Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Tomas Šneideris"'
Autor:
Natalia Szulc, Michał Burdukiewicz, Marlena Gąsior-Głogowska, Jakub W. Wojciechowski, Jarosław Chilimoniuk, Paweł Mackiewicz, Tomas Šneideris, Vytautas Smirnovas, Malgorzata Kotulska
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
Abstract Several disorders are related to amyloid aggregation of proteins, for example Alzheimer’s or Parkinson’s diseases. Amyloid proteins form fibrils of aggregated beta structures. This is preceded by formation of oligomers—the most cytotox
Externí odkaz:
https://doaj.org/article/1b581be9c50f488f8323d496d600981b
Autor:
Rodrigo Cataldi, Sean Chia, Katarina Pisani, Francesco S. Ruggeri, Catherine K. Xu, Tomas Šneideris, Michele Perni, Sunehera Sarwat, Priyanka Joshi, Janet R. Kumita, Sara Linse, Johnny Habchi, Tuomas P. J. Knowles, Benedetta Mannini, Christopher M. Dobson, Michele Vendruscolo
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-10 (2021)
Cataldi et al. investigates the impact of the dopamine derivative DOPAL on the Aβ peptide oligomer formation. They report that DOPAL promotes the formation of stable Aβ oligomers that exert toxicity on neuroblastoma cells by increasing cytosolic ca
Externí odkaz:
https://doaj.org/article/4d14647112154fb9bb2c49c0fb14d6b7
Autor:
Rodrigo Cataldi, Sean Chia, Katarina Pisani, Francesco S. Ruggeri, Catherine K. Xu, Tomas Šneideris, Michele Perni, Sunehera Sarwat, Priyanka Joshi, Janet R. Kumita, Sara Linse, Johnny Habchi, Tuomas P. J. Knowles, Benedetta Mannini, Christopher M. Dobson, Michele Vendruscolo
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-1 (2021)
A Correction to this paper has been published: https://doi.org/10.1038/s42003-021-01680-7
Externí odkaz:
https://doaj.org/article/dfee79f008f742058b9470e8d55da296
Autor:
Tomas Šneideris, Lina Baranauskienė, Jonathan G. Cannon, Rasa Rutkienė, Rolandas Meškys, Vytautas Smirnovas
Publikováno v:
PeerJ, Vol 3, p e1271 (2015)
A range of diseases is associated with amyloid fibril formation. Despite different proteins being responsible for each disease, all of them share similar features including beta-sheet-rich secondary structure and fibril-like protein aggregates. A num
Externí odkaz:
https://doaj.org/article/b1012f5598f04939a6007b9a1c2a2e59
Autor:
Tomas Sneideris, Nadia A. Erkamp, Hannes Ausserwöger, Kadi L. Saar, Timothy J. Welsh, Daoyuan Qian, Kai Katsuya-Gaviria, Margaret L. L. Y. Johncock, Georg Krainer, Alexander Borodavka, Tuomas P. J. Knowles
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract Antimicrobial peptides (AMPs), which combat bacterial infections by disrupting the bacterial cell membrane or interacting with intracellular targets, are naturally produced by a number of different organisms, and are increasingly also explor
Externí odkaz:
https://doaj.org/article/f347a58e300d44799db612aff9c099ee
Autor:
Nadia A. Erkamp, Tomas Sneideris, Hannes Ausserwöger, Daoyuan Qian, Seema Qamar, Jonathon Nixon-Abell, Peter St George-Hyslop, Jeremy D. Schmit, David A. Weitz, Tuomas P. J. Knowles
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-8 (2023)
Biomolecular condensates with internal structure allow cells to further organise their processes. In this work the authors investigate how condensates can obtain an internal structure with droplets of dilute phase inside via kinetic, rather than pure
Externí odkaz:
https://doaj.org/article/7c07f116ca21498c96519569ce628d42
Autor:
Jēkabs Fridmanis, Zigmantas Toleikis, Tomas Sneideris, Mantas Ziaunys, Raitis Bobrovs, Vytautas Smirnovas, Kristaps Jaudzems
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 17, p 9635 (2021)
Prion diseases are associated with conformational conversion of cellular prion protein into a misfolded pathogenic form, which resembles many properties of amyloid fibrils. The same prion protein sequence can misfold into different conformations, whi
Externí odkaz:
https://doaj.org/article/5227503a16954705b49fdd0bfc0c08b7
Publikováno v:
PeerJ, Vol 7, p e7554 (2019)
Protein aggregation into amyloid fibrils has been linked to multiple neurodegenerative disorders. Determining the kinetics of fibril formation, as well as their structural stability are important for the mechanistic understanding of amyloid aggregati
Externí odkaz:
https://doaj.org/article/d8a1f12afd9b447bbf3adecac707527a
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 4, p 1775 (2021)
Protein aggregation into amyloid fibrils is linked to multiple disorders. The understanding of how natively non-harmful proteins convert to these highly cytotoxic amyloid aggregates is still not sufficient, with new ideas and hypotheses being present
Externí odkaz:
https://doaj.org/article/5eb9d9bf43a44ebd881fdb39a2d141d4
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 23, p 8916 (2020)
The formation of amyloid fibrils is linked to multiple neurodegenerative disorders, including Alzheimer’s and Parkinson’s disease. Despite years of research and countless studies on the topic of such aggregate formation, as well as their resultin
Externí odkaz:
https://doaj.org/article/ef7bb2c52ea14255a531a44ef2eb15c2