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PUBMED FOR HANDHELDS

Journal Abstract Search

96 related items for PubMed ID: 10064142

  • 1. Homo-dimeric spherulin 3a: a single-domain member of the beta gamma-crystallin superfamily.
    Kretschmar M, Mayr EM, Jaenicke R.
    Biol Chem; 1999 Jan; 380(1):89-94. PubMed ID: 10064142
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  • 3. Ca2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype gamma-crystallin fold in aqueous solution.
    Rosinke B, Renner C, Mayr EM, Jaenicke R, Holak TA.
    J Mol Biol; 1997 Aug 29; 271(4):645-55. PubMed ID: 9281431
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  • 5. Crystal structure of the calcium-loaded spherulin 3a dimer sheds light on the evolution of the eye lens betagamma-crystallin domain fold.
    Clout NJ, Kretschmar M, Jaenicke R, Slingsby C.
    Structure; 2001 Feb 07; 9(2):115-24. PubMed ID: 11250196
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  • 9. The domains in gammaB-crystallin: identical fold-different stabilities.
    Mayr EM, Jaenicke R, Glockshuber R.
    J Mol Biol; 1997 Jun 06; 269(2):260-9. PubMed ID: 9191069
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  • 10. Association of partially folded lens betaB2-crystallins with the alpha-crystallin molecular chaperone.
    Evans P, Slingsby C, Wallace BA.
    Biochem J; 2008 Feb 01; 409(3):691-9. PubMed ID: 17937660
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  • 11. Creation of a new eye lens crystallin (Gambeta) through structure-guided mutagenic grafting of the surface of betaB2 crystallin onto the hydrophobic core of gammaB crystallin.
    Kapoor D, Singh B, Subramanian K, Guptasarma P.
    FEBS J; 2009 Jun 01; 276(12):3341-53. PubMed ID: 19438717
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  • 14. Caulollins from Caulobacter crescentus, a pair of partially unstructured proteins of betagamma-crystallin superfamily, gain structure upon binding calcium.
    Jobby MK, Sharma Y.
    Biochemistry; 2007 Oct 30; 46(43):12298-307. PubMed ID: 17915944
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  • 15. Calcium-binding to lens betaB2- and betaA3-crystallins suggests that all beta-crystallins are calcium-binding proteins.
    Jobby MK, Sharma Y.
    FEBS J; 2007 Aug 30; 274(16):4135-47. PubMed ID: 17651443
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  • 17. Eye lens betaB2-crystallin: circular permutation does not influence the oligomerization state but enhances the conformational stability.
    Wieligmann K, Norledge B, Jaenicke R, Mayr EM.
    J Mol Biol; 1998 Jul 24; 280(4):721-9. PubMed ID: 9677299
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  • 19. Folding pattern of the alpha-crystallin domain in alphaA-crystallin determined by site-directed spin labeling.
    Koteiche HA, Mchaourab HS.
    J Mol Biol; 1999 Nov 26; 294(2):561-77. PubMed ID: 10610780
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