Publicaciones 2011-2020

@article{RN341,
title = {The Polyphenol Altenusin Inhibits in Vitro Fibrillization of Tau and Reduces Induced Tau Pathology in Primary Neurons},
author = { S.W. Chua and A. Cornejo and J. Van Eersel and C.H. Stevens and I. Vaca and M. Cueto and M. Kassiou and A. Gladbach and A. Macmillan and L. Lewis and R. Whan and L.M. Ittner},
url = {/brokenurl#<Go to ISI>://WOS:000399968400009},
doi = {10.1021/acschemneuro.6b00433},
issn = {1948-7193},
year = {2017},
date = {2017-01-01},
journal = {Acs Chemical Neuroscience},
volume = {8},
number = {4},
pages = {743-751},
abstract = {In Alzheimer's disease, the microtubule-associated protein tau forms intracellular neurofibrillary tangles (NFTs). A critical step in the formation of NFTs is the conversion of soluble tau into insoluble filaments. Accordingly, a current therapeutic strategy in clinical trials is aimed at preventing tau aggregation. Here, we assessed altenusin, a bioactive polyphenolic compound, for its potential to inhibit tau aggregation. Altenusin inhibits aggregation of tau protein into paired helical filaments in vitro. This was associated with stabilization of, tau dimers and other oligomers into globular structures as revealed by atomic force microscopy. Moreover, altenusin reduced tau phosphorylation in cells expressing pathogenic tau, and prevented neuritic tau pathology induced by incubation of primary neurons with tau fibrils. However, treatment of tau transgenic mice did not improve neuropathology and functional deficits. Taken together, altenusin prevents tau fibrillization in vitro and induced tau pathology in neurons.},
keywords = {alzheimer's alzheimers-disease, antiaggregation, associated disease, filaments, helical methylene-blue, mice, microtubule model, mouse neurodegeneration, paired phosphorylation, protein tangles tau, tauopathy, transgenic},
pubstate = {published},
tppubtype = {article}
}

@article{RN286,
title = {Secondary Metabolites in Ramalina Terebrata Detected by Uhplc/Esi/Ms/Ms and Identification of Parietin as Tau Protein Inhibitor},
author = { A. Cornejo and F. Salgado and J. Caballero and R. Vargas and M. Simirgiotis and C. Areche},
url = {/brokenurl#<Go to ISI>://WOS:000382337900115},
doi = {10.3390/ijms17081303},
issn = {1422-0067},
year = {2016},
date = {2016-01-01},
journal = {International Journal of Molecular Sciences},
volume = {17},
number = {8},
abstract = {Liquid chromatography coupled with mass spectrometry is an outstanding methodology for fast analysis of phenolic compounds in biological samples. Twenty two compounds were quickly and accurately identified in the methanolic extract of the Antarctic lichen Ramalina terebrata for the first time using ultra high pressure liquid chromatography coupled with photodiode array detector and high resolution mass spectrometry (UHPLC-PDA-Q/Orbitrap/MS/MS). In addition, the extract and the four compounds isolated from this species were tested for the inhibitory activity of tau protein aggregation, which is a protein involved in Alzheimer's disease (AD). All compounds showed null activity with the exception of parietin, which it was able to inhibit aggregation process of tau in a concentration range between 3 mu g/mL (10 mu M) to 28 mu g/mL (100 mu M). In addition, we show how parietin interact with tau (306)VQIVYK(311) hexapeptide inside of the microtubule binding domain (4R) with the help of molecular docking experiments. Finally, the constituents present in the methanolic extract could possibly contribute to the established anti-aggregation activity for this extract and this in-depth analysis of the chemical composition of R. terebrata could guide further research into its medicinal properties and potential uses.},
keywords = {alzheimer's alzheimers-disease, biological disease, docking, evaluation, fibril filaments, formation helical lichen lichens, liquid-chromatography, mass-spectrometry, molecular paired parietin, phenolic-compounds, protein, ramalina, tau uhplc-q/orbitrap/ms/ms, uhplc/ms, xanthoria-parietina},
pubstate = {published},
tppubtype = {article}
}