Molecular characterisation of a novel vipar interacting protein in health and disease

Autor: Banushi, Blerida

Arthrogryposis, Renal dysfunction, and Cholestasis (ARC) syndrome is a multisystem disorder caused by mutations in genes encoding two proteins VPS33B or VIPAR, which appear to be critical regulators of cell polarity. VPS33B and VIPAR may function as

Externí odkaz: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.589679

An Ex Vivo Human Tumor Assay Shows Distinct Patterns of EGFR Trafficking in Squamous Cell Carcinoma Correlating to Therapeutic Outcomes

Autor: Joseph, Shannon R., Gaffney, Daniel, Barry, Rachael, Hu, Lingbo, Banushi, Blerida, Wells, James W., Lambie, Duncan, Strutton, Geoffrey, Porceddu, Sandro V., Burmeister, Bryan, Leggatt, Graham R., Schaider, Helmut, Dolcetti, Riccardo, Frazer, Ian H., Saunders, Nicholas A., Foote, Matthew, Soyer, H. Peter, Simpson, Fiona

Publikováno v: In Journal of Investigative Dermatology January 2019 139(1):213-223

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α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson’s disease

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

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f0b0da49f274033083306f195bd37f3
http://link.springer.com/article/10.1038/s41467-018-04422-2