Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Franziska Kundel"'
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
Autor:
Suman De, David C. Wirthensohn, Patrick Flagmeier, Craig Hughes, Francesco A. Aprile, Francesco S. Ruggeri, Daniel R. Whiten, Derya Emin, Zengjie Xia, Juan A. Varela, Pietro Sormanni, Franziska Kundel, Tuomas P. J. Knowles, Christopher M. Dobson, Clare Bryant, Michele Vendruscolo, David Klenerman
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
Amyloid beta (Aβ42) peptides form heterogeneous mixtures of aggregates, which are closely linked to Alzheimer’s disease. This study shows how different types of Aβ42 aggregates are associated with distinct mechanisms of toxicity
Externí odkaz:
https://doaj.org/article/dda94a3ed6064b0ba41892597f9160ae
Publikováno v:
Cell Reports, Vol 26, Iss 8, Pp 2140-2149.e3 (2019)
Summary: Filamentous aggregates (fibrils) are regarded as the final stage in the assembly of amyloidogenic proteins and are formed in many neurodegenerative diseases. Accumulation of aggregates occurs as a result of an imbalance between their formati
Externí odkaz:
https://doaj.org/article/587625afb80741749fe12ceb1fbef706
Publikováno v:
Cell Reports, Vol 26, Iss 8, Pp 2140-2149.e3 (2019)
Cell Reports
Cell Reports
Summary Filamentous aggregates (fibrils) are regarded as the final stage in the assembly of amyloidogenic proteins and are formed in many neurodegenerative diseases. Accumulation of aggregates occurs as a result of an imbalance between their formatio
Autor:
Giuseppe Federico Amodeo, David Klenerman, Noemí Esteras, Franziska Kundel, Andrey Y. Abramov, Evgeny Pavlov
Most neurodegenerative disorders are associated with aggregation and accumulation of misfolded proteins. One of these proteins, tau, is involved in a number of pathologies including Alzheimer's disease and frontotemporal dementia. Aggregation and pho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d9ee54aed8c7809200a92fadd01c102
https://www.repository.cam.ac.uk/handle/1810/305249
https://www.repository.cam.ac.uk/handle/1810/305249
Autor:
Tuomas P. J. Knowles, David Klenerman, Andrey Y. Abramov, Thomas C. T. Michaels, William A. McEwan, Liu Hong, Noemí Esteras, Michel Goedert, Franziska Kundel, Georg Meisl, Benjamin Falcon
Publikováno v:
ACS Chemical Neuroscience (2018)
ACS Chemical Neuroscience
ACS Chemical Neuroscience
The ordered assembly of amyloidogenic proteins causes a wide spectrum of common neurodegenerative diseases, including Alzheimer’s and Parkinson’s diseases. These diseases share common features with prion diseases, in which misfolded proteins can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98338a2f46bfb068818b827a7851c18d
Autor:
Tuomas P. J. Knowles, Franziska Kundel, Georg Meisl, David Klenerman, Michel Goedert, Liu Hong, William A. McEwan, Benjamin Falcon
Publikováno v:
Alzheimer's & Dementia. 14
Autor:
Magnus, Kjaergaard, Alexander J, Dear, Franziska, Kundel, Seema, Qamar, Georg, Meisl, Tuomas P J, Knowles, David, Klenerman
Publikováno v:
ACS Chemical Neuroscience
The molecular mechanism of protein aggregation is of both fundamental and clinical importance as amyloid aggregates are linked to a number of neurodegenerative disorders. Such protein aggregates include macroscopic insoluble fibrils as well as small
Autor:
Daniel R, Whiten, Yukun, Zuo, Laura, Calo, Minee-Liane, Choi, Suman, De, Patrick, Flagmeier, David C, Wirthensohn, Franziska, Kundel, Rohan T, Ranasinghe, Santiago E, Sanchez, Dilan, Athauda, Steven F, Lee, Christopher M, Dobson, Sonia, Gandhi, Maria-Grazia, Spillantini, David, Klenerman, Mathew H, Horrocks
Publikováno v:
Chembiochem
The aberrant misfolding and subsequent conversion of monomeric protein into amyloid aggregates characterises many neurodegenerative disorders, including Parkinson's and Alzheimer's diseases. These aggregates are highly heterogeneous in structure, gen
Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity
Autor:
Magnus Kjaergaard, Franziska Kundel, David Klenerman, Sophie E. Jackson, Mathew H. Horrocks, Suman De, Christopher M. Dobson, Sarah L. Shammas, Patrick Flagmeier
Publikováno v:
Kundel, F, De, S, Flagmeier, P, Horrocks, M H, Kjaergaard, M, Shammas, S L, Jackson, S E, Dobson, C M & Klenerman, D 2018, ' Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity ', ACS chemical biology, vol. 13, no. 3, pp. 636-646 . https://doi.org/10.1021/acschembio.7b01039
ACS Chemical Biology
Kundel, F, Mukhopadhyay, S, Flagmeier, P, Horrocks, M, Kjaergaard, M, Shammas, S L, Jackson, S E, Dobson, C M & Klenerman, D 2018, ' Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity ', Acs chemical biology . https://doi.org/10.1021/acschembio.7b01039
ACS Chemical Biology
Kundel, F, Mukhopadhyay, S, Flagmeier, P, Horrocks, M, Kjaergaard, M, Shammas, S L, Jackson, S E, Dobson, C M & Klenerman, D 2018, ' Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity ', Acs chemical biology . https://doi.org/10.1021/acschembio.7b01039
As a key player of the protein quality control network of the cell, the molecular chaperone Hsp70 inhibits the aggregation of the amyloid protein tau. To date, the mechanism of this inhibition and the tau species targeted by Hsp70 remainunknown. This
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41e024956d05dcf96fdfabe3b28ebae2
https://pure.au.dk/portal/da/publications/hsp70-inhibits-the-nucleation-and-elongation-of-tau-and-sequesters-tau-aggregates-with-high-affinity(e8aaade5-fbc9-4be7-b5cc-4414ad578e41).html
https://pure.au.dk/portal/da/publications/hsp70-inhibits-the-nucleation-and-elongation-of-tau-and-sequesters-tau-aggregates-with-high-affinity(e8aaade5-fbc9-4be7-b5cc-4414ad578e41).html
Autor:
David Klenerman, Daniel R. Whiten, Franziska Kundel, David C. Wirthensohn, Laura Tosatto, Mathew H. Horrocks
Publikováno v:
Kundel, F, Tosatto, L, Whiten, D R, Wirthensohn, D C, Horrocks, M H & Klenerman, D 2018, ' Shedding light on aberrant interactions : A review of modern tools for studying protein aggregates ', Febs Journal . https://doi.org/10.1111/febs.14409
The link between protein aggregation and neurodegenerative disease is well established. However, given the heterogeneity of species formed during the aggregation process, it is difficult to delineate details of the molecular events involved in genera