Zobrazeno 1 - 10
of 128
pro vyhledávání: '"R Maitland"'
Autor:
Rachel D. Kelly, Gursimran Parmar, Laila Bayat, Matthew E. R. Maitland, Gilles A. Lajoie, David R. Edgell, Caroline Schild-Poulter
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-15 (2023)
Abstract The Ku70/80 heterodimer is a key player in non-homologous end-joining DNA repair but is involved in other cellular functions like telomere regulation and maintenance, in which Ku’s role is not fully characterized. It was previously reporte
Externí odkaz:
https://doaj.org/article/eb6a2b9fcb3446e0b036e18a1fd9df1c
Autor:
R. Harris, V. Lowers, C. Hulme, G. Burnside, A. Best, J. E. Clarkson, R. Cooke, M. Van Der Zande, R. Maitland
Publikováno v:
Trials, Vol 23, Iss 1, Pp 1-16 (2022)
Abstract Background People with disadvantaged backgrounds are less likely to visit the dentist for planned care, even though they have disproportionately poorer oral health. They are correspondingly more likely to experience dental problems and use u
Externí odkaz:
https://doaj.org/article/992aa78b533c4fc89cb48a6ab36e5268
Publikováno v:
BMC Cancer, Vol 17, Iss 1, Pp 1-16 (2017)
Abstract Background Histone deacetylase 6 (HDAC6) is a microtubule-associated deacetylase that promotes many cellular processes that lead to cell transformation and tumour development. We previously documented an interaction between Ran-Binding Prote
Externí odkaz:
https://doaj.org/article/0c7681a932594b92b0509b56b41bdf59
Publikováno v:
Open Biology, Vol 7, Iss 6 (2017)
RanBPM (Ran-binding protein M, also called RanBP9) is an evolutionarily conserved, ubiquitous protein which localizes to both nucleus and cytoplasm. RanBPM has been implicated in the regulation of a number of signalling pathways to regulate several c
Externí odkaz:
https://doaj.org/article/971f51057e2b458e9a327f2dce33e9c8
Distinct nuclear and cytoplasmic assemblies and interactomes of the mammalian CTLH E3 ligase complex
Publikováno v:
Journal of Cell Science. 135
The C-terminal to LisH (CTLH) complex is a newly discovered multi-subunit E3 ubiquitin ligase and its cellular functions are poorly characterized. Although some CTLH subunits have been found to localize in both the nucleus and cytoplasm of mammalian
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2042e9e402e696d7610c24c6eaf78ae
https://doi.org/10.1242/jcs.259638
https://doi.org/10.1242/jcs.259638
Autor:
Rachel E. Lackie, Aline S. de Miranda, Mei Peng Lim, Vladislav Novikov, Nimrod Madrer, Nadun C. Karunatilleke, Benjamin S. Rutledge, Stephanie Tullo, Anne Brickenden, Matthew E. R. Maitland, David Greenberg, Daniel Gallino, Wen Luo, Anoosha Attaran, Irina Shlaifer, Esther Del Cid Pellitero, Caroline Schild-Poulter, Thomas M. Durcan, Edward A. Fon, Martin Duennwald, Flavio H. Beraldo, M. Mallar Chakravarty, Timothy J. Bussey, Lisa M. Saksida, Hermona Soreq, Wing-Yiu Choy, Vania F. Prado, Marco A. M. Prado
Publikováno v:
Neuroscience Institute Publications
The predominantly pre-synaptic intrinsically disordered protein α-synuclein is prone to misfolding and aggregation in synucleinopathies, such as Parkinson’s disease (PD) and Dementia with Lewy bodies (DLB). Molecular chaperones play important role
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba6c8d325062fc051dc64081d7b95377
https://pubmed.ncbi.nlm.nih.gov/36121476
https://pubmed.ncbi.nlm.nih.gov/36121476
Publikováno v:
International journal of molecular sciences. 23(11)
Multi-subunit E3 ligases facilitate ubiquitin transfer by coordinating various substrate receptor subunits with a single catalytic center. Small molecules inducing targeted protein degradation have exploited such complexes, proving successful as ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec4b2613308bcd39c19c8cdf098382be
https://pubmed.ncbi.nlm.nih.gov/35682545
https://pubmed.ncbi.nlm.nih.gov/35682545
Publikováno v:
The FASEB Journal. 35
Ubiquitination is an essential post-translational modification that regulates protein stability or function. Its substrate specificity is dictated by various E3 ligases. The human C-terminal to LisH (CTLH) complex is a newly discovered multi-subunit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d4ef5d4bfb532724b6318d190301442
https://doi.org/10.1096/fj.202100664r
https://doi.org/10.1096/fj.202100664r
Autor:
Gilles A. Lajoie, Xu Wang, Christopher A. Chiasson, Gary S. Shaw, Gabriel Onea, Kathryn R. Barber, Jun Ma, Sarah E. Moor, Caroline Schild-Poulter, Matthew E. R. Maitland
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-14 (2019)
Scientific Reports
Scientific Reports
The multi-subunit C-terminal to LisH (CTLH) complex is the mammalian homologue of the yeast Gid E3 ubiquitin ligase complex. In this study, we investigated the human CTLH complex and characterized its E3 ligase activity. We confirm that the complex i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3aa39f95421b517b5326395c6b4791cd
http://link.springer.com/article/10.1038/s41598-019-46279-5
http://link.springer.com/article/10.1038/s41598-019-46279-5
Publikováno v:
The FASEB Journal. 35
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::725d191db7b8ed99a149bd4901aca002
https://doi.org/10.1096/fasebj.2021.35.s1.01693
https://doi.org/10.1096/fasebj.2021.35.s1.01693