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Items: 1 to 20 of 270

1.

Copper prevents amyloid-β(1-42) from forming amyloid fibrils under near-physiological conditions in vitro.

Mold M, Ouro-Gnao L, Wieckowski BM, Exley C.

Sci Rep. 2013;3:1256. doi: 10.1038/srep01256. Epub 2013 Feb 13.

2.

Aluminum, copper, iron and zinc differentially alter amyloid-Aβ(1-42) aggregation and toxicity.

Bolognin S, Messori L, Drago D, Gabbiani C, Cendron L, Zatta P.

Int J Biochem Cell Biol. 2011 Jun;43(6):877-85. doi: 10.1016/j.biocel.2011.02.009. Epub 2011 Mar 3.

PMID:
21376832
3.

Copper abolishes the beta-sheet secondary structure of preformed amyloid fibrils of amyloid-beta(42).

House E, Mold M, Collingwood J, Baldwin A, Goodwin S, Exley C.

J Alzheimers Dis. 2009;18(4):811-7. doi: 10.3233/JAD-2009-1235.

4.

Zn(II)- and Cu(II)-induced non-fibrillar aggregates of amyloid-beta (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators.

Tõugu V, Karafin A, Zovo K, Chung RS, Howells C, West AK, Palumaa P.

J Neurochem. 2009 Sep;110(6):1784-95. doi: 10.1111/j.1471-4159.2009.06269.x. Epub 2009 Jul 8.

5.

Engineered non-fluorescent Affibody molecules facilitate studies of the amyloid-beta (Aβ) peptide in monomeric form: low pH was found to reduce Aβ/Cu(II) binding affinity.

Lindgren J, Segerfeldt P, Sholts SB, Gräslund A, Karlström AE, Wärmländer SK.

J Inorg Biochem. 2013 Mar;120:18-23. doi: 10.1016/j.jinorgbio.2012.11.005. Epub 2012 Nov 30.

PMID:
23262458
6.

Amyloid-β peptide (1-42) aggregation induced by copper ions under acidic conditions.

Bin Y, Li X, He Y, Chen S, Xiang J.

Acta Biochim Biophys Sin (Shanghai). 2013 Jul;45(7):570-7. doi: 10.1093/abbs/gmt044. Epub 2013 Jun 6.

PMID:
23747389
7.

AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin.

Raman B, Ban T, Sakai M, Pasta SY, Ramakrishna T, Naiki H, Goto Y, Rao ChM.

Biochem J. 2005 Dec 15;392(Pt 3):573-81.

8.

The second Cu(II)-binding site in a proton-rich environment interferes with the aggregation of amyloid-beta(1-40) into amyloid fibrils.

Jun S, Gillespie JR, Shin BK, Saxena S.

Biochemistry. 2009 Nov 17;48(45):10724-32. doi: 10.1021/bi9012935.

PMID:
19824649
9.

Role of metal ions in the self-assembly of the Alzheimer's amyloid-β peptide.

Faller P, Hureau C, Berthoumieu O.

Inorg Chem. 2013 Nov 4;52(21):12193-206. doi: 10.1021/ic4003059. Epub 2013 Apr 22. Review.

PMID:
23607830
10.

Metal ions differentially influence the aggregation and deposition of Alzheimer's beta-amyloid on a solid template.

Ha C, Ryu J, Park CB.

Biochemistry. 2007 May 22;46(20):6118-25. Epub 2007 Apr 25.

PMID:
17455909
11.

Inhibition of Cu-amyloid-β by using bifunctional peptides with β-sheet breaker and chelator moieties.

Jensen M, Canning A, Chiha S, Bouquerel P, Pedersen JT, Østergaard J, Cuvillier O, Sasaki I, Hureau C, Faller P.

Chemistry. 2012 Apr 16;18(16):4836-9. doi: 10.1002/chem.201103546. Epub 2012 Mar 15.

PMID:
22422637
12.

Studies on the interactions of copper and zinc ions with β-amyloid peptides by a surface plasmon resonance biosensor.

Yao F, Zhang R, Tian H, Li X.

Int J Mol Sci. 2012;13(9):11832-43. doi: 10.3390/ijms130911832. Epub 2012 Sep 19.

13.

In silico and in vitro studies to elucidate the role of Cu2+ and galanthamine as the limiting step in the amyloid beta (1-42) fibrillation process.

Hernández-Rodríguez M, Correa-Basurto J, Benitez-Cardoza CG, Resendiz-Albor AA, Rosales-Hernández MC.

Protein Sci. 2013 Oct;22(10):1320-35. doi: 10.1002/pro.2319. Epub 2013 Aug 19.

14.

Reaction rates and mechanism of the ascorbic acid oxidation by molecular oxygen facilitated by Cu(II)-containing amyloid-beta complexes and aggregates.

Jiang D, Li X, Liu L, Yagnik GB, Zhou F.

J Phys Chem B. 2010 Apr 15;114(14):4896-903. doi: 10.1021/jp9095375.

15.

Stability of Aβ (1-42) peptide fibrils as consequence of environmental modifications.

Gregori M, Cassina V, Brogioli D, Salerno D, De Kimpe L, Scheper W, Masserini M, Mantegazza F.

Eur Biophys J. 2010 Nov;39(12):1613-23. doi: 10.1007/s00249-010-0619-6. Epub 2010 Aug 9.

PMID:
20694815
16.

Molecular-level examination of Cu2+ binding structure for amyloid fibrils of 40-residue Alzheimer's β by solid-state NMR spectroscopy.

Parthasarathy S, Long F, Miller Y, Xiao Y, McElheny D, Thurber K, Ma B, Nussinov R, Ishii Y.

J Am Chem Soc. 2011 Mar 16;133(10):3390-400. doi: 10.1021/ja1072178. Epub 2011 Feb 22.

17.

Human pro-islet amyloid polypeptide (ProIAPP(1-48)) forms amyloid fibrils and amyloid spherulites in vitro.

Exley C, House E, Patel T, Wu L, Fraser PE.

J Inorg Biochem. 2010 Oct;104(10):1125-9. doi: 10.1016/j.jinorgbio.2010.05.012. Epub 2010 Jun 9.

PMID:
20579740
18.

Local structure and global patterning of Cu2+ binding in fibrillar amyloid-β [Aβ(1-40)] protein.

Gunderson WA, Hernández-Guzmán J, Karr JW, Sun L, Szalai VA, Warncke K.

J Am Chem Soc. 2012 Nov 7;134(44):18330-7. doi: 10.1021/ja306946q. Epub 2012 Oct 24.

19.

β-amyloid fibrils in Alzheimer disease are not inert when bound to copper ions but can degrade hydrogen peroxide and generate reactive oxygen species.

Mayes J, Tinker-Mill C, Kolosov O, Zhang H, Tabner BJ, Allsop D.

J Biol Chem. 2014 Apr 25;289(17):12052-62. doi: 10.1074/jbc.M113.525212. Epub 2014 Mar 11.

20.

A bifunctional non-natural tetrapeptide modulates amyloid-beta peptide aggregation in the presence of Cu(ii).

Márquez M, Blancas-Mejía LM, Campos A, Rojas L, Castañeda-Hernández G, Quintanar L.

Metallomics. 2014 Dec;6(12):2189-92. doi: 10.1039/c4mt00257a. Epub 2014 Oct 28.

PMID:
25350343
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