Age-related disturbances in DNA (hydroxy)methylation in APP/PS1 mice

Autor: Chouliaras Leonidas, Lardenoije Roy, Kenis Gunter, Mastroeni Diego, Hof Patrick R., Os Jim van, Steinbusch Harry W.M., van Leeuwen Fred W., Rutten Bart P.F., van den Hove Daniel L.A.

Publikováno v: Translational Neuroscience, Vol 9, Iss 1, Pp 190-202 (2018)

Brain aging has been associated with aberrant DNA methylation patterns, and changes in the levels of DNA methylation and associated markers have been observed in the brains of Alzheimer’s disease (AD) patients. DNA hydroxymethylation, however, has

Externí odkaz: https://doaj.org/article/11f7a83096394034ba2d2df2d2de7937

Autophagy is increased following either pharmacological or genetic silencing of mGluR5 signaling in Alzheimer’s disease mouse models

Autor: Khaled S. Abd-Elrahman, Alison Hamilton, Maryam Vasefi, Stephen S. G. Ferguson

Publikováno v: Molecular Brain, Vol 11, Iss 1, Pp 1-8 (2018)

Abstract Alzheimer’s disease (AD) is characterized by neurotoxicity mediated by the accumulation of beta amyloid (Aβ) oligomers, causing neuronal loss and progressive cognitive decline. Genetic deletion or chronic pharmacological inhibition of mGl

Externí odkaz: https://doaj.org/article/837d5bcb12f0440aaac2e7c5836b767c

Effector function of anti-pyroglutamate-3 Aβ antibodies affects cognitive benefit, glial activation and amyloid clearance in Alzheimer’s-like mice

Autor: Stephan Schilling, Brian O'Nuallain, Marcelo F. DiCarli, Mi-Ae Park, Helen Crehan, Kevin X. Le, Bin Liu, Birgit Hutter-Paier, Martin Kleinschmidt, Thore Hettmann, Cynthia A. Lemere, Jens Ulrich Rahfeld, Barbara J. Caldarone, Jeffrey L. Frost, Inge Lues

Publikováno v: Alzheimer’s Research & Therapy, Vol 12, Iss 1, Pp 1-19 (2020)
Alzheimer's Research & Therapy

Background Pyroglutamate-3 Aβ (pGlu-3 Aβ) is an N-terminally truncated and post-translationally modified Aβ species found in Alzheimer’s disease (AD) brain. Its increased peptide aggregation propensity and toxicity make it an attractive emerging

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ebfc5f03231495d17f7cd7a3efadcdd
https://doaj.org/article/a0a62adb0fd742e6bf4a5334e028d25a

Age-Related Disturbances In Dna (Hydroxy) Methylation In App/Ps1 Mice

Autor: Leonidas Chouliaras, Fred W. Van Leeuwen, Diego Mastroeni, Patrick R. Hof, Daniel L.A. van den Hove, H.W.M. Steinbusch, Gunter Kenis, Roy Lardenoije, Jim van Os, Bart P. F. Rutten

Publikováno v: Translational Neuroscience, 9(1), 190. De Gruyter Open Ltd.
Translational Neuroscience, 9(1), 190-202. De Gruyter Open Ltd.
Translational Neuroscience
Translational Neuroscience, Vol 9, Iss 1, Pp 190-202 (2018)

Brain aging has been associated with aberrant DNA methylation patterns, and changes in the levels of DNA methylation and associated markers have been observed in the brains of Alzheimer’s disease (AD) patients. DNA hydroxymethylation, however, has

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f938b75188fbc3dabcb255825d91051
https://doi.org/10.1515/tnsci-2018-0028

Age-Dependent Changes in the Sarkosyl-Insoluble Proteome of APPSWE/PS1ΔE9 Transgenic Mice Implicate Dysfunctional Mitochondria in the Pathogenesis of Alzheimer's Disease

Autor: Athanasios Metaxas, Martin R. Larsen, Camilla Thygesen, Bente Finsen

Publikováno v: Thygesen, C, Metaxas, A, Larsen, M R & Finsen, B 2018, ' Age-Dependent Changes in the Sarkosyl-Insoluble Proteome of APPSWE/PS1ΔE9 Transgenic Mice Implicate Dysfunctional Mitochondria in the Pathogenesis of Alzheimer's Disease ', Journal of Alzheimer's disease : JAD, vol. 64, no. 4, pp. 1247-1259 . https://doi.org/10.3233/JAD-180197

BACKGROUND: Alzheimer's disease (AD), the most common cause of dementia, is characterized by the intra- and extracellular aggregation and accumulation of proteins. The major molecular hallmark is the aggregation of amyloid-β (Aβ) and hyperphosphory

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb1ecce951f601f25f194b39249a888a
https://pubmed.ncbi.nlm.nih.gov/29991132