Zobrazeno 1 - 10
of 86
pro vyhledávání: '"Whiten, Daniel R."'
Autor:
Whiten, Daniel R., Cox, Dezerae, Horrocks, Mathew H., Taylor, Christopher G., De, Suman, Flagmeier, Patrick, Tosatto, Laura, Kumita, Janet R., Ecroyd, Heath, Dobson, Christopher M., Klenerman, David, Wilson, Mark R.
Publikováno v:
In Cell Reports 19 June 2018 23(12):3492-3500
PTEN-induced kinase 1 (PINK1) impacts cell health and human pathology through diverse pathways. The strict processing of full-length PINK1 on the outer mitochondrial membrane populates a cytoplasmic pool of cleaved PINK1 (cPINK1) that is constitutive
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::182e8af09223c4196a450ec357d1394e
Autor:
Konč, Juraj, Brown, Libby, Whiten, Daniel R, Zuo, Yukun, Ravn, Peter, Klenerman, David, Bernardes, Gonçalo JL
Many bioconjugation strategies for DNA oligonucleotides and antibodies suffer limitations, such as site-specificity, stoichiometry and hydrolytic instability of the conjugates, which makes them unsuitable for biological applications. Here, we report
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b94fcac259f85c0bd69562a8d440a0f8
Akademický článek
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Akademický článek
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Akademický článek
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Autor:
Scheidt, Tom, Łapińska, Urszula, Kumita, Janet R, Whiten, Daniel R, Klenerman, David, Wilson, Mark R, Cohen, Samuel IA, Linse, Sara, Vendruscolo, Michele, Dobson, Christopher M, Knowles, Tuomas PJ, Arosio, Paolo
The aggregates of the Aβ peptide associated with Alzheimer's disease are able to both grow in size as well as generate, through secondary nucleation, new small oligomeric species, that are major cytotoxins associated with neuronal death. Despite the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c634b190ef6f0bc0d2c3ae4e6be9fb8
Autor:
Ludtmann, Marthe HR, Angelova, Plamena R, Horrocks, Mathew H, Choi, Minee L, Rodrigues, Margarida, Baev, Artyom Y, Berezhnov, Alexey V, Yao, Zhi, Little, Daniel, Banushi, Blerida, Al-Menhali, Afnan Saleh, Ranasinghe, Rohan T, Whiten, Daniel R, Yapom, Ratsuda, Dolt, Karamjit Singh, Devine, Michael J, Gissen, Paul, Kunath, Tilo, Jaganjac, Morana, Pavlov, Evgeny V, Klenerman, David, Abramov, Andrey Y, Gandhi, Sonia
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-16 (2018)
Ludtmann, M HR, Angelova, P R, Horrocks, M H, Choi, M, Rodrigues, M, Baev, A Y, Berezhnov, A V, Yao, Z, Little, D, Banushi, B, Al-Menhali, A S, Ranasinghe, R T, Whiten, D R, Yapom, R, Singh Dolt, K, Devine, M J, Gissen, P, Kunath, T, Jaganjac, M, Pavlov, E V, Klenerman, D, Abramov, A Y & Gandhi, S 2018, ' α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease ', Nature Communications, vol. 9, 2293 . https://doi.org/10.1038/s41467-018-04422-2
Nature Communications
Ludtmann, M HR, Angelova, P R, Horrocks, M H, Choi, M, Rodrigues, M, Baev, A Y, Berezhnov, A V, Yao, Z, Little, D, Banushi, B, Al-Menhali, A S, Ranasinghe, R T, Whiten, D R, Yapom, R, Singh Dolt, K, Devine, M J, Gissen, P, Kunath, T, Jaganjac, M, Pavlov, E V, Klenerman, D, Abramov, A Y & Gandhi, S 2018, ' α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease ', Nature Communications, vol. 9, 2293 . https://doi.org/10.1038/s41467-018-04422-2
Nature Communications
Protein aggregation causes α-synuclein to switch from its physiological role to a pathological toxic gain of function. Under physiological conditions, monomeric α-synuclein improves ATP synthase efficiency. Here, we report that aggregation of monom
Autor:
Gregory, Jenna M.1,2, Whiten, Daniel R.3, Brown, Rebecca A.4, Barros, Teresa P.3, Kumita, Janet R.3, Yerbury, Justin J.4, Satapathy, Sandeep4, McDade, Karina1, Smith, Colin1, Luheshi, Leila M.3, Dobson, Christopher M.3 cmd44@cam.ac.uk, Wilson, Mark R.4 mrw@uow.edu.au
Publikováno v:
Acta Neuropathologica Communications. 11/7/2017, Vol. 5, p1-16. 16p.
Publikováno v:
Essays in Biochemistry; Dec2021, Vol. 65 Issue 7, p913-923, 11p