Found: 13
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Surface carboxylation or PEGylation decreases CuO nanoparticles' cytotoxicity to human cells in vitro without compromising their antibacterial properties.
- Published in:
- Archives of Toxicology, 2020, v. 94, n. 5, p. 1561, doi. 10.1007/s00204-020-02720-7
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- Article
In situ fibrillizing amyloid-beta 1-42 induces neurite degeneration and apoptosis of differentiated SH-SY5Y cells.
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- PLoS ONE, 2017, v. 12, n. 10, p. 1, doi. 10.1371/journal.pone.0186636
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- Article
α-Lipoic acid: a potential regulator of copper metabolism in Alzheimer's disease.
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- Frontiers in Molecular Biosciences, 2024, p. 1, doi. 10.3389/fmolb.2024.1451536
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- Article
Copper(II) partially protects three histidine residues and the N‐terminus of amyloid‐β peptide from diethyl pyrocarbonate (DEPC) modification.
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- FEBS Open Bio, 2020, v. 10, n. 6, p. 1072, doi. 10.1002/2211-5463.12857
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- Article
Evaluation of Zn 2+ - and Cu 2+ -Binding Affinities of Native Cu,Zn-SOD1 and Its G93A Mutant by LC-ICP MS.
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- Molecules, 2022, v. 27, n. 10, p. 3160, doi. 10.3390/molecules27103160
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- Article
Redox properties of Cys<sub>2</sub>His<sub>2</sub> and Cys<sub>4</sub> zinc fingers determined by electrospray ionization mass spectrometry.
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- FEBS Open Bio, 2018, v. 8, n. 6, p. 923, doi. 10.1002/2211-5463.12422
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- Article
Metallothionein 2A affects the cell respiration by suppressing the expression of mitochondrial protein cytochrome c oxidase subunit II.
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- Journal of Bioenergetics & Biomembranes, 2015, v. 47, n. 3, p. 209, doi. 10.1007/s10863-015-9609-9
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- Article
Insulin Fibrillization at Acidic and Physiological pH Values is Controlled by Different Molecular Mechanisms.
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- Protein Journal, 2015, v. 34, n. 6, p. 398, doi. 10.1007/s10930-015-9634-x
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- Article
Affinity of zinc and copper ions for insulin monomers.
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- Metallomics, 2014, v. 6, n. 7, p. 1296, doi. 10.1039/c4mt00059e
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- Article
Effect of agitation on the peptide fibrillization: Alzheimer's amyloid- β peptide 1-42 but not amylin and insulin fibrils can grow under quiescent conditions.
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- Journal of Peptide Science, 2013, v. 19, n. 6, p. 386, doi. 10.1002/psc.2513
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- Article
Interference of low-molecular substances with the thioflavin-T fluorescence assay of amyloid fibrils.
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- Journal of Peptide Science, 2012, v. 18, n. 1, p. 59, doi. 10.1002/psc.1416
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- Article
Zn(II)- and Cu(II)-induced non-fibrillar aggregates of amyloid-β (1–42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators.
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- Journal of Neurochemistry, 2009, v. 110, n. 6, p. 1784, doi. 10.1111/j.1471-4159.2009.06269.x
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- Article
Binding of zinc(II) and copper(II) to the full-length Alzheimer’s amyloid-β peptide.
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- Journal of Neurochemistry, 2008, v. 104, n. 5, p. 1249, doi. 10.1111/j.1471-4159.2007.05061.x
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- Article