Zobrazeno 1 - 10
of 81
pro vyhledávání: '"Axel Knebel"'
Autor:
Francisco Bustos, Anna Segarra-Fas, Viduth K. Chaugule, Lennart Brandenburg, Emma Branigan, Rachel Toth, Thomas Macartney, Axel Knebel, Ronald T. Hay, Helen Walden, Greg M. Findlay
Publikováno v:
Cell Reports, Vol 23, Iss 6, Pp 1599-1611 (2018)
Summary: X-linked intellectual disability (XLID) is a heterogeneous syndrome affecting mainly males. Human genetics has identified >100 XLID genes, although the molecular and developmental mechanisms underpinning this disorder remain unclear. Here, w
Externí odkaz:
https://doaj.org/article/a7ffd6fa9df048268b625e400ceb92e8
Autor:
Kerryn Berndsen, Pawel Lis, Wondwossen M Yeshaw, Paulina S Wawro, Raja S Nirujogi, Melanie Wightman, Thomas Macartney, Mark Dorward, Axel Knebel, Francesca Tonelli, Suzanne R Pfeffer, Dario R Alessi
Publikováno v:
eLife, Vol 8 (2019)
Mutations that activate LRRK2 protein kinase cause Parkinson’s disease. LRRK2 phosphorylates a subset of Rab GTPases within their Switch-II motif controlling interaction with effectors. An siRNA screen of all human protein phosphatases revealed tha
Externí odkaz:
https://doaj.org/article/6a5369c02adb4cf08a138e9a247156ed
Autor:
Thomas G. McWilliams, Erica Barini, Risto Pohjolan-Pirhonen, Simon P. Brooks, François Singh, Sophie Burel, Kristin Balk, Atul Kumar, Lambert Montava-Garriga, Alan R. Prescott, Sidi Mohamed Hassoun, François Mouton-Liger, Graeme Ball, Rachel Hills, Axel Knebel, Ayse Ulusoy, Donato A. Di Monte, Jevgenia Tamjar, Odetta Antico, Kyle Fears, Laura Smith, Riccardo Brambilla, Eino Palin, Miko Valori, Johanna Eerola-Rautio, Pentti Tienari, Olga Corti, Stephen B. Dunnett, Ian G. Ganley, Anu Suomalainen, Miratul M. K. Muqit
Publikováno v:
Open Biology, Vol 8, Iss 11 (2018)
Mutations in PINK1 and Parkin result in autosomal recessive Parkinson's disease (PD). Cell culture and in vitro studies have elaborated the PINK1-dependent regulation of Parkin and defined how this dyad orchestrates the elimination of damaged mitocho
Externí odkaz:
https://doaj.org/article/1d714fdf77f7434a8620cf73ff0a6aee
Autor:
Nicolas Huguenin-Dezot, Virginia De Cesare, Julien Peltier, Axel Knebel, Yosua Adi Kristaryianto, Daniel T. Rogerson, Yogesh Kulathu, Matthias Trost, Jason W. Chin
Publikováno v:
Cell Reports, Vol 16, Iss 4, Pp 1180-1193 (2016)
Ubiquitin is post-translationally modified by phosphorylation at several sites, but the consequences of these modifications are largely unknown. Here, we synthesize multi-milligram quantities of ubiquitin phosphorylated at serine 20, serine 57, and s
Externí odkaz:
https://doaj.org/article/b5b139d187af49c2bc7b15568d7770ec
Autor:
Chandana Kondapalli, Agne Kazlauskaite, Ning Zhang, Helen I. Woodroof, David G. Campbell, Robert Gourlay, Lynn Burchell, Helen Walden, Thomas J. Macartney, Maria Deak, Axel Knebel, Dario R. Alessi, Miratul M. K. Muqit
Publikováno v:
Open Biology, Vol 2, Iss 5 (2012)
Summary Missense mutations in PTEN-induced kinase 1 (PINK1) cause autosomal-recessive inherited Parkinson's disease (PD). We have exploited our recent discovery that recombinant insect PINK1 is catalytically active to test whether PINK1 directly phos
