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Items: 1 to 20 of 109

1.

Conformational Dynamics and Stability of U-Shaped and S-Shaped Amyloid β Assemblies.

Grasso G, Rebella M, Muscat S, Morbiducci U, Tuszynski J, Danani A, Deriu MA.

Int J Mol Sci. 2018 Feb 14;19(2). pii: E571. doi: 10.3390/ijms19020571.

2.

The inhibitory mechanism of a fullerene derivative against amyloid-β peptide aggregation: an atomistic simulation study.

Sun Y, Qian Z, Wei G.

Phys Chem Chem Phys. 2016 May 14;18(18):12582-91. doi: 10.1039/c6cp01014h. Epub 2016 Apr 19.

PMID:
27091578
3.

Polymorphic structures of Alzheimer's β-amyloid globulomers.

Yu X, Zheng J.

PLoS One. 2011;6(6):e20575. doi: 10.1371/journal.pone.0020575. Epub 2011 Jun 7.

4.

Aβ monomers transiently sample oligomer and fibril-like configurations: ensemble characterization using a combined MD/NMR approach.

Rosenman DJ, Connors CR, Chen W, Wang C, García AE.

J Mol Biol. 2013 Sep 23;425(18):3338-59. doi: 10.1016/j.jmb.2013.06.021. Epub 2013 Jun 25.

5.

Familial Alzheimer's disease Osaka mutant (ΔE22) β-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment.

Jang H, Arce FT, Ramachandran S, Kagan BL, Lal R, Nussinov R.

J Phys Chem B. 2013 Oct 3;117(39):11518-29. doi: 10.1021/jp405389n. Epub 2013 Sep 13.

6.

Stability of a Recently Found Triple-β-Stranded Aβ1-42 Fibril Motif.

Xi W, Wang W, Abbott G, Hansmann UH.

J Phys Chem B. 2016 May 26;120(20):4548-57. doi: 10.1021/acs.jpcb.6b01724. Epub 2016 May 17.

PMID:
27137996
7.

S14G-humanin inhibits Aβ1-42 fibril formation, disaggregates preformed fibrils, and protects against Aβ-induced cytotoxicity in vitro.

Zhang W, Du Y, Bai M, Xi Y, Li Z, Miao J.

J Pept Sci. 2013 Mar;19(3):159-65. doi: 10.1002/psc.2484. Epub 2013 Jan 24. Retraction in: J Pept Sci. 2016 Jun;22(6):434.

PMID:
23349038
8.

Conformational Ensembles of the Wild-Type and S8C Aβ1-42 Dimers.

Man VH, Nguyen PH, Derreumaux P.

J Phys Chem B. 2017 Mar 23;121(11):2434-2442. doi: 10.1021/acs.jpcb.7b00267. Epub 2017 Mar 10.

9.

Understanding amyloid fibril nucleation and aβ oligomer/drug interactions from computer simulations.

Nguyen P, Derreumaux P.

Acc Chem Res. 2014 Feb 18;47(2):603-11. doi: 10.1021/ar4002075. Epub 2013 Dec 24. Review.

PMID:
24368046
10.

Out-of-Register Aβ42 Assemblies as Models for Neurotoxic Oligomers and Fibrils.

Xi W, Vanderford EK, Hansmann UHE.

J Chem Theory Comput. 2018 Feb 13;14(2):1099-1110. doi: 10.1021/acs.jctc.7b01106. Epub 2018 Jan 31.

PMID:
29357242
11.
12.

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.

13.

Conformational stability of fibrillar amyloid-beta oligomers via protofilament pair formation - a systematic computational study.

Kahler A, Sticht H, Horn AH.

PLoS One. 2013 Jul 31;8(7):e70521. doi: 10.1371/journal.pone.0070521. Print 2013.

14.

The conformational stability of nonfibrillar amyloid-β peptide oligomers critically depends on the C-terminal peptide length.

Socher E, Sticht H, Horn AH.

ACS Chem Neurosci. 2014 Mar 19;5(3):161-7. doi: 10.1021/cn400208r. Epub 2014 Feb 11.

15.

Role of water in protein aggregation and amyloid polymorphism.

Thirumalai D, Reddy G, Straub JE.

Acc Chem Res. 2012 Jan 17;45(1):83-92. doi: 10.1021/ar2000869. Epub 2011 Jul 15.

16.

Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.

Meral D, Urbanc B.

J Mol Biol. 2013 Jun 26;425(12):2260-75. doi: 10.1016/j.jmb.2013.03.010. Epub 2013 Mar 13. Erratum in: J Mol Biol. 2015 Aug 14;427(16):2728-9.

17.

Molecular dynamics simulations to investigate the aggregation behaviors of the Abeta(17-42) oligomers.

Zhao JH, Liu HL, Liu YF, Lin HY, Fang HW, Ho Y, Tsai WB.

J Biomol Struct Dyn. 2009 Feb;26(4):481-90.

PMID:
19108587
18.

Mechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field.

Rojas A, Liwo A, Browne D, Scheraga HA.

J Mol Biol. 2010 Dec 3;404(3):537-52. doi: 10.1016/j.jmb.2010.09.057. Epub 2010 Oct 1.

19.

Understanding Amyloid-β Oligomerization at the Molecular Level: The Role of the Fibril Surface.

Barz B, Strodel B.

Chemistry. 2016 Jun 20;22(26):8768-72. doi: 10.1002/chem.201601701. Epub 2016 May 24.

PMID:
27135646
20.

Recent Advances by In Silico and In Vitro Studies of Amyloid-β 1-42 Fibril Depicted a S-Shape Conformation.

Villalobos Acosta DMÁ, Chimal Vega B, Correa Basurto J, Fragoso Morales LG, Rosales Hernández MC.

Int J Mol Sci. 2018 Aug 16;19(8). pii: E2415. doi: 10.3390/ijms19082415. Review.

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