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Journal Abstract Search

159 related items for PubMed ID: 32650012

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  • 2. Heat treatment of soluble proteins isolated from human cataract lens leads to the formation of non-fibrillar amyloid-like protein aggregates.
    Mittal C, Kumari A, De I, Singh M, Harsolia R, Yadav JK.
    Int J Biol Macromol; 2021 Oct 01; 188():512-522. PubMed ID: 34333005
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  • 3. Congenital cataract-causing mutation βB1-L116P is prone to amyloid fibrils aggregation and protease degradation with low structural stability.
    Liu J, Xu W, Wang K, Chen F, Ren L, Xu J, Yao K, Chen X.
    Int J Biol Macromol; 2022 Jan 15; 195():475-482. PubMed ID: 34896472
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  • 4. Congenital microcornea-cataract syndrome-causing mutation X253R increases βB1-crystallin hydrophobicity to promote aggregate formation.
    Leng XY, Li HY, Wang J, Qi LB, Xi YB, Yan YB.
    Biochem J; 2016 Jul 15; 473(14):2087-96. PubMed ID: 27208166
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  • 7. Cataract-causing mutation S228P promotes βB1-crystallin aggregation and degradation by separating two interacting loops in C-terminal domain.
    Qi LB, Hu LD, Liu H, Li HY, Leng XY, Yan YB.
    Protein Cell; 2016 Jul 15; 7(7):501-15. PubMed ID: 27318838
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  • 8. Heteromeric formation with βA3 protects the low thermal stability of βB1-L116P.
    Xu J, Zhang Y, Liu J, Hu L, Luo C, Yao K, Chen X.
    Br J Ophthalmol; 2023 Nov 22; 107(12):1936-1942. PubMed ID: 36126102
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  • 9. Increasing βB1-crystallin sensitivity to proteolysis caused by the congenital cataract-microcornea syndrome mutation S129R.
    Wang S, Zhao WJ, Liu H, Gong H, Yan YB.
    Biochim Biophys Acta; 2013 Feb 22; 1832(2):302-11. PubMed ID: 23159606
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  • 10. Cataract-causing variant Q70P damages structural stability of βB1-crystallin and increases its tendency to form insoluble aggregates.
    Zhang Y, Ren L, Wu W, Liu J, Tian Q, Yao K, Yu Y, Hu L, Chen X.
    Int J Biol Macromol; 2023 Jul 01; 242(Pt 2):124722. PubMed ID: 37148932
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  • 11. A novel mutation in CRYBB1 associated with congenital cataract-microcornea syndrome: the p.Ser129Arg mutation destabilizes the βB1/βA3-crystallin heteromer but not the βB1-crystallin homomer.
    Wang KJ, Wang S, Cao NQ, Yan YB, Zhu SQ.
    Hum Mutat; 2011 Mar 01; 32(3):E2050-60. PubMed ID: 21972112
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  • 16. Cataract-Causing S93R Mutant Destabilized Structural Conformation of βB1 Crystallin Linking With Aggregates Formation and Cellular Viability.
    Ren L, Hu L, Zhang Y, Liu J, Xu W, Wu W, Xu J, Chen X, Yao K, Yu Y.
    Front Mol Biosci; 2022 Mar 01; 9():844719. PubMed ID: 35359596
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  • 17. Specificity of alphaA-crystallin binding to destabilized mutants of betaB1-crystallin.
    McHaourab HS, Kumar MS, Koteiche HA.
    FEBS Lett; 2007 May 15; 581(10):1939-43. PubMed ID: 17449033
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  • 18. Inhibition of amyloid fibrillation of γD-crystallin model peptide by the cochineal Carmine.
    Abu-Hussien M, Viswanathan GK, Borisover L, Mimouni M, Engel H, Zayit-Soudry S, Gazit E, Segal D.
    Int J Biol Macromol; 2021 Feb 01; 169():342-351. PubMed ID: 33347930
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  • 19. The importance of the last strand at the C-terminus in βB2-crystallin stability and assembly.
    Zhang K, Zhao WJ, Leng XY, Wang S, Yao K, Yan YB.
    Biochim Biophys Acta; 2014 Jan 01; 1842(1):44-55. PubMed ID: 24120835
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