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Items: 10

1.

Stabilization and characterization of cytotoxic Aβ40 oligomers isolated from an aggregation reaction in the presence of zinc ions.

Mannini B, Habchi J, Chia SKR, Ruggeri FS, Perni M, Knowles TPJ, Dobson CM, Vendruscolo M.

ACS Chem Neurosci. 2018 Jul 9. doi: 10.1021/acschemneuro.8b00141. [Epub ahead of print]

PMID:
29986583
2.

Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine.

Perni M, Flagmeier P, Limbocker R, Cascella R, Aprile FA, Galvagnion C, Heller GT, Meisl G, Chen SW, Kumita JR, Challa PK, Kirkegaard JB, Cohen SIA, Mannini B, Barbut D, Nollen EAA, Cecchi C, Cremades N, Knowles TPJ, Chiti F, Zasloff M, Vendruscolo M, Dobson CM.

ACS Chem Biol. 2018 Jun 28. doi: 10.1021/acschembio.8b00466. [Epub ahead of print]

PMID:
29953201
3.

Massively parallel C. elegans tracking provides multi-dimensional fingerprints for phenotypic discovery.

Perni M, Challa PK, Kirkegaard JB, Limbocker R, Koopman M, Hardenberg MC, Sormanni P, Müller T, Saar KL, Roode LWY, Habchi J, Vecchi G, Fernando N, Casford S, Nollen EAA, Vendruscolo M, Dobson CM, Knowles TPJ.

J Neurosci Methods. 2018 Aug 1;306:57-67. doi: 10.1016/j.jneumeth.2018.02.005. Epub 2018 Feb 13.

PMID:
29452179
4.

Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers.

Fusco G, Chen SW, Williamson PTF, Cascella R, Perni M, Jarvis JA, Cecchi C, Vendruscolo M, Chiti F, Cremades N, Ying L, Dobson CM, De Simone A.

Science. 2017 Dec 15;358(6369):1440-1443. doi: 10.1126/science.aan6160.

5.

Delivery of Native Proteins into C. elegans Using a Transduction Protocol Based on Lipid Vesicles.

Perni M, Aprile FA, Casford S, Mannini B, Sormanni P, Dobson CM, Vendruscolo M.

Sci Rep. 2017 Nov 8;7(1):15045. doi: 10.1038/s41598-017-13755-9.

6.

Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method.

Aprile FA, Sormanni P, Perni M, Arosio P, Linse S, Knowles TPJ, Dobson CM, Vendruscolo M.

Sci Adv. 2017 Jun 21;3(6):e1700488. doi: 10.1126/sciadv.1700488. eCollection 2017 Jun.

7.

A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity.

Perni M, Galvagnion C, Maltsev A, Meisl G, Müller MB, Challa PK, Kirkegaard JB, Flagmeier P, Cohen SI, Cascella R, Chen SW, Limbocker R, Sormanni P, Heller GT, Aprile FA, Cremades N, Cecchi C, Chiti F, Nollen EA, Knowles TP, Vendruscolo M, Bax A, Zasloff M, Dobson CM.

Proc Natl Acad Sci U S A. 2017 Feb 7;114(6):E1009-E1017. doi: 10.1073/pnas.1610586114. Epub 2017 Jan 17. Erratum in: Proc Natl Acad Sci U S A. 2017 Mar 21;114(12 ):E2543. Limboker, Ryan [corrected to Limbocker, Ryan].

8.

Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer's disease.

Habchi J, Chia S, Limbocker R, Mannini B, Ahn M, Perni M, Hansson O, Arosio P, Kumita JR, Challa PK, Cohen SI, Linse S, Dobson CM, Knowles TP, Vendruscolo M.

Proc Natl Acad Sci U S A. 2017 Jan 10;114(2):E200-E208. doi: 10.1073/pnas.1615613114. Epub 2016 Dec 23.

9.

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. eCollection 2016 Feb.

10.

TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells.

Capitini C, Conti S, Perni M, Guidi F, Cascella R, De Poli A, Penco A, Relini A, Cecchi C, Chiti F.

PLoS One. 2014 Jan 30;9(1):e86720. doi: 10.1371/journal.pone.0086720. eCollection 2014.

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