Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Alexia F Kalogeropulou"'
Autor:
Alexia F Kalogeropulou, Elena Purlyte, Francesca Tonelli, Sven M Lange, Melanie Wightman, Alan R Prescott, Shalini Padmanabhan, Esther Sammler, Dario R Alessi
Publikováno v:
Biochemical Journal. 479:1759-1783
Mutations enhancing the kinase activity of LRRK2 cause Parkinson’s disease (PD) and therapies that reduce LRRK2 kinase activity are being tested in clinical trials. Numerous rare variants of unknown clinical significance have been reported, but how
Autor:
Xingui Liu, Alexia F. Kalogeropulou, Sofia Domingos, Nikolai Makukhin, Raja S. Nirujogi, Francois Singh, Natalia Shpiro, Anton Saalfrank, Esther Sammler, Ian G. Ganley, Rui Moreira, Dario R. Alessi, Alessio Ciulli
Publikováno v:
Journal of the American Chemical Society. 144:16930-16952
Leucine-rich repeat kinase 2 (LRRK2) is one of the most promising targets for Parkinson's disease. LRRK2-targeting strategies have primarily focused on type 1 kinase inhibitors, which, however, have limitations as the inhibited protein can interfere
Autor:
Nicole K. Polinski, Jordana B. Freemantle, Pawel Lis, Alexia F. Kalogeropulou, Dario R. Alessi, Edmundo G Vides
Publikováno v:
Biochemical Journal
Mutations that enhance LRRK2 protein kinase activity cause inherited Parkinson's disease. LRRK2 phosphorylates a group of Rab GTPase proteins, including Rab10 and Rab12, within the effector-binding switch-II motif. Previous work has indicated that th
Autor:
Edmundo G Vides, Alexia F. Kalogeropulou, Pawel Lis, Jordana B. Freemantle, Dario R. Alessi, Nicole K. Polinski
Mutations that enhance LRRK2 protein kinase activity cause inherited Parkinson’s disease. LRRK2 phosphorylates a group of Rab GTPase proteins, including Rab10 and Rab12, within the effector-binding switch-II motif. Previous work has indicated that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1497f283a76f132b8a55b1983a2acdd
https://doi.org/10.1101/2020.06.08.139675
https://doi.org/10.1101/2020.06.08.139675
P62/SQSTM1 is a novel leucine-rich repeat kinase 2 (LRRK2) substrate that enhances neuronal toxicity
Autor:
Marc Bolliger, Anna Memou, Hardy J. Rideout, Alexia F. Kalogeropulou, William H. Wilson, Jing Zhao, R. Jeremy Nichols, Tyler P. Molitor, Shreya Narasimha
Publikováno v:
Biochemical Journal. 475:1271-1293
Autosomal-dominant, missense mutations in the leucine-rich repeat protein kinase 2 (LRRK2) gene are the most common genetic predisposition to develop Parkinson's disease (PD). LRRK2 kinase activity is increased in several pathogenic mutations (N1437H