Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Signe Andrea Frank"'
Autor:
Arpit Gupta, Priyanka Singh, Arpit Mehrotra, Ankur Gautam, K. Srividya, Rajlaxmi Panigrahi, Shubham Vashishtha, Jasdeep Singh, Gagandeep Jaiswal, Krishna Upadhayay, Signe Andrea Frank, Janni Nielsen, Samir Kumar Nath, Neeraj Khatri, Daniel E. Otzen, G.P.S. Raghava, Anil Koul, Bishwajit Kundu, Ashutosh Kumar, Aamir Nazir, Deepak Sharma
Parkinson’s disease (PD) is the second most common neurodegenerative disease. The presence of lewy bodies, primarily consisting of α-synuclein (α-syn) aggregates is one of the common features seen in the substantia nigra region of the brain in PD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6c25288aed82db475c0949ed4a6dd3d6
https://doi.org/10.1101/2022.06.24.497475
https://doi.org/10.1101/2022.06.24.497475
Autor:
Mitra Pirhaghi, Signe Andrea Frank, Parvez Alam, Janni Nielsen, Vita Sereikaite, Arpit Gupta, Kristian Strømgaard, Maria Andreasen, Deepak Sharma, Ali Akbar Saboury, Daniel Erik Otzen
Publikováno v:
Pirhaghi, M, Frank, S A, Alam, P, Nielsen, J, Sereikaite, V, Gupta, A, Strømgaard, K, Andreasen, M, Sharma, D, Saboury, A A & Otzen, D E 2022, ' A penetratin-derived peptide reduces the membrane permeabilization and cell toxicity of α-synuclein oligomers ', Journal of Biological Chemistry, vol. 298, no. 12, 102688 . https://doi.org/10.1016/j.jbc.2022.102688
Parkinson's disease is a neurodegenerative movement disorder associated with the intracellular aggregation of α-synuclein (α-syn). Cytotoxicity is mainly associated with the oligomeric species (αSOs) formed at early stages in α-syn aggregation. C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c0ecfe4baf81651af7875314a2fba7a
https://doi.org/10.1016/j.jbc.2022.102688
https://doi.org/10.1016/j.jbc.2022.102688
Autor:
Thorbjørn V Sønderby, Signe Andrea Frank, Helena Ø. Rasmussen, Jan Skov Pedersen, Daniel E. Otzen
Publikováno v:
Sønderby, T V, Rasmussen, H Ø, Frank, S A, Skov Pedersen, J & Otzen, D E 2022, ' Folding steps in the fibrillation of functional amyloid : denaturant sensitivity reveals common features in nucleation and elongation ', Journal of Molecular Biology, vol. 434, no. 2, 167337 . https://doi.org/10.1016/j.jmb.2021.167337
Functional bacterial amyloids (FuBA) are intrinsically disordered proteins (IDPs) which rapidly and efficiently aggregate, forming extremely stable fibrils. The conversion from IDP to amyloid is evolutionarily optimized and likely couples folding to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70d1bdbf49e838989d571f1163980e3c
https://pubmed.ncbi.nlm.nih.gov/34748745
https://pubmed.ncbi.nlm.nih.gov/34748745
Autor:
Thorbjørn Vincent Sønderby, Signe Andrea Frank, Daniel E. Otzen, Line Friis Bakmann Christensen, Jan Stanislaw Nowak
Publikováno v:
The journal of Biological Chemistry
J Biol Chem
Christensen, L F B, Nowak, J S, Sønderby, T V, Frank, S A & Otzen, D E 2020, ' Quantitating denaturation by formic acid : Imperfect repeats are essential to the stability of the functional amyloid protein FapC ', The Journal of biological chemistry, vol. 295, no. 37, pp. 13031–13046 . https://doi.org/10.1074/jbc.RA120.013396
J Biol Chem
Christensen, L F B, Nowak, J S, Sønderby, T V, Frank, S A & Otzen, D E 2020, ' Quantitating denaturation by formic acid : Imperfect repeats are essential to the stability of the functional amyloid protein FapC ', The Journal of biological chemistry, vol. 295, no. 37, pp. 13031–13046 . https://doi.org/10.1074/jbc.RA120.013396
Bacterial functional amyloids are evolutionarily optimized to aggregate to help them fulfil their biological functions,e.g.to provide mechanical stability to biofilm. Amyloid is formed inPseudomonassp. by the protein FapC which contains 3 imperfect r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5d20383db4daeb28d88fd6d5b71ee3d
Publikováno v:
Frislev, H S, Jakobsen, S C L, Frank, S A & Otzen, D E 2018, ' Dynamic content exchange between liprotides ', Biophysical Chemistry, vol. 233, pp. 13-18 . https://doi.org/10.1016/j.bpc.2017.11.006
Liprotides are complexes composed of partially denatured proteins and fatty acids in which the fatty acids form a micelle-like core surrounded by a shell of proteins. Liprotides, composed of α-lactalbumin (aLA) and oleic acid (OA), are similar in co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c75b594e3028d72a7c5436a5784dc2cf
https://doi.org/10.1016/j.bpc.2017.11.006
https://doi.org/10.1016/j.bpc.2017.11.006
Autor:
Jan J. Enghild, Arun Kumar Somavarapu, Mihaela M. Apetri, Carsten Scavenius, Femke van Diggelen, Janni Nielsen, Daniel E. Otzen, Armand W.J.W. Tepper, Signe Andrea Frank
Publikováno v:
van Diggelen, F, Frank, S A, Somavarapu, A K, Scavenius, C, Apetri, M M, Nielsen, J, Tepper, A W J W, Enghild, J J & Otzen, D E 2020, ' The interactome of stabilized α-synuclein oligomers and neuronal proteins ', The FEBS Journal, vol. 287, no. 10, pp. 2037-2054 . https://doi.org/10.1111/febs.15124
While it is generally accepted that α-synuclein oligomers (αSOs) play an important role in neurodegeneration in Parkinson's disease, the basis for their cytotoxicity remains unclear. We have previously shown that docosahexaenoic acid (DHA) stabiliz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63d05a26ab7dd1a49de771b556d0f0f6
https://pubmed.ncbi.nlm.nih.gov/31686426
https://pubmed.ncbi.nlm.nih.gov/31686426