Zobrazeno 1 - 10
of 389
pro vyhledávání: '"Sara Linse"'
Autor:
Catherine K. Xu, Georg Meisl, Ewa A. Andrzejewska, Georg Krainer, Alexander J. Dear, Marta Castellana-Cruz, Soma Turi, Irina A. Edu, Giorgio Vivacqua, Raphaël P. B. Jacquat, William E. Arter, Maria Grazia Spillantini, Michele Vendruscolo, Sara Linse, Tuomas P. J. Knowles
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-11 (2024)
Abstract Oligomeric species arising during the aggregation of α-synuclein are implicated as a major source of toxicity in Parkinson’s disease, and thus a major potential drug target. However, both their mechanism of formation and role in aggregati
Externí odkaz:
https://doaj.org/article/a4d1104eb0184ade8af0b5e5b4fb8983
Publikováno v:
JACS Au, Vol 4, Iss 4, Pp 1250-1262 (2024)
Externí odkaz:
https://doaj.org/article/ba382113cc6443619aa3b02c1ce60f8e
Publikováno v:
QRB Discovery, Vol 4 (2023)
The human chaperone DNAJB6b increases the solubility of proteins involved in protein aggregation diseases and suppresses the nucleation of amyloid structures. Due to such favourable properties, DNAJB6b has gained increasing attention over the past de
Externí odkaz:
https://doaj.org/article/0fcaf53ac0fe47b0a50372abc2bc7adc
Autor:
Alexandra Andersson, Marco Fornasier, Katarzyna Makasewicz, Tinna Pálmadóttir, Sara Linse, Emma Sparr, Peter Jönsson
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 15 (2022)
Interactions of lipid vesicles play important roles in a large variety of functions and dysfunctions in the human body. Vital for several biochemical functions is the interaction between monomeric proteins and lipid membranes, and the induced phenome
Externí odkaz:
https://doaj.org/article/e6bf2404c8714d98aa99689e2d37eead
Autor:
Tanja Weiffert, Georg Meisl, Samo Curk, Risto Cukalevski, Anđela Šarić, Tuomas P. J. Knowles, Sara Linse
Publikováno v:
Frontiers in Neuroscience, Vol 16 (2022)
Amyloid formation is linked to devastating neurodegenerative diseases, motivating detailed studies of the mechanisms of amyloid formation. For Aβ, the peptide associated with Alzheimer’s disease, the mechanism and rate of aggregation have been est
Externí odkaz:
https://doaj.org/article/d37c9ffbb60b4063b3536fe69e8183fc
Autor:
Tinna Pálmadóttir, Christopher A. Waudby, Katja Bernfur, John Christodoulou, Sara Linse, Anders Malmendal
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 6, p 5191 (2023)
Amyloid fibrils may adopt different morphologies depending on the solution conditions and the protein sequence. Here, we show that two chemically identical but morphologically distinct α-synuclein fibrils can form under identical conditions. This wa
Externí odkaz:
https://doaj.org/article/46e73693990b46e1a3a94c4afed3f98c
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:
Janina Sprenger, Anda Trifan, Neal Patel, Ashley Vanderbeck, Jenny Bredfelt, Emad Tajkhorshid, Roger Rowlett, Leila Lo Leggio, Karin S. Åkerfeldt, Sara Linse
Publikováno v:
Current Research in Structural Biology, Vol 3, Iss , Pp 121-132 (2021)
Calmodulin (CaM) is a ubiquitous Ca2+ sensing protein that binds to and modulates numerous target proteins and enzymes during cellular signaling processes. A large number of CaM-target complexes have been identified and structurally characterized, re
Externí odkaz:
https://doaj.org/article/ca9bbe845bb241dc86a94af47d5c09fb
Autor:
Roxine Staats, Thomas C. T. Michaels, Patrick Flagmeier, Sean Chia, Robert I. Horne, Johnny Habchi, Sara Linse, Tuomas P. J. Knowles, Christopher M. Dobson, Michele Vendruscolo
Publikováno v:
Communications Chemistry, Vol 3, Iss 1, Pp 1-9 (2020)
Promising treatments for neurogenerative disorders may involve targeting kinetic intermediates, including α-synuclein oligomers. Here a kinetic method for quantifying oligomer populations is used to screen small molecule inhibitors of oligomerisatio
Externí odkaz:
https://doaj.org/article/25cc20ef6fa54796a866e8e34065ca87
Publikováno v:
QRB Discovery, Vol 3 (2022)
α-Synuclein is a small neuronal protein that reversibly associates with lipid membranes. The membrane interactions are believed to be central to the healthy function of this protein involved in synaptic plasticity and neurotransmitter release. α-Sy
Externí odkaz:
https://doaj.org/article/e158eb16f848486c8328f53eac7c2e9f