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PUBMED FOR HANDHELDS

Journal Abstract Search


182 related items for PubMed ID: 17567739

  • 21. Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant.
    Ahmad MF, Raman B, Ramakrishna T, Rao ChM.
    J Mol Biol; 2008 Jan 25; 375(4):1040-51. PubMed ID: 18061612
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  • 22. Crystal structure and assembly of a eukaryotic small heat shock protein.
    van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E.
    Nat Struct Biol; 2001 Dec 25; 8(12):1025-30. PubMed ID: 11702068
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  • 23. Structural studies on the oligomeric transition of a small heat shock protein, StHsp14.0.
    Hanazono Y, Takeda K, Yohda M, Miki K.
    J Mol Biol; 2012 Sep 07; 422(1):100-8. PubMed ID: 22613762
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  • 24. Insights into the evolution of allosteric properties. The NADH binding site of hexameric type II citrate synthases.
    Maurus R, Nguyen NT, Stokell DJ, Ayed A, Hultin PG, Duckworth HW, Brayer GD.
    Biochemistry; 2003 May 20; 42(19):5555-65. PubMed ID: 12741811
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  • 25. Chaperone action of a versatile small heat shock protein from Methanococcoides burtonii, a cold adapted archaeon.
    Laksanalamai P, Narayan S, Luo H, Robb FT.
    Proteins; 2009 May 01; 75(2):275-81. PubMed ID: 18951410
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  • 26. Crystal structures of Xanthomonas small heat shock protein provide a structural basis for an active molecular chaperone oligomer.
    Hilario E, Martin FJ, Bertolini MC, Fan L.
    J Mol Biol; 2011 Apr 22; 408(1):74-86. PubMed ID: 21315085
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  • 27. Probing alpha-crystallin structure using chemical cross-linkers and mass spectrometry.
    Peterson JJ, Young MM, Takemoto LJ.
    Mol Vis; 2004 Nov 16; 10():857-66. PubMed ID: 15570221
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  • 31. Structural aspects and chaperone activity of human HspB3: role of the "C-terminal extension".
    Asthana A, Raman B, Ramakrishna T, Rao ChM.
    Cell Biochem Biophys; 2012 Sep 16; 64(1):61-72. PubMed ID: 22610661
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  • 32. 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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  • 34. An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones.
    Basha E, Jones C, Blackwell AE, Cheng G, Waters ER, Samsel KA, Siddique M, Pett V, Wysocki V, Vierling E.
    J Mol Biol; 2013 May 27; 425(10):1683-96. PubMed ID: 23416558
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  • 36. Molecular chaperone activity of tomato (Lycopersicon esculentum) endoplasmic reticulum-located small heat shock protein.
    Mamedov TG, Shono M.
    J Plant Res; 2008 Mar 27; 121(2):235-43. PubMed ID: 18288562
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  • 37. Probing the dimeric structure of porcine aminoacylase 1 by mass spectrometric and modeling procedures.
    D'Ambrosio C, Talamo F, Vitale RM, Amodeo P, Tell G, Ferrara L, Scaloni A.
    Biochemistry; 2003 Apr 22; 42(15):4430-43. PubMed ID: 12693939
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  • 38. Hsp26: a temperature-regulated chaperone.
    Haslbeck M, Walke S, Stromer T, Ehrnsperger M, White HE, Chen S, Saibil HR, Buchner J.
    EMBO J; 1999 Dec 01; 18(23):6744-51. PubMed ID: 10581247
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