194 related articles for article (PubMed ID: 10976105)
1. Redox switch of hsp33 has a novel zinc-binding motif.
Jakob U; Eser M; Bardwell JC
J Biol Chem; 2000 Dec; 275(49):38302-10. PubMed ID: 10976105
[TBL] [Abstract][Full Text] [Related]
2. The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold.
Won HS; Low LY; Guzman RD; Martinez-Yamout M; Jakob U; Dyson HJ
J Mol Biol; 2004 Aug; 341(4):893-9. PubMed ID: 15328602
[TBL] [Abstract][Full Text] [Related]
3. Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity.
Kim SJ; Jeong DG; Chi SW; Lee JS; Ryu SE
Nat Struct Biol; 2001 May; 8(5):459-66. PubMed ID: 11323724
[TBL] [Abstract][Full Text] [Related]
4. Activation of the redox-regulated molecular chaperone Hsp33--a two-step mechanism.
Graumann J; Lilie H; Tang X; Tucker KA; Hoffmann JH; Vijayalakshmi J; Saper M; Bardwell JC; Jakob U
Structure; 2001 May; 9(5):377-87. PubMed ID: 11377198
[TBL] [Abstract][Full Text] [Related]
5. Activation of the redox-regulated chaperone Hsp33 by domain unfolding.
Graf PC; Martinez-Yamout M; VanHaerents S; Lilie H; Dyson HJ; Jakob U
J Biol Chem; 2004 May; 279(19):20529-38. PubMed ID: 15023991
[TBL] [Abstract][Full Text] [Related]
6. HSP33 in eukaryotes - an evolutionary tale of a chaperone adapted to photosynthetic organisms.
Segal N; Shapira M
Plant J; 2015 Jun; 82(5):850-60. PubMed ID: 25892083
[TBL] [Abstract][Full Text] [Related]
7. Redox-regulated molecular chaperones.
Graf PC; Jakob U
Cell Mol Life Sci; 2002 Oct; 59(10):1624-31. PubMed ID: 12475172
[TBL] [Abstract][Full Text] [Related]
8. Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone.
Barbirz S; Jakob U; Glocker MO
J Biol Chem; 2000 Jun; 275(25):18759-66. PubMed ID: 10764757
[TBL] [Abstract][Full Text] [Related]
9. The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism.
Janda I; Devedjiev Y; Derewenda U; Dauter Z; Bielnicki J; Cooper DR; Graf PC; Joachimiak A; Jakob U; Derewenda ZS
Structure; 2004 Oct; 12(10):1901-7. PubMed ID: 15458638
[TBL] [Abstract][Full Text] [Related]
10. Zinc center as redox switch--new function for an old motif.
Ilbert M; Graf PC; Jakob U
Antioxid Redox Signal; 2006; 8(5-6):835-46. PubMed ID: 16771674
[TBL] [Abstract][Full Text] [Related]
11. Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity.
Chi SW; Jeong DG; Woo JR; Lee HS; Park BC; Kim BY; Erikson RL; Ryu SE; Kim SJ
FEBS Lett; 2011 Feb; 585(4):664-70. PubMed ID: 21266175
[TBL] [Abstract][Full Text] [Related]
12. The 2.2 A crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity.
Vijayalakshmi J; Mukhergee MK; Graumann J; Jakob U; Saper MA
Structure; 2001 May; 9(5):367-75. PubMed ID: 11377197
[TBL] [Abstract][Full Text] [Related]
13. Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone.
Cremers CM; Reichmann D; Hausmann J; Ilbert M; Jakob U
J Biol Chem; 2010 Apr; 285(15):11243-51. PubMed ID: 20139072
[TBL] [Abstract][Full Text] [Related]
14. Chaperone activity with a redox switch.
Jakob U; Muse W; Eser M; Bardwell JC
Cell; 1999 Feb; 96(3):341-52. PubMed ID: 10025400
[TBL] [Abstract][Full Text] [Related]
15. Contributions of cysteine residues in Zn2 to zinc fingers and thiol-disulfide oxidoreductase activities of chaperone DnaJ.
Shi YY; Tang W; Hao SF; Wang CC
Biochemistry; 2005 Feb; 44(5):1683-9. PubMed ID: 15683252
[TBL] [Abstract][Full Text] [Related]
16. Unique Unfoldase/Aggregase Activity of a Molecular Chaperone Hsp33 in its Holding-Inactive State.
Jo KS; Kim JH; Ryu KS; Kang JS; Wang CY; Lee YS; Seo MD; Lee YH; Won HS
J Mol Biol; 2019 Mar; 431(7):1468-1480. PubMed ID: 30822413
[TBL] [Abstract][Full Text] [Related]
17. Identification of a redox-regulated chaperone network.
Hoffmann JH; Linke K; Graf PC; Lilie H; Jakob U
EMBO J; 2004 Jan; 23(1):160-8. PubMed ID: 14685279
[TBL] [Abstract][Full Text] [Related]
18. Functional characterization of Hsp33 protein from Bacillus psychrosaccharolyticus; additional function of HSP33 on resistance to solvent stress.
Kang HJ; Heo DH; Choi SW; Kim KN; Shim J; Kim CW; Sung HC; Yun CW
Biochem Biophys Res Commun; 2007 Jul; 358(3):743-50. PubMed ID: 17512907
[TBL] [Abstract][Full Text] [Related]
19. The cold atmospheric pressure plasma-generated species superoxide, singlet oxygen and atomic oxygen activate the molecular chaperone Hsp33.
Dirks T; Krewing M; Vogel K; Bandow JE
J R Soc Interface; 2023 Oct; 20(207):20230300. PubMed ID: 37876273
[TBL] [Abstract][Full Text] [Related]
20. Redox-regulated chaperone function and conformational changes of Escherichia coli Hsp33.
Raman B; Siva Kumar LV; Ramakrishna T; Mohan Rao C
FEBS Lett; 2001 Jan; 489(1):19-24. PubMed ID: 11231006
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
