; Koldewey P; Stull F; Bardwell JC
Curr Opin Struct Biol; 2018 Feb; 48():1-5. PubMed ID: 28734135
[TBL] [Abstract][Full Text] [Related]
16. The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis.
Mogk A; Homuth G; Scholz C; Kim L; Schmid FX; Schumann W
EMBO J; 1997 Aug; 16(15):4579-90. PubMed ID: 9303302
[TBL] [Abstract][Full Text] [Related]
17. All three J-domain proteins of the Escherichia coli DnaK chaperone machinery are DNA binding proteins.
Gur E; Katz C; Ron EZ
FEBS Lett; 2005 Mar; 579(9):1935-9. PubMed ID: 15792799
[TBL] [Abstract][Full Text] [Related]
18. Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response.
Groemping Y; Reinstein J
J Mol Biol; 2001 Nov; 314(1):167-78. PubMed ID: 11724541
[TBL] [Abstract][Full Text] [Related]
19. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.
Harrison CJ; Hayer-Hartl M; Di Liberto M; Hartl F; Kuriyan J
Science; 1997 Apr; 276(5311):431-5. PubMed ID: 9103205
[TBL] [Abstract][Full Text] [Related]
20. 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]
[Next] [New Search]
