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Journal Abstract Search

178 related items for PubMed ID: 30102987

  • 1. 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; 120(Pt A):302-309. PubMed ID: 30102987
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  • 4. 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
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  • 6. 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 08; 84():121-34. PubMed ID: 26657584
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  • 7. Glycation and phosphorylation of beta-lactoglobulin by dry-heating: effect on protein structure and some properties.
    Enomoto H, Li CP, Morizane K, Ibrahim HR, Sugimoto Y, Ohki S, Ohtomo H, Aoki T.
    J Agric Food Chem; 2007 Mar 21; 55(6):2392-8. PubMed ID: 17315885
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  • 8. Effects of heating and glycation of beta-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients.
    Taheri-Kafrani A, Gaudin JC, Rabesona H, Nioi C, Agarwal D, Drouet M, Chobert JM, Bordbar AK, Haertle T.
    J Agric Food Chem; 2009 Jun 10; 57(11):4974-82. PubMed ID: 19489627
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  • 9. 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 10; 13(14):. PubMed ID: 28146312
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  • 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 10; 95(8):4188-202. PubMed ID: 22818432
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  • 14. Heat-induced redistribution of disulfide bonds in milk proteins. 1. Bovine beta-lactoglobulin.
    Creamer LK, Bienvenue A, Nilsson H, Paulsson M, van Wanroij M, Lowe EK, Anema SG, Boland MJ, Jiménez-Flores R.
    J Agric Food Chem; 2004 Dec 15; 52(25):7660-8. PubMed ID: 15675818
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  • 15. Β-lactoglobulin self-assembly: structural changes in early stages and disulfide bonding in fibrils.
    Dave AC, Loveday SM, Anema SG, Loo TS, Norris GE, Jameson GB, Singh H.
    J Agric Food Chem; 2013 Aug 14; 61(32):7817-28. PubMed ID: 23848407
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  • 16. 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
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  • 17. Influence of calcium on β-lactoglobulin denaturation kinetics: Implications in unfolding and aggregation mechanisms.
    Petit J, Herbig AL, Moreau A, Delaplace G.
    J Dairy Sci; 2011 Dec 19; 94(12):5794-810. PubMed ID: 22118070
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  • 18. 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 19; 159(2-3):311-20. PubMed ID: 21920659
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  • 19. Formation of β-lactoglobulin nanofibrils by microwave heating gives a peptide composition different from conventional heating.
    Hettiarachchi CA, Melton LD, Gerrard JA, Loveday SM.
    Biomacromolecules; 2012 Sep 10; 13(9):2868-80. PubMed ID: 22877308
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  • 20. Hydrophobicity and aggregation, but not glycation, are key determinants for uptake of thermally processed β-lactoglobulin by THP-1 macrophages.
    Deng Y, Govers C, Bastiaan-Net S, van der Hulst N, Hettinga K, Wichers HJ.
    Food Res Int; 2019 Jun 10; 120():102-113. PubMed ID: 31000219
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