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PUBMED FOR HANDHELDS

Journal Abstract Search


221 related items for PubMed ID: 15328602

  • 21.
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    [No Abstract] [Full Text] [Related]

  • 22. NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
    Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wüthrich K.
    J Mol Biol; 1996 Jul 12; 260(2):236-50. PubMed ID: 8764403
    [Abstract] [Full Text] [Related]

  • 23. Identification of a redox-regulated chaperone network.
    Hoffmann JH, Linke K, Graf PC, Lilie H, Jakob U.
    EMBO J; 2004 Jan 14; 23(1):160-8. PubMed ID: 14685279
    [Abstract] [Full Text] [Related]

  • 24. Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli.
    Cupp-Vickery JR, Vickery LE.
    J Mol Biol; 2000 Dec 15; 304(5):835-45. PubMed ID: 11124030
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  • 25. 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; 15(2):408-17. PubMed ID: 8617216
    [Abstract] [Full Text] [Related]

  • 26. Order out of disorder: working cycle of an intrinsically unfolded chaperone.
    Reichmann D, Xu Y, Cremers CM, Ilbert M, Mittelman R, Fitzgerald MC, Jakob U.
    Cell; 2012 Mar 02; 148(5):947-57. PubMed ID: 22385960
    [Abstract] [Full Text] [Related]

  • 27. NMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigens.
    Berjanskii MV, Riley MI, Xie A, Semenchenko V, Folk WR, Van Doren SR.
    J Biol Chem; 2000 Nov 17; 275(46):36094-103. PubMed ID: 10950962
    [Abstract] [Full Text] [Related]

  • 28.
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  • 29. 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 17; 20(207):20230300. PubMed ID: 37876273
    [Abstract] [Full Text] [Related]

  • 30. Protein unfolding as a switch from self-recognition to high-affinity client binding.
    Groitl B, Horowitz S, Makepeace KAT, Petrotchenko EV, Borchers CH, Reichmann D, Bardwell JCA, Jakob U.
    Nat Commun; 2016 Jan 20; 7():10357. PubMed ID: 26787517
    [Abstract] [Full Text] [Related]

  • 31. Oxidative stress: Protein folding with a novel redox switch.
    Ruddock LW, Klappa P.
    Curr Biol; 1999 Jun 03; 9(11):R400-2. PubMed ID: 10359689
    [Abstract] [Full Text] [Related]

  • 32. A Role of Metastable Regions and Their Connectivity in the Inactivation of a Redox-Regulated Chaperone and Its Inter-Chaperone Crosstalk.
    Rimon O, Suss O, Goldenberg M, Fassler R, Yogev O, Amartely H, Propper G, Friedler A, Reichmann D.
    Antioxid Redox Signal; 2017 Nov 20; 27(15):1252-1267. PubMed ID: 28394178
    [Abstract] [Full Text] [Related]

  • 33. Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry.
    Fassler R, Edinger N, Rimon O, Reichmann D.
    J Vis Exp; 2018 Jun 07; (136):. PubMed ID: 29939186
    [Abstract] [Full Text] [Related]

  • 34. Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33.
    Winter J, Linke K, Jatzek A, Jakob U.
    Mol Cell; 2005 Feb 04; 17(3):381-92. PubMed ID: 15694339
    [Abstract] [Full Text] [Related]

  • 35.
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  • 36. Wrapping the alpha-crystallin domain fold in a chaperone assembly.
    Stamler R, Kappé G, Boelens W, Slingsby C.
    J Mol Biol; 2005 Oct 14; 353(1):68-79. PubMed ID: 16165157
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  • 37.
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  • 40. Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin.
    Gomis-Rüth FX, Stöcker W, Huber R, Zwilling R, Bode W.
    J Mol Biol; 1993 Feb 20; 229(4):945-68. PubMed ID: 8445658
    [Abstract] [Full Text] [Related]


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