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Items: 1 to 20 of 136

1.

Amyloid beta protein: Abeta40 inhibits Abeta42 oligomerization.

Murray MM, Bernstein SL, Nyugen V, Condron MM, Teplow DB, Bowers MT.

J Am Chem Soc. 2009 May 13;131(18):6316-7. doi: 10.1021/ja8092604.

2.

Alzheimer's Aβ42 and Aβ40 peptides form interlaced amyloid fibrils.

Gu L, Guo Z.

J Neurochem. 2013 Aug;126(3):305-11. doi: 10.1111/jnc.12202. Epub 2013 Mar 12.

3.

Aβ(39-42) modulates Aβ oligomerization but not fibril formation.

Gessel MM, Wu C, Li H, Bitan G, Shea JE, Bowers MT.

Biochemistry. 2012 Jan 10;51(1):108-17. doi: 10.1021/bi201520b. Epub 2011 Dec 23.

4.

Z-Phe-Ala-diazomethylketone (PADK) disrupts and remodels early oligomer states of the Alzheimer disease Aβ42 protein.

Zheng X, Gessel MM, Wisniewski ML, Viswanathan K, Wright DL, Bahr BA, Bowers MT.

J Biol Chem. 2012 Feb 24;287(9):6084-8. doi: 10.1074/jbc.C111.328575. Epub 2012 Jan 17.

5.

Structural dynamics of the ΔE22 (Osaka) familial Alzheimer's disease-linked amyloid β-protein.

Inayathullah M, Teplow DB.

Amyloid. 2011 Sep;18(3):98-107. doi: 10.3109/13506129.2011.580399. Epub 2011 Jun 13.

6.

C-terminal turn stability determines assembly differences between Aβ40 and Aβ42.

Roychaudhuri R, Yang M, Deshpande A, Cole GM, Frautschy S, Lomakin A, Benedek GB, Teplow DB.

J Mol Biol. 2013 Jan 23;425(2):292-308. doi: 10.1016/j.jmb.2012.11.006. Epub 2012 Nov 12.

7.

Synergistic interactions between Alzheimer's Aβ40 and Aβ42 on the surface of primary neurons revealed by single molecule microscopy.

Chang CC, Althaus JC, Carruthers CJ, Sutton MA, Steel DG, Gafni A.

PLoS One. 2013 Dec 2;8(12):e82139. doi: 10.1371/journal.pone.0082139. eCollection 2013.

8.

Synthetic Models of Quasi-Stable Amyloid β40 Oligomers with Significant Neurotoxicity.

Irie Y, Murakami K, Hanaki M, Hanaki Y, Suzuki T, Monobe Y, Takai T, Akagi KI, Kawase T, Hirose K, Irie K.

ACS Chem Neurosci. 2017 Apr 19;8(4):807-816. doi: 10.1021/acschemneuro.6b00390. Epub 2017 Jan 12.

PMID:
28026168
9.

Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease.

Bernstein SL, Dupuis NF, Lazo ND, Wyttenbach T, Condron MM, Bitan G, Teplow DB, Shea JE, Ruotolo BT, Robinson CV, Bowers MT.

Nat Chem. 2009 Jul;1(4):326-31. doi: 10.1038/nchem.247.

10.

Aβ40 and Aβ42 amyloid fibrils exhibit distinct molecular recycling properties.

Sánchez L, Madurga S, Pukala T, Vilaseca M, López-Iglesias C, Robinson CV, Giralt E, Carulla N.

J Am Chem Soc. 2011 May 4;133(17):6505-8. doi: 10.1021/ja1117123. Epub 2011 Apr 12.

PMID:
21486030
11.
12.

The Mechanism Underlying Amyloid Polymorphism is Opened for Alzheimer's Disease Amyloid-β Peptide.

Selivanova OM, Surin AK, Marchenkov VV, Dzhus UF, Grigorashvili EI, Suvorina MY, Glyakina AV, Dovidchenko NV, Galzitskaya OV.

J Alzheimers Dis. 2016 Sep 6;54(2):821-30. doi: 10.3233/JAD-160405.

PMID:
27567850
13.

The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity.

Jan A, Gokce O, Luthi-Carter R, Lashuel HA.

J Biol Chem. 2008 Oct 17;283(42):28176-89. doi: 10.1074/jbc.M803159200. Epub 2008 Aug 11.

14.

Amyloid β-Protein Assembly: Differential Effects of the Protective A2T Mutation and Recessive A2V Familial Alzheimer's Disease Mutation.

Zheng X, Liu D, Roychaudhuri R, Teplow DB, Bowers MT.

ACS Chem Neurosci. 2015 Oct 21;6(10):1732-40. doi: 10.1021/acschemneuro.5b00171. Epub 2015 Aug 12.

15.

Wild-type, Flemish, and Dutch amyloid-β exhibit different cytotoxicities depending on Aβ40 to Aβ42 interaction time and concentration ratio.

Shahnawaz M, Sharoar MG, Shin SY, Park IS.

J Pept Sci. 2013 Sep;19(9):545-53. doi: 10.1002/psc.2531. Epub 2013 Jul 13.

PMID:
23853087
16.

Elongation affinity, activation barrier, and stability of Aβ42 oligomers/fibrils in physiological saline.

Rodriguez RA, Chen LY, Plascencia-Villa G, Perry G.

Biochem Biophys Res Commun. 2017 May 27;487(2):444-449. doi: 10.1016/j.bbrc.2017.04.084. Epub 2017 Apr 17.

PMID:
28427941
17.

The structures of the E22Δ mutant-type amyloid-β alloforms and the impact of E22Δ mutation on the structures of the wild-type amyloid-β alloforms.

Coskuner O, Wise-Scira O, Perry G, Kitahara T.

ACS Chem Neurosci. 2013 Feb 20;4(2):310-20. doi: 10.1021/cn300149j. Epub 2012 Dec 18.

18.

Comparison of neurotoxicity of different aggregated forms of Aβ40, Aβ42 and Aβ43 in cell cultures.

Fu L, Sun Y, Guo Y, Chen Y, Yu B, Zhang H, Wu J, Yu X, Kong W, Wu H.

J Pept Sci. 2017 Mar;23(3):245-251. doi: 10.1002/psc.2975. Epub 2017 Feb 16.

PMID:
28211253
19.

Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.

Sato T, Kienlen-Campard P, Ahmed M, Liu W, Li H, Elliott JI, Aimoto S, Constantinescu SN, Octave JN, Smith SO.

Biochemistry. 2006 May 2;45(17):5503-16.

20.

Amino acid position-specific contributions to amyloid beta-protein oligomerization.

Maji SK, Ogorzalek Loo RR, Inayathullah M, Spring SM, Vollers SS, Condron MM, Bitan G, Loo JA, Teplow DB.

J Biol Chem. 2009 Aug 28;284(35):23580-91. doi: 10.1074/jbc.M109.038133. Epub 2009 Jun 30.

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