Residue-specific binding of Ni(II) ions influences the structure and aggregation of amyloid beta (Aβ) peptides

Autor: Elina Berntsson, Faraz Vosough, Teodor Svantesson, Jonathan Pansieri, Igor A. Iashchishyn, Lucija Ostojić, Xiaolin Dong, Suman Paul, Jüri Jarvet, Per M. Roos, Andreas Barth, Ludmilla A. Morozova-Roche, Astrid Gräslund, Sebastian K. T. S. Wärmländer

Publikováno v: Scientific Reports, Vol 13, Iss 1, Pp 1-19 (2023)

Abstract Alzheimer’s disease (AD) is the most common cause of dementia worldwide. AD brains display deposits of insoluble amyloid plaques consisting mainly of aggregated amyloid-β (Aβ) peptides, and Aβ oligomers are likely a toxic species in AD

Externí odkaz: https://doaj.org/article/903339b11f044e5986d29f6a034d02f2

Co-aggregation of pro-inflammatory S100A9 with α-synuclein in Parkinson’s disease: ex vivo and in vitro studies

Autor: Istvan Horvath, Igor A. Iashchishyn, Roman A. Moskalenko, Chao Wang, Sebastian K. T. S. Wärmländer, Cecilia Wallin, Astrid Gräslund, Gabor G. Kovacs, Ludmilla A. Morozova-Roche

Publikováno v: Journal of Neuroinflammation, Vol 15, Iss 1, Pp 1-16 (2018)

Abstract Background Chronic neuroinflammation is a hallmark of Parkinson’s disease (PD) pathophysiology, associated with increased levels of pro-inflammatory factors in PD brain tissues. The pro-inflammatory mediator and highly amyloidogenic protei

Externí odkaz: https://doaj.org/article/3b9ba4579bfc41a19ce74af63ca4e99b

Proinflammatory S100A9 stimulates TLR4/NF-κB signaling pathways causing enhanced phagocytic capacity of microglial cells

Autor: Xiaoyin Zhang, Dan Sun, Xin Zhou, Ce Zhang, Qing Yin, Li Chen, Yong Tang, Yonggang Liu, Ludmilla A Morozova-Roche

Publikováno v: Immunology Letters. 255:54-61

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1c83eb8681433efd29c4a69aa395c215
https://doi.org/10.1016/j.imlet.2023.02.008

Surface-Directed Structural Transition of Amyloidogenic Aggregates and the Resulting Neurotoxicity

Autor: Dan Sun, Haiming Fan, Ludmilla A. Morozova-Roche, Hao Chen, Yin Tian, Yonggang Liu, Ce Zhang

Publikováno v: ACS Omega
ACS Omega, Vol 5, Iss 6, Pp 2856-2864 (2020)

The transition of amyloidogenic species into ordered structures (i.e., prefibrillar oligomers, protofibrils, mature fibrils, and amyloidogenic aggregates) is closely associated with many neurodegenerative disease pathologies. It is increasingly appre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac5e0442baa4f051766f30696bfc5486
http://europepmc.org/articles/PMC7034003

Human Polymerase δ-Interacting Protein 2 (PolDIP2) Inhibits the Formation of Human Tau Oligomers and Fibrils

Autor: Kazutoshi Kasho, Ludmilla A. Morozova-Roche, Vytautas Smirnovas, Lukas Krasauskas, Gorazd Stojkovič, Sjoerd Wanrooij

Publikováno v: International Journal of Molecular Sciences
International journal of molecular sciences, Basel : MDPI, 2021, vol. 22, no. 11, art. no. 5768, p. [1-14]
International Journal of Molecular Sciences, Vol 22, Iss 5768, p 5768 (2021)
Volume 22
Issue 11

A central characteristic of Alzheimer’s disease (AD) and other tauopathies is the accumulation of aggregated and misfolded Tau deposits in the brain. Tau-targeting therapies for AD have been unsuccessful in patients to date. Here we show that human

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d9812349da9892a4e9d0b1463fbb0bf
https://pubmed.ncbi.nlm.nih.gov/34071254