Externí odkaz:
https://doaj.org/article/a7ccab88220e49e2ad360b217db36be0
Autor:
Andrew D. Waddell, Hina Ojha, Shalini Agarwal, Christopher J. Clarke, Ana Terriente-Felix, Houjiang Zhou, Poonam Kakade, Axel Knebel, Andrew M. Shaw, Robert Gourlay, Joby Varghese, Renata F. Soares, Rachel Toth, Thomas Macartney, Patrick A. Eyers, Nick Morrice, Richard Bayliss, Alexander J. Whitworth, Claire E. Eyers, Miratul M. K. Muqit
Loss-of-function mutations in the human PINK1 kinase (hPINK1) are causative of early-onset Parkinson’s disease (PD). Activation of hPINK1 induces phosphorylated ubiquitin to initiate removal of damaged mitochondria by autophagy. Previously we solve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0e00472b151d1285b844ca753507a62
https://doi.org/10.1101/2023.03.31.534916
https://doi.org/10.1101/2023.03.31.534916
Autor:
Syed Arif Abdul Rehman, Elena Di Nisio, Chiara Cazzaniga, Odetta Antico, Axel Knebel, Clare Johnson, Frederic Lamoliatte, Rodolfo Negri, Miratul Muqit MK, Virginia De Cesare
E2 conjugating enzymes (E2s) play a central role in the enzymatic cascade that leads to the attachment of ubiquitin to a substrate. This process, termed ubiquitylation is fundamental for maintaining cellular homeostasis and impacts almost all cellula
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5213529c293d7dae87454baf4c9f7290
https://doi.org/10.1101/2023.03.05.531151
https://doi.org/10.1101/2023.03.05.531151
Autor:
Sven M. Lange, Matthew R. McFarland, Frederic Lamoliatte, Dominika Kwaśna, Linnan Shen, Iona Wallace, Isobel Cole, Lee A. Armstrong, Axel Knebel, Clare Johnson, Virginia De Cesare, Yogesh Kulathu
Branched ubiquitin (Ub) chains make up a significant proportion of Ub polymers in human cells and are formed when two or more sites on a single Ub molecule are modified with Ub creating bifurcated architectures. Despite their abundance, we have a poo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e35913596d7c4ef61fc79481ed7099a7
https://doi.org/10.1101/2023.01.10.523363
https://doi.org/10.1101/2023.01.10.523363
Autor:
Sven M. Lange, Syed Arif Abdul Rehman, Dmitri I. Svergun, Lee A. Armstrong, Yogesh Kulathu, Yosua Adi Kristariyanto, Axel Knebel, Tobias W. Gräwert
Publikováno v:
'Molecular Cell ', vol: 81, pages: 4176-4190 (2021)
Molecular cell 81, S1097276521006912 (1-15) (2021). doi:10.1016/j.molcel.2021.08.024
Molecular Cell
Molecular cell 81, S1097276521006912 (1-15) (2021). doi:10.1016/j.molcel.2021.08.024
Molecular Cell
Summary Of the eight distinct polyubiquitin (polyUb) linkages that can be assembled, the roles of K48-linked polyUb (K48-polyUb) are the most established, with K48-polyUb modified proteins being targeted for degradation. MINDY1 and MINDY2 are members
Autor:
Virginia De Cesare, Ryan Traynor, Axel Knebel, C. James Hastie, Paul Davies, Hilary McLauchlan, Matthias Trost, Jennifer Moran, Maria Stella Ritorto
Publikováno v:
Nature Protocols. 15:4034-4057
Deubiquitylating enzymes (DUBs) play a vital role in the ubiquitin pathway by editing or removing ubiquitin from their substrate. As breakthroughs within the ubiquitin field continue to highlight the potential of deubiquitylating enzymes as drug targ