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Items: 1 to 20 of 101

1.

A novel inhibitor of amyloid β (Aβ) peptide aggregation: from high throughput screening to efficacy in an animal model of Alzheimer disease.

McKoy AF, Chen J, Schupbach T, Hecht MH.

J Biol Chem. 2012 Nov 9;287(46):38992-9000. doi: 10.1074/jbc.M112.348037.

2.

Structure-activity relationships for a series of compounds that inhibit aggregation of the Alzheimer's peptide, Aβ42.

McKoy AF, Chen J, Schupbach T, Hecht MH.

Chem Biol Drug Des. 2014 Nov;84(5):505-12. doi: 10.1111/cbdd.12341.

3.
4.

Aβ42-oligomer Interacting Peptide (AIP) neutralizes toxic amyloid-β42 species and protects synaptic structure and function.

Barucker C, Bittner HJ, Chang PK, Cameron S, Hancock MA, Liebsch F, Hossain S, Harmeier A, Shaw H, Charron FM, Gensler M, Dembny P, Zhuang W, Schmitz D, Rabe JP, Rao Y, Lurz R, Hildebrand PW, McKinney RA, Multhaup G.

Sci Rep. 2015 Oct 29;5:15410. doi: 10.1038/srep15410.

5.

Aβ42 and Aβ40: similarities and differences.

Qiu T, Liu Q, Chen YX, Zhao YF, Li YM.

J Pept Sci. 2015 Jul;21(7):522-9. doi: 10.1002/psc.2789. Review.

PMID:
26018760
6.

Inhibition of Abeta42 aggregation using peptides selected from combinatorial libraries.

Baine M, Georgie DS, Shiferraw EZ, Nguyen TP, Nogaj LA, Moffet DA.

J Pept Sci. 2009 Aug;15(8):499-503. doi: 10.1002/psc.1150.

7.

A plant cell-based system that predicts aβ42 misfolding: potential as a drug discovery tool for Alzheimer's disease.

Zhao T, Zeng Y, Kermode AR.

Mol Genet Metab. 2012 Nov;107(3):571-9. doi: 10.1016/j.ymgme.2012.08.010.

PMID:
22944366
8.

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.

9.

Discovery of amyloid-beta aggregation inhibitors using an engineered assay for intracellular protein folding and solubility.

Lee LL, Ha H, Chang YT, DeLisa MP.

Protein Sci. 2009 Feb;18(2):277-86. doi: 10.1002/pro.33.

10.

Design of LVFFARK and LVFFARK-functionalized nanoparticles for inhibiting amyloid β-protein fibrillation and cytotoxicity.

Xiong N, Dong XY, Zheng J, Liu FF, Sun Y.

ACS Appl Mater Interfaces. 2015 Mar 18;7(10):5650-62. doi: 10.1021/acsami.5b00915.

PMID:
25700145
11.

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.

12.

Inhibition of amyloid-β aggregation in Alzheimer's disease.

Wang Q, Yu X, Li L, Zheng J.

Curr Pharm Des. 2014;20(8):1223-43. Review.

PMID:
23713775
13.

Oleuropein aglycone protects transgenic C. elegans strains expressing Aβ42 by reducing plaque load and motor deficit.

Diomede L, Rigacci S, Romeo M, Stefani M, Salmona M.

PLoS One. 2013;8(3):e58893. doi: 10.1371/journal.pone.0058893.

14.

Inhibition of Alzheimer's amyloid toxicity with a tricyclic pyrone molecule in vitro and in vivo.

Hong HS, Rana S, Barrigan L, Shi A, Zhang Y, Zhou F, Jin LW, Hua DH.

J Neurochem. 2009 Feb;108(4):1097-1108. doi: 10.1111/j.1471-4159.2008.05866.x.

15.

Substoichiometric inhibition of Abeta(1-40) aggregation by a tandem Abeta(40-1-Gly8-1-40) peptide.

Mustafi SM, Garai K, Crick SL, Baban B, Frieden C.

Biochem Biophys Res Commun. 2010 Jul 2;397(3):509-12. doi: 10.1016/j.bbrc.2010.05.144.

16.

An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.

Habchi J, Arosio P, Perni M, Costa AR, Yagi-Utsumi M, Joshi P, Chia S, Cohen SI, Müller MB, Linse S, Nollen EA, Dobson CM, Knowles TP, Vendruscolo M.

Sci Adv. 2016 Feb 12;2(2):e1501244. doi: 10.1126/sciadv.1501244.

17.

A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide.

Kim W, Kim Y, Min J, Kim DJ, Chang YT, Hecht MH.

ACS Chem Biol. 2006 Aug 22;1(7):461-9.

PMID:
17168524
18.

Site-specific inhibitory mechanism for amyloid β42 aggregation by catechol-type flavonoids targeting the Lys residues.

Sato M, Murakami K, Uno M, Nakagawa Y, Katayama S, Akagi K, Masuda Y, Takegoshi K, Irie K.

J Biol Chem. 2013 Aug 9;288(32):23212-24. doi: 10.1074/jbc.M113.464222.

19.

Effective screen for amyloid β aggregation inhibitor using amyloid β-conjugated gold nanoparticles.

Han SH, Chang YJ, Jung ES, Kim JW, Na DL, Mook-Jung I.

Int J Nanomedicine. 2010 Dec 15;6:1-12. doi: 10.2147/IJN.S15278.

20.

Biophysical characterization of Abeta42 C-terminal fragments: inhibitors of Abeta42 neurotoxicity.

Li H, Monien BH, Fradinger EA, Urbanc B, Bitan G.

Biochemistry. 2010 Feb 16;49(6):1259-67. doi: 10.1021/bi902075h.

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