567 related articles for article (PubMed ID: 10221986)
41. Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy.
Mayer MP; Laufen T; Paal K; McCarty JS; Bukau B
J Mol Biol; 1999 Jun; 289(4):1131-44. PubMed ID: 10369787
[TBL] [Abstract][Full Text] [Related]
42. A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.
Szabo A; Korszun R; Hartl FU; Flanagan J
EMBO J; 1996 Jan; 15(2):408-17. PubMed ID: 8617216
[TBL] [Abstract][Full Text] [Related]
43. Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK.
Mattoo RU; Farina Henriquez Cuendet A; Subanna S; Finka A; Priya S; Sharma SK; Goloubinoff P
Front Mol Biosci; 2014; 1():7. PubMed ID: 25988148
[TBL] [Abstract][Full Text] [Related]
44. Molecular chaperones and mitochondrial protein folding.
Martin J
J Bioenerg Biomembr; 1997 Feb; 29(1):35-43. PubMed ID: 9067800
[TBL] [Abstract][Full Text] [Related]
45. The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70.
Farinha CM; Nogueira P; Mendes F; Penque D; Amaral MD
Biochem J; 2002 Sep; 366(Pt 3):797-806. PubMed ID: 12069690
[TBL] [Abstract][Full Text] [Related]
46. Chaperone-assisted protein folding.
Martin J; Hartl FU
Curr Opin Struct Biol; 1997 Feb; 7(1):41-52. PubMed ID: 9032064
[TBL] [Abstract][Full Text] [Related]
47. Efficient production of native actin upon translation in a bacterial lysate supplemented with the eukaryotic chaperonin TRiC.
Stemp MJ; Guha S; Hartl FU; Barral JM
Biol Chem; 2005 Aug; 386(8):753-7. PubMed ID: 16201870
[TBL] [Abstract][Full Text] [Related]
48. Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones.
Ben-Zvi A; De Los Rios P; Dietler G; Goloubinoff P
J Biol Chem; 2004 Sep; 279(36):37298-303. PubMed ID: 15201275
[TBL] [Abstract][Full Text] [Related]
49. Disulfide bonds convert small heat shock protein Hsp16.3 from a chaperone to a non-chaperone: implications for the evolution of cysteine in molecular chaperones.
Fu X; Li W; Mao Q; Chang Z
Biochem Biophys Res Commun; 2003 Aug; 308(3):627-35. PubMed ID: 12914797
[TBL] [Abstract][Full Text] [Related]
50. The neurodegenerative-disease-related protein sacsin is a molecular chaperone.
Anderson JF; Siller E; Barral JM
J Mol Biol; 2011 Aug; 411(4):870-80. PubMed ID: 21726565
[TBL] [Abstract][Full Text] [Related]
51. Molecular chaperones in protein folding: the art of avoiding sticky situations.
Hartl FU; Hlodan R; Langer T
Trends Biochem Sci; 1994 Jan; 19(1):20-5. PubMed ID: 7908149
[TBL] [Abstract][Full Text] [Related]
52. Hydrogen deuterium exchange mass spectrometry applied to chaperones and chaperone-assisted protein folding.
Georgescauld F; Wales TE; Engen JR
Expert Rev Proteomics; 2019 Jul; 16(7):613-625. PubMed ID: 31215268
[No Abstract] [Full Text] [Related]
53. Disaggregating chaperones: an unfolding story.
Sharma SK; Christen P; Goloubinoff P
Curr Protein Pept Sci; 2009 Oct; 10(5):432-46. PubMed ID: 19538153
[TBL] [Abstract][Full Text] [Related]
54. Chaperones in control of protein disaggregation.
Liberek K; Lewandowska A; Zietkiewicz S
EMBO J; 2008 Jan; 27(2):328-35. PubMed ID: 18216875
[TBL] [Abstract][Full Text] [Related]
55. Protein folding assisted by chaperones.
Borges JC; Ramos CH
Protein Pept Lett; 2005 Apr; 12(3):257-61. PubMed ID: 15777275
[TBL] [Abstract][Full Text] [Related]
56. A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu.
To P; Xia Y; Lee SO; Devlin T; Fleming KG; Fried SD
Proc Natl Acad Sci U S A; 2022 Nov; 119(48):e2210536119. PubMed ID: 36417429
[TBL] [Abstract][Full Text] [Related]
57. Mechanism of chaperone coordination during cotranslational protein folding in bacteria.
Roeselová A; Maslen SL; Shivakumaraswamy S; Pellowe GA; Howell S; Joshi D; Redmond J; Kjær S; Skehel JM; Balchin D
Mol Cell; 2024 Jun; ():. PubMed ID: 38908370
[TBL] [Abstract][Full Text] [Related]
58. Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.
Mattoo RU; Goloubinoff P
Cell Mol Life Sci; 2014 Sep; 71(17):3311-25. PubMed ID: 24760129
[TBL] [Abstract][Full Text] [Related]
59. Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones.
Finka A; Sharma SK; Goloubinoff P
Front Mol Biosci; 2015; 2():29. PubMed ID: 26097841
[TBL] [Abstract][Full Text] [Related]
60. Molecular chaperones, folding catalysts, and the recovery of active recombinant proteins from E. coli. To fold or to refold.
Thomas JG; Ayling A; Baneyx F
Appl Biochem Biotechnol; 1997 Jun; 66(3):197-238. PubMed ID: 9276922
[TBL] [Abstract][Full Text] [Related]
[Previous] [Next] [New Search]