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Journal Abstract Search

406 related items for PubMed ID: 28925863

  • 1. Resveratrol Induces the Conversion from Amyloid to Amorphous Aggregation of β-lactoglobulin>.
    Ma B, Zhang F, Liu Y, Xie J, Wang X.
    Protein Pept Lett; 2018 Feb 08; 24(12):1113-1119. PubMed ID: 28925863
    [Abstract] [Full Text] [Related]

  • 2. Role of 1,2-dioleoyl-3-trimethylammonium-propane (DOTAP) in β-lactoglobulin aggregation.
    Ma B, Wang X, Liu Y, Li Z, Zhang F.
    Chem Phys Lipids; 2018 Jan 08; 210():76-81. PubMed ID: 29128322
    [Abstract] [Full Text] [Related]

  • 3. Macromolecular crowding modulates the kinetics and morphology of amyloid self-assembly by β-lactoglobulin.
    Ma B, Xie J, Wei L, Li W.
    Int J Biol Macromol; 2013 Feb 08; 53():82-7. PubMed ID: 23148946
    [Abstract] [Full Text] [Related]

  • 4. Negatively charged food additive dye "Allura Red" rapidly induces SDS-soluble amyloid fibril in beta-lactoglobulin protein.
    Al-Shabib NA, Khan JM, Malik A, Alsenaidy AM, Alsenaidy MA, Husain FM, Shamsi MB, Hidayathulla S, Khan RH.
    Int J Biol Macromol; 2018 Feb 08; 107(Pt B):1706-1716. PubMed ID: 29020652
    [Abstract] [Full Text] [Related]

  • 5. Heat-induced amyloid-like aggregation of β-lactoglobulin affected by glycation by α-dicarbonyl compounds in a model study.
    Zhao D, Zhang X, Xu D, Su G, Li B, Li C.
    J Sci Food Agric; 2020 Jan 30; 100(2):607-613. PubMed ID: 31591730
    [Abstract] [Full Text] [Related]

  • 6. Heat-induced amyloid-like aggregation of β-lactoglobulin regulated by glycation: A comparison of five kinds of reducing saccharides.
    Zhao D, Li L, Xu D, Sheng B, Chen J, Li B, Zhang X.
    Int J Biol Macromol; 2018 Dec 30; 120(Pt A):302-309. PubMed ID: 30102987
    [Abstract] [Full Text] [Related]

  • 7. Beta-lactoglobulin assembles into amyloid through sequential aggregated intermediates.
    Giurleo JT, He X, Talaga DS.
    J Mol Biol; 2008 Sep 19; 381(5):1332-48. PubMed ID: 18590743
    [Abstract] [Full Text] [Related]

  • 8. Fibrillar beta-lactoglobulin gels: Part 1. Fibril formation and structure.
    Gosal WS, Clark AH, Ross-Murphy SB.
    Biomacromolecules; 2004 Sep 19; 5(6):2408-19. PubMed ID: 15530058
    [Abstract] [Full Text] [Related]

  • 9. Insight into the co-solvent induced conformational changes and aggregation of bovine β-lactoglobulin.
    Pal S, Maity S, Sardar S, Chakraborty J, Halder UC.
    Int J Biol Macromol; 2016 Mar 19; 84():121-34. PubMed ID: 26657584
    [Abstract] [Full Text] [Related]

  • 10. Silver nanoparticle modulates the aggregation of beta-lactoglobulin and induces to form rod-like aggregates.
    Sardar S, Anas M, Maity S, Pal S, Parvej H, Begum S, Dalui R, Sepay N, Halder UC.
    Int J Biol Macromol; 2019 Mar 15; 125():596-604. PubMed ID: 30528992
    [Abstract] [Full Text] [Related]

  • 11. Amyloidogenic and non-amyloidogenic molten globule conformation of β-lactoglobulin in self-crowded regime.
    Venturi S, Rossi B, Tortora M, Torre R, Lapini A, Foggi P, Paolantoni M, Catalini S.
    Int J Biol Macromol; 2023 Jul 01; 242(Pt 1):124621. PubMed ID: 37141974
    [Abstract] [Full Text] [Related]

  • 12. Coaggregation of κ-Casein and β-Lactoglobulin Produces Morphologically Distinct Amyloid Fibrils.
    Raynes JK, Day L, Crepin P, Horrocks MH, Carver JA.
    Small; 2017 Apr 01; 13(14):. PubMed ID: 28146312
    [Abstract] [Full Text] [Related]

  • 13. Granulomorphometry: a suitable tool for identifying hydrophobic and disulfide bonds in β-lactoglobulin aggregates. Application to the study of β-lactoglobulin aggregation mechanism between 70 and 95°C.
    Petit J, Herbig AL, Moreau A, Le Page JF, Six T, Delaplace G.
    J Dairy Sci; 2012 Aug 01; 95(8):4188-202. PubMed ID: 22818432
    [Abstract] [Full Text] [Related]

  • 14. Investigating the effect of sugar-terminated nanoparticles on amyloid fibrillogenesis of β-lactoglobulin.
    Lin CY, Wang TH, How SC, Bednarikova Z, Fedunova D, Gazova Z, Wu JW, Wang SS.
    Int J Biol Macromol; 2020 Dec 15; 165(Pt A):291-307. PubMed ID: 32961178
    [Abstract] [Full Text] [Related]

  • 15. Protein oxidation during temperature-induced amyloid aggregation of beta-lactoglobulin.
    Keppler JK, Heyn TR, Meissner PM, Schrader K, Schwarz K.
    Food Chem; 2019 Aug 15; 289():223-231. PubMed ID: 30955606
    [Abstract] [Full Text] [Related]

  • 16. Inhibitory effects of β-ionone on amyloid fibril formation of β-lactoglobulin.
    Ma B, You X, Lu F.
    Int J Biol Macromol; 2014 Mar 15; 64():162-7. PubMed ID: 24325860
    [Abstract] [Full Text] [Related]

  • 17. Amyloid fibril formation by native and modified bovine β-lactoglobulins proceeds through unfolded form of proteins: a comparative study.
    Ghadami SA, Khodarahmi R, Ghobadi S, Ghasemi M, Pirmoradi S.
    Biophys Chem; 2011 Dec 15; 159(2-3):311-20. PubMed ID: 21920659
    [Abstract] [Full Text] [Related]

  • 18. Protective effect of β-lactoglobulin against heat induced loss of antioxidant activity of resveratrol.
    Guo Y, Jauregi P.
    Food Chem; 2018 Nov 15; 266():101-109. PubMed ID: 30381164
    [Abstract] [Full Text] [Related]

  • 19. Molecular Dynamics Insights into the Aggregation Behavior of N-Terminal β-Lactoglobulin Peptides.
    Pusara S.
    Int J Mol Sci; 2024 Apr 25; 25(9):. PubMed ID: 38731878
    [Abstract] [Full Text] [Related]

  • 20. Simultaneous acquisition of infrared, fluorescence and light scattering spectra of proteins: direct evidence for pre-fibrillar species in amyloid fibril formation.
    Baldassarre M, Bennett M, Barth A.
    Analyst; 2016 Feb 07; 141(3):963-73. PubMed ID: 26668843
    [Abstract] [Full Text] [Related]

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