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298 related items for PubMed ID: 21689790

  • 1. Aggregation and structural changes of α(S1)-, β- and κ-caseins induced by homocysteinylation.
    Stroylova YY, Zimny J, Yousefi R, Chobert JM, Jakubowski H, Muronetz VI, Haertlé T.
    Biochim Biophys Acta; 2011 Oct; 1814(10):1234-45. PubMed ID: 21689790
    [Abstract] [Full Text] [Related]

  • 2. Kinetics of fibril formation of bovine kappa-casein indicate a conformational rearrangement as a critical step in the process.
    Leonil J, Henry G, Jouanneau D, Delage MM, Forge V, Putaux JL.
    J Mol Biol; 2008 Sep 19; 381(5):1267-80. PubMed ID: 18616951
    [Abstract] [Full Text] [Related]

  • 3. N-homocysteinylation of ovine prion protein induces amyloid-like transformation.
    Stroylova YY, Chobert JM, Muronetz VI, Jakubowski H, Haertlé T.
    Arch Biochem Biophys; 2012 Oct 01; 526(1):29-37. PubMed ID: 22782079
    [Abstract] [Full Text] [Related]

  • 4. The dissociated form of kappa-casein is the precursor to its amyloid fibril formation.
    Ecroyd H, Thorn DC, Liu Y, Carver JA.
    Biochem J; 2010 Jul 15; 429(2):251-60. PubMed ID: 20441567
    [Abstract] [Full Text] [Related]

  • 5. Protein N-homocysteinylation induces the formation of toxic amyloid-like protofibrils.
    Paoli P, Sbrana F, Tiribilli B, Caselli A, Pantera B, Cirri P, De Donatis A, Formigli L, Nosi D, Manao G, Camici G, Ramponi G.
    J Mol Biol; 2010 Jul 23; 400(4):889-907. PubMed ID: 20510245
    [Abstract] [Full Text] [Related]

  • 6. Effect of homocysteinylation on structure, chaperone activity and fibrillation propensity of lens alpha-crystallin.
    Yousefi R, Khazaei S, Moosavi-Movahedi AA.
    Protein Pept Lett; 2013 Aug 23; 20(8):932-41. PubMed ID: 23458667
    [Abstract] [Full Text] [Related]

  • 7. Aggregation behavior of bovine κ- and β-casein studied with small angle neutron scattering, light scattering, and cryogenic transmission electron microscopy.
    Ossowski S, Jackson A, Obiols-Rabasa M, Holt C, Lenton S, Porcar L, Paulsson M, Nylander T.
    Langmuir; 2012 Sep 25; 28(38):13577-89. PubMed ID: 22924693
    [Abstract] [Full Text] [Related]

  • 8. Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein.
    Thorn DC, Meehan S, Sunde M, Rekas A, Gras SL, MacPhee CE, Dobson CM, Wilson MR, Carver JA.
    Biochemistry; 2005 Dec 27; 44(51):17027-36. PubMed ID: 16363816
    [Abstract] [Full Text] [Related]

  • 9. Environmental influences on bovine kappa-casein: reduction and conversion to fibrillar (amyloid) structures.
    Farrell HM, Cooke PH, Wickham ED, Piotrowski EG, Hoagland PD.
    J Protein Chem; 2003 Apr 27; 22(3):259-73. PubMed ID: 12962326
    [Abstract] [Full Text] [Related]

  • 10. Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein.
    Thorn DC, Ecroyd H, Sunde M, Poon S, Carver JA.
    Biochemistry; 2008 Mar 25; 47(12):3926-36. PubMed ID: 18302322
    [Abstract] [Full Text] [Related]

  • 11. Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels.
    Jakubowski H.
    FASEB J; 1999 Dec 25; 13(15):2277-83. PubMed ID: 10593875
    [Abstract] [Full Text] [Related]

  • 12. Aggregation and fibrillation of eye lens crystallins by homocysteinylation; implication in the eye pathological disorders.
    Khazaei S, Yousefi R, Alavian-Mehr MM.
    Protein J; 2012 Dec 25; 31(8):717-27. PubMed ID: 23070797
    [Abstract] [Full Text] [Related]

  • 13. Modification of erythropoietin structure by N-homocysteinylation affects its antiapoptotic and proliferative functions.
    Schiappacasse A, Maltaneri RE, Chamorro ME, Nesse AB, Wetzler DE, Vittori DC.
    FEBS J; 2018 Oct 25; 285(20):3801-3814. PubMed ID: 30103295
    [Abstract] [Full Text] [Related]

  • 14. Existence of molten globule state in homocysteine-induced protein covalent modifications.
    Kumar T, Sharma GS, Singh LR.
    PLoS One; 2014 Oct 25; 9(11):e113566. PubMed ID: 25405350
    [Abstract] [Full Text] [Related]

  • 15. Interaction with Al and Zn induces structure formation and aggregation in natively unfolded caseins.
    Chakraborty A, Basak S.
    J Photochem Photobiol B; 2008 Oct 16; 93(1):36-43. PubMed ID: 18700180
    [Abstract] [Full Text] [Related]

  • 16. Effect of the A and B variants of both alpha s1- and kappa-casein on bovine casein micelle solvation and kappa-casein content.
    Anema SG, Creamer LK.
    J Dairy Res; 1993 Nov 16; 60(4):505-16. PubMed ID: 8294607
    [Abstract] [Full Text] [Related]

  • 17. Dephosphorylation of alpha(s)- and beta-caseins and its effect on chaperone activity: a structural and functional investigation.
    Koudelka T, Hoffmann P, Carver JA.
    J Agric Food Chem; 2009 Jul 08; 57(13):5956-64. PubMed ID: 19527030
    [Abstract] [Full Text] [Related]

  • 18. pH-induced structural transitions of caseins.
    Chakraborty A, Basak S.
    J Photochem Photobiol B; 2007 Jun 26; 87(3):191-9. PubMed ID: 17537643
    [Abstract] [Full Text] [Related]

  • 19. The Effect of Milk Constituents and Crowding Agents on Amyloid Fibril Formation by κ-Casein.
    Liu J, Dehle FC, Liu Y, Bahraminejad E, Ecroyd H, Thorn DC, Carver JA.
    J Agric Food Chem; 2016 Feb 17; 64(6):1335-43. PubMed ID: 26807595
    [Abstract] [Full Text] [Related]

  • 20. Amyloid-like fibrils formed from intrinsically disordered caseins: physicochemical and nanomechanical properties.
    Pan K, Zhong Q.
    Soft Matter; 2015 Aug 07; 11(29):5898-904. PubMed ID: 26112282
    [Abstract] [Full Text] [Related]

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