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Journal Abstract Search

124 related items for PubMed ID: 11342048

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  • 2. Substitution of conserved methionines by leucines in chloroplast small heat shock protein results in loss of redox-response but retained chaperone-like activity.
    Gustavsson N, Kokke BP, Anzelius B, Boelens WC, Sundby C.
    Protein Sci; 2001 Sep; 10(9):1785-93. PubMed ID: 11514669
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  • 4. Conserved methionines in chloroplasts.
    Sundby C, Härndahl U, Gustavsson N, Ahrman E, Murphy DJ.
    Biochim Biophys Acta; 2005 Jan 17; 1703(2):191-202. PubMed ID: 15680227
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  • 7. Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity.
    Rutsdottir G, Härmark J, Weide Y, Hebert H, Rasmussen MI, Wernersson S, Respondek M, Akke M, Højrup P, Koeck PJB, Söderberg CAG, Emanuelsson C.
    J Biol Chem; 2017 May 12; 292(19):8103-8121. PubMed ID: 28325834
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  • 10. Tsp36, a tapeworm small heat-shock protein with a duplicated alpha-crystallin domain, forms dimers and tetramers with good chaperone-like activity.
    Kappé G, Aquilina JA, Wunderink L, Kamps B, Robinson CV, Garate T, Boelens WC, de Jong WW.
    Proteins; 2004 Oct 01; 57(1):109-17. PubMed ID: 15326597
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  • 11. Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21.
    Lambert W, Koeck PJ, Ahrman E, Purhonen P, Cheng K, Elmlund D, Hebert H, Emanuelsson C.
    Protein Sci; 2011 Feb 01; 20(2):291-301. PubMed ID: 21280121
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  • 12. Chaperone-client interactions between Hsp21 and client proteins monitored in solution by small angle X-ray scattering and captured by crosslinking mass spectrometry.
    Rutsdottir G, I Rasmussen M, Hojrup P, Bernfur K, Emanuelsson C, Söderberg CAG.
    Proteins; 2018 Jan 01; 86(1):110-123. PubMed ID: 29082555
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  • 13. The chloroplast small heat shock protein undergoes oxidation-dependent conformational changes and may protect plants from oxidative stress.
    Härndahl U, Hall RB, Osteryoung KW, Vierling E, Bornman JF, Sundby C.
    Cell Stress Chaperones; 1999 Jun 01; 4(2):129-38. PubMed ID: 10547062
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  • 14. Small heat shock proteins prevent aggregation of citrate synthase and bind to the N-terminal region which is absent in thermostable forms of citrate synthase.
    Ahrman E, Gustavsson N, Hultschig C, Boelens WC, Emanuelsson CS.
    Extremophiles; 2007 Sep 01; 11(5):659-66. PubMed ID: 17486291
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  • 16. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state.
    Lee GJ, Roseman AM, Saibil HR, Vierling E.
    EMBO J; 1997 Feb 03; 16(3):659-71. PubMed ID: 9034347
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  • 17. Chaperone activity of cytosolic small heat shock proteins from wheat.
    Basha E, Lee GJ, Demeler B, Vierling E.
    Eur J Biochem; 2004 Apr 03; 271(8):1426-36. PubMed ID: 15066169
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  • 18. A critical motif for oligomerization and chaperone activity of bacterial alpha-heat shock proteins.
    Studer S, Obrist M, Lentze N, Narberhaus F.
    Eur J Biochem; 2002 Jul 03; 269(14):3578-86. PubMed ID: 12135498
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  • 19. Mutation or deletion of the C-terminal tail affects the function and structure of Xenopus laevis small heat shock protein, hsp30.
    Fernando P, Abdulle R, Mohindra A, Guillemette JG, Heikkila JJ.
    Comp Biochem Physiol B Biochem Mol Biol; 2002 Sep 03; 133(1):95-103. PubMed ID: 12223216
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  • 20. The chloroplast small heat-shock protein oligomer is not phosphorylated and does not dissociate during heat stress in vivo.
    Suzuki TC, Krawitz DC, Vierling E.
    Plant Physiol; 1998 Mar 03; 116(3):1151-61. PubMed ID: 9501148
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