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of 14
pro vyhledávání: '"Michaels, Thomas Ct"'
The formation and proliferation of protein aggregates play a central role in a number of devastating neuro-degenerative diseases. Many experimental studies indicate that the ability of existing aggregates to replicate is a key property in generating
Externí odkaz:
http://arxiv.org/abs/2008.09699
Autor:
Toprakcioglu, Zenon, Kamada, Ayaka, Michaels, Thomas CT, Xie, Mengqi, Krausser, Johannes, Wei, Jiapeng, Saric, Andela, Vendruscolo, Michele, Knowles, Tuomas PJ
Primary nucleation is the fundamental event that initiates the conversion of proteins from their normal physiological forms into pathological amyloid aggregates associated with the onset and development of disorders including systemic amyloidosis, as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb921c8bb121cc32450c2765f3ee4723
https://doi.org/10.26434/chemrxiv-2022-tjrtf
https://doi.org/10.26434/chemrxiv-2022-tjrtf
Funder: Frances and Augustus Newman Foundation
Funder: Laboratory for Molecular Cell Biology, University College London
Funder: Biotechnology and Biological Sciences Research Council
A self-consistent analytical solution for binodal co
Funder: Laboratory for Molecular Cell Biology, University College London
Funder: Biotechnology and Biological Sciences Research Council
A self-consistent analytical solution for binodal co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3af7adc68f28dd47a4d86f7d0a5fcd78
https://www.repository.cam.ac.uk/handle/1810/341128
https://www.repository.cam.ac.uk/handle/1810/341128
Publikováno v:
eLife
eLife, Vol 9 (2020)
eLife, Vol 9 (2020)
During dynamic instability, self-assembling microtubules (MTs) stochastically alternate between phases of growth and shrinkage. This process is driven by the presence of two distinct states of MT subunits, GTP- and GDP-bound tubulin dimers, that have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecb246506c67c00f542eda3283253f3e
https://www.repository.cam.ac.uk/handle/1810/307360
https://www.repository.cam.ac.uk/handle/1810/307360
We use perturbative renormalization group theory to study the kinetics of protein aggregation phenomena in a unified manner across multiple timescales. Using this approach, we find that, irrespective of the specific molecular details or experimental
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93a5b8b483c78726790ceb4d4f1c0ed5
Autor:
Wright, Maya A, Aprile, Francesco A, Bellaiche, Mathias MJ, Michaels, Thomas CT, Müller, Thomas, Arosio, Paolo, Vendruscolo, Michele, Dobson, Christopher M, Knowles, Tuomas PJ
Publikováno v:
Biochemistry
Many molecular chaperones exist as oligomeric complexes in their functional states, yet the physical determinants underlying such self-assembly behavior, as well as the role of oligomerization in the activity of molecular chaperones in inhibiting pro
Autor:
Andreasen, Maria, Meisl, Georg, Taylor, Jonathan D, Michaels, Thomas CT, Levin, Aviad, Otzen, Daniel E, Chapman, Matthew R, Dobson, Christopher M, Matthews, Steve J, Knowles, Tuomas PJ
Publikováno v:
Andreasen, M, Meisl, G, Taylor, J D, Michaels, T C T, Levin, A, Otzen, D E, Chapman, M R, Dobson, C M, Matthews, S J & Knowles, T P J 2019, ' Physical Determinants of Amyloid Assembly in Biofilm Formation ', mBio, vol. 10, no. 1, e02279-18 . https://doi.org/10.1128/mBio.02279-18
mBio, Vol 10, Iss 1 (2019)
mBio, Vol 10, Iss 1, p e02279-18 (2019)
mBio, Vol 10, Iss 1 (2019)
mBio, Vol 10, Iss 1, p e02279-18 (2019)
A wide range of bacterial pathogens have been shown to form biofilms, which significantly increase their resistance to environmental stresses, such as antibiotics, and are thus of central importance in the context of bacterial diseases. One of the ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4bfeebe7ba5776cbc5adca699605a71
https://pure.au.dk/portal/da/publications/physical-determinants-of-amyloid-assembly-in-biofilm-formation(91bf63ce-237e-45be-9064-f7d057f0405c).html
https://pure.au.dk/portal/da/publications/physical-determinants-of-amyloid-assembly-in-biofilm-formation(91bf63ce-237e-45be-9064-f7d057f0405c).html
Autor:
Šarić, Anđela, Buell, Alexander K, Meisl, Georg, Michaels, Thomas CT, Dobson, Christopher M, Linse, Sara, Knowles, Tuomas PJ, Frenkel, Daan
The ability of biological molecules to replicate themselves, achieved with the aid of a complex cellular machinery, is the foundation of life. However, a range of aberrant processes involve the self-replication of pathological protein structures with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______109::e4d7c4943586c59ccfa549f950bc6a12
https://www.repository.cam.ac.uk/handle/1810/255775
https://www.repository.cam.ac.uk/handle/1810/255775
Autor:
Iljina, Marija, Dear, Alexander J, Garcia, Gonzalo A, De, Suman, Tosatto, Laura, Flagmeier, Patrick, Whiten, Daniel R, Michaels, Thomas CT, Frenkel, Daan, Dobson, Christopher M, Knowles, Tuomas PJ, Klenerman, David
Small oligomers of the protein α-synuclein (αS) are highly cytotoxic species associated with Parkinson's disease (PD). In addition, αS can form co-aggregates with its mutational variants and with other proteins such as amyloid-β (Aβ) and tau, wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2708ae4273c1b536cf23fb375aaa9a33
Autor:
Limbocker, Ryan, Chia, Sean, Ruggeri, Francesco S, Perni, Michele, Cascella, Roberta, Heller, Gabriella T, Meisl, Georg, Mannini, Benedetta, Habchi, Johnny, Michaels, Thomas CT, Challa, Pavan K, Ahn, Minkoo, Casford, Samuel T, Fernando, Nilumi, Xu, Catherine K, Kloss, Nina D, Cohen, Samuel IA, Kumita, Janet R, Cecchi, Cristina, Zasloff, Michael, Linse, Sara, Knowles, Tuomas PJ, Chiti, Fabrizio, Vendruscolo, Michele, Dobson, Christopher M
Transient oligomeric species formed during the aggregation process of the 42-residue form of the amyloid-β peptide (Aβ42) are key pathogenic agents in Alzheimer's disease (AD). To investigate the relationship between Aβ42 aggregation and its cytot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::40c212943137fc6fad7330806e28254f