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210 related items for PubMed ID: 16706200

  • 1. [Room temperature phosphorescence of amorphous aggregates and amyloid fibrils resulting from protein misfolding].
    Mazhul' VM, Zaĭtseva EM, Shavlovskiĭ MM, Povarova OI, Kuznetsova IM, Turoverov KK.
    Tsitologiia; 2005; 47(11):978-87. PubMed ID: 16706200
    [Abstract] [Full Text] [Related]

  • 2. Monitoring of actin unfolding by room temperature tryptophan phosphorescence.
    Mazhul' VM, Zaitseva EM, Shavlovsky MM, Stepanenko OV, Kuznetsova IM, Turoverov KK.
    Biochemistry; 2003 Nov 25; 42(46):13551-7. PubMed ID: 14622002
    [Abstract] [Full Text] [Related]

  • 3. [Tryptophan phosphorescence of nascent and inactivated actin at the room temperature].
    Mazhul' VM, Zaĭtseva EM, Shavlovskiĭ MM, Kuznetsova IM, Turoverov KK.
    Biofizika; 2001 Nov 25; 46(6):988-96. PubMed ID: 11771297
    [Abstract] [Full Text] [Related]

  • 4. [Kinetics of inactivation of lectin: analysis of a method of tryptophan phosphorescence at room temperature].
    Mazhul' VM, Zaĭtseva EM, Shavlovskiĭ MM, Kuznetsova IM, Turoverov KK.
    Biofizika; 2003 Nov 25; 48(5):837-43. PubMed ID: 14582408
    [Abstract] [Full Text] [Related]

  • 5. The structure and dynamics of partially folded actin.
    Turoverov KK, Biktashev AG, Khaitlina SY, Kuznetsova IM.
    Biochemistry; 1999 May 11; 38(19):6261-9. PubMed ID: 10320355
    [Abstract] [Full Text] [Related]

  • 6. [Physical-chemical properties of actin in different structural states. New ideas about its folding-unfolding pathways].
    Povarova OI, Kuznetsova IM, Turoverov KK.
    Tsitologiia; 2005 May 11; 47(11):953-77. PubMed ID: 16706199
    [Abstract] [Full Text] [Related]

  • 7. Time-resolved protein phosphorescence in the stopped-flow: denaturation of horse liver alcohol dehydrogenase by urea and guanidine hydrochloride.
    Gonnelli M, Strambini GB.
    Biochemistry; 1997 Dec 23; 36(51):16212-20. PubMed ID: 9405055
    [Abstract] [Full Text] [Related]

  • 8. Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.
    Patra AK, Udgaonkar JB.
    Biochemistry; 2007 Oct 23; 46(42):11727-43. PubMed ID: 17902706
    [Abstract] [Full Text] [Related]

  • 9. Different disturbances--one pathway of protein unfolding. Actin folding-unfolding and misfolding.
    Povarova OI, Kuznetsova IM, Turoverov KK.
    Cell Biol Int; 2007 Apr 23; 31(4):405-12. PubMed ID: 17336100
    [Abstract] [Full Text] [Related]

  • 10. [Features of the structural organization of inactivated actin--an intermediate form of the protein during the folding-unfolding process].
    Kuznetsova IM, Khaĭtlina SIu, Turoverov KK.
    Bioorg Khim; 1998 Dec 23; 24(12):883-92. PubMed ID: 10079945
    [Abstract] [Full Text] [Related]

  • 11. Kinetics of actin unfolding induced by guanidine hydrochloride.
    Turoverov KK, Verkhusha VV, Shavlovsky MM, Biktashev AG, Povarova OI, Kuznetsova IM.
    Biochemistry; 2002 Jan 22; 41(3):1014-9. PubMed ID: 11790125
    [Abstract] [Full Text] [Related]

  • 12. Unfolding and refolding pathways of a major kinetic trap in the oxidative folding of alpha-lactalbumin.
    Salamanca S, Chang JY.
    Biochemistry; 2005 Jan 18; 44(2):744-50. PubMed ID: 15641801
    [Abstract] [Full Text] [Related]

  • 13. Tryptophan to phenylalanine substitutions allow differentiation of short- and long-range conformational changes during denaturation of goat alpha-lactalbumin.
    Vanhooren A, Chedad A, Farkas V, Majer Z, Joniau M, Van Dael H, Hanssens I.
    Proteins; 2005 Jul 01; 60(1):118-30. PubMed ID: 15861407
    [Abstract] [Full Text] [Related]

  • 14. Tetrameric N(5)-(L-1-carboxyethyl)-L-ornithine synthase: guanidine. HCl-induced unfolding and a low temperature requirement for refolding.
    Ruvinov SB, Thompson J, Sackett DL, Ginsburg A.
    Arch Biochem Biophys; 1999 Nov 01; 371(1):115-23. PubMed ID: 10525296
    [Abstract] [Full Text] [Related]

  • 15. Revealing a concealed intermediate that forms after the rate-limiting step of refolding of the SH3 domain of PI3 kinase.
    Wani AH, Udgaonkar JB.
    J Mol Biol; 2009 Mar 27; 387(2):348-62. PubMed ID: 19356591
    [Abstract] [Full Text] [Related]

  • 16. Two-state folding of horse ferrocytochrome c: analyses of linear free energy relationship, chevron curvature, and stopped-flow burst relaxation kinetics.
    Kumar R, Bhuyan AK.
    Biochemistry; 2005 Mar 01; 44(8):3024-33. PubMed ID: 15723546
    [Abstract] [Full Text] [Related]

  • 17. Kinetics of folding and unfolding of goat alpha-lactalbumin.
    Chedad A, Van Dael H.
    Proteins; 2004 Nov 01; 57(2):345-56. PubMed ID: 15340922
    [Abstract] [Full Text] [Related]

  • 18. The place of inactivated actin and its kinetic predecessor in actin folding-unfolding.
    Kuznetsova IM, Stepanenko OV, Stepanenko OV, Povarova OI, Biktashev AG, Verkhusha VV, Shavlovsky MM, Turoverov KK.
    Biochemistry; 2002 Nov 05; 41(44):13127-32. PubMed ID: 12403613
    [Abstract] [Full Text] [Related]

  • 19. Oleic acid inhibits amyloid formation of the intermediate of alpha-lactalbumin at moderately acidic pH.
    Yang F, Zhang M, Zhou BR, Chen J, Liang Y.
    J Mol Biol; 2006 Sep 29; 362(4):821-34. PubMed ID: 16935298
    [Abstract] [Full Text] [Related]

  • 20. Effect of self-association on the structural organization of partially folded proteins: inactivated actin.
    Kuznetsova IM, Biktashev AG, Khaitlina SY, Vassilenko KS, Turoverov KK, Uversky VN.
    Biophys J; 1999 Nov 29; 77(5):2788-800. PubMed ID: 10545377
    [Abstract] [Full Text] [Related]

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