Zobrazeno 1 - 10
of 290
pro vyhledávání: '"Knowles TPJ"'
Autor:
Rodrigues, M, Bhattacharjee, P, Brinkmalm, A, Do, DT, Pearson, CM, De, S, Ponjavic, A, Varela, JA, Kulenkampff, K, Baudrexel, I, Emin, D, Ruggeri, FS, Lee, JE, Carr, AR, Knowles, TPJ, Zetterberg, H, Snaddon, TN, Gandhi, S, Lee, SF, Klenerman, D
Publikováno v:
Nature Chemistry, 14(9), 1045-1053
Nature Chemistry 14 (2022) 9
Nature Chemistry 14 (2022) 9
Funding: This work was supported by the National Institute of Health Research University College London Hospitals Biomedical Research Centre. SG is an MRC Senior Clinical Fellow (MR/T008199/1). H.Z. is a Wallenberg Scholar supported by grants from th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44466f17b9de5a1796608ad8f28a5775
https://research.wur.nl/en/publications/structure-specific-amyloid-precipitation-in-biofluids
https://research.wur.nl/en/publications/structure-specific-amyloid-precipitation-in-biofluids
Autor:
Scheidt, T, Carozza, JA, Kolbe, CC, Aprile, FA, Tkachenko, O, Bellaiche, MMJ, Meisl, G, Peter, QAE, Herling, TW, Ness, S, Castellana-Cruz, M, Benesch, JLP, Vendruscolo, M, Dobson, CM, Arosio, P, Knowles, TPJ
Molecular chaperones are key components of the cellular proteostasis network whose role includes the suppression of the formation and proliferation of pathogenic aggregates associated with neurodegenerative diseases. The molecular principles that all
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______1032::77ff3a64c145a5558da41bc6427d831a
http://hdl.handle.net/10044/1/92310
http://hdl.handle.net/10044/1/92310
Autor:
Kosmoliaptsis, Catherine K. Xu, Georg Meisl, Tom Scheidt, Michele T.M. Hu, Matthias Schneider, Priddey Aj, Knowles Tpj, Christopher M. Dobson, Devenish Sra
The detection and characterisation of antibodies in human blood is a key for clinical diagnostics and risk assessment for autoimmunity, infectious diseases and transplanta-tion. Antibody titre derived from immunoassays is a commonly used measure for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ea3179217026896c48db6e87bba4362f
https://doi.org/10.1101/2020.09.14.296442
https://doi.org/10.1101/2020.09.14.296442
Autor:
Diana Sobota, Hernandez Ainsa S, Javier García-Nafría, Kevin N. Baumann, Luca Piantanida, Knowles Tpj, Kislon Voïtchovsky
The self-assembly of the protein clathrin on biological membranes facilitates essential processes of endocytosis in biological systems and has provided a source of inspiration for materials design by the highly ordered structural appearance. By mimic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77bb42f9d35d07bab576df51b21ba62d
https://doi.org/10.26434/chemrxiv.8859017.v1
https://doi.org/10.26434/chemrxiv.8859017.v1
Autor:
St George-Hyslop, PH, Qamar, S, Wang, Guozhen, Randle, SJ, Ruggeri, Francesco Simone, Varela, Juan, Kaminski, CF, Kaminski, GS, Vendruscolo, M, Knowles, TPJ, Klenerman, D, Holt, CE, Lin, Q, Meadows, William
Reversible phase separation, which underpins the role of FUS in ribonucleoprotein granules and other membrane-free organelles, is in part driven by the intrinsically disordered low complexity (LC) domain of FUS. Here, we report that cooperative catio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e149434a94dcae6a5baaf8fc21f00548
Autor:
Perni, M, Flagmeier, P, Limbocker, R, Cascella, R, Aprile, Fa, Galvagnion, C, Heller, Gt, Meisl, G, Chen, Sw, Kumita, Jr, Challa, Pk, Kirkegaard, Jb, Cohen, Sia, Mannini, B, Barbut, D, Nollen, Eaa, Cecchi, C, Cremades, N, Knowles, Tpj, Chiti, F, Zasloff, M, Vendruscolo, M, Dobson, Cm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______310::643934268520e9e7d9e32fb2a8239319
http://hdl.handle.net/2158/1132660
http://hdl.handle.net/2158/1132660
Parkinson’s disease (PD) is characterized by proteinaceous aggregates named Lewy Bodies and Lewy Neurites containing $\alpha$-synuclein fibrils. The underlying aggregation mechanism of this protein is dominated by a secondary process at mildly acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3318417307ef9cdf4d115f43dda19ad
https://www.repository.cam.ac.uk/handle/1810/263245
https://www.repository.cam.ac.uk/handle/1810/263245
Autor:
Taylor, JD, Hawthorne, WJ, Lo, J, Dear, A, Jain, N, Meisl, G, Andreasen, M, Fletcher, C, Koch, M, Darvill, N, Scull, N, Escalera-Maurer, A, Sefer, L, Wenman, R, Lambert, S, Jean, J, Xu, Y, Turner, B, Kazarian, SG, Chapman, MR, Bubeck, D, De Simone, A, Knowles, TPJ, Matthews, SJ
Publikováno v:
Scientific Reports
Polypeptide aggregation into amyloid is linked with several debilitating human diseases. Despite the inherent risk of aggregation-induced cytotoxicity, bacteria control the export of amyloid-prone subunits and assemble adhesive amyloid fibres during
We have explored amyloid formation using poly(amino acid) model systems in which differences in peptide secondary structure and hydrophobicity can be introduced in a controlled manner. We show that an environmentally sensitive fluorescent dye, dapoxy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d9d7571a6bbc622c0e4738dbcdf7105
https://www.repository.cam.ac.uk/handle/1810/267219
https://www.repository.cam.ac.uk/handle/1810/267219
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