Zobrazeno 1 - 10
of 98
pro vyhledávání: '"Catherine L. Day"'
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Attachment of ubiquitin to proteins is tightly regulated and controls many signalling pathways. Here, the authors show that addition of ubiquitin by the RING E3 ligases Arkadia and Ark2C is enhanced by ubiquitin and a charged loop that precedes the R
Externí odkaz:
https://doaj.org/article/8a8cd9124e9c4313b181a60fb3e1d1bf
Autor:
Reuben McGregor, Alana L. Whitcombe, Campbell R. Sheen, James M. Dickson, Catherine L. Day, Lauren H. Carlton, Prachi Sharma, J. Shaun Lott, Barbara Koch, Julie Bennett, Michael G. Baker, Stephen R. Ritchie, Shivani Fox-Lewis, Susan C. Morpeth, Susan L. Taylor, Sally A. Roberts, Rachel H. Webb, Nicole J. Moreland
Publikováno v:
PeerJ, Vol 8, p e9863 (2020)
Background Serological assays that detect antibodies to SARS-CoV-2 are critical for determining past infection and investigating immune responses in the COVID-19 pandemic. We established ELISA-based immunoassays using locally produced antigens when N
Externí odkaz:
https://doaj.org/article/f4d51d459e1742a5b2037cdfc57a8dd8
Autor:
Martina Foglizzo, Adam J. Middleton, Abigail E. Burgess, Jennifer M. Crowther, Renwick C. J. Dobson, James M. Murphy, Catherine L. Day, Peter D. Mace
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
The Polycomb Repressive-Deubiquitinase (PR-DUB) complex is responsible for the removal of the ubiquitin epigenetic modification from Histone 2A. Here the authors describe the structure of the Drosophila PR-DUB complex, providing new insight into its
Externí odkaz:
https://doaj.org/article/5fe6531411b6437bb98f283f88b4a26c
Autor:
Adam J. Middleton, Rhesa Budhidarmo, Anubrita Das, Jingyi Zhu, Martina Foglizzo, Peter D. Mace, Catherine L. Day
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
TRAF6 is a RING E3 ligase that builds Lys63-linked ubiquitin chains. Here, the authors present the crystal structure of TRAF6 bound to the Ubc13~Ub conjugate, which, together with biochemical assays, reveals the role of the zinc finger domains and wh
Externí odkaz:
https://doaj.org/article/ddb61465d25e4a88871e1ae208a5f36f
Publikováno v:
FEBS Letters. 597:1213-1224
For many inflammatory cytokines, the response elicited is dependent on the recruitment of the tumour necrosis factor receptor-associated factor (TRAF) family of adaptor proteins. All TRAF proteins have a trimeric C-terminal TRAF domain, while at the
Autor:
Peter D. Mace, Catherine L. Day
Publikováno v:
Science. 379:1093-1094
Publikováno v:
Nature communications. 13(1)
A large family of E3 ligases that contain both substrate recruitment and RING domains confer specificity within the ubiquitylation cascade. Regulation of RING E3s depends on modulating their ability to stabilise the RING bound E2~ubiquitin conjugate
Autor:
Anubrita Das, Adam J. Middleton, Catherine L. Day, Elizabeth C. Ledgerwood, Prasanth Padala, Peter D. Mace
Publikováno v:
Journal of molecular biology. 433(8)
Tumour necrosis factor (TNF) receptor associated factor (TRAF) family members share a common domain architecture, but play non-redundant physiological roles in cell signalling. At the N terminus, most TRAFs have a RING domain, followed by a series of
Autor:
James M. J. Dickson, Alana L. Whitcombe, Sally A Roberts, Rachel Webb, Campbell R. Sheen, Barbara Koch, Catherine L. Day, Susan C. Morpeth, Lauren H Carlton, Nicole J. Moreland, Shivani Fox-Lewis, Reuben McGregor, Michael G Baker, Julie Bennett, Susan Taylor, J. Shaun Lott, Stephen R Ritchie, Prachi Sharma
Publikováno v:
PeerJ, Vol 8, p e9863 (2020)
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Background Serological assays that detect antibodies to SARS-CoV-2 are critical for determining past infection and investigating immune responses in the COVID-19 pandemic. We established ELISA-based immunoassays using locally produced antigens when N
Autor:
Peter D. Mace, Antonia L Cadell, Catherine L. Day, Pavel Filipčík, David R. Croucher, Sharissa L. Latham
The MEKK1 protein is a pivotal kinase activator of responses to cellular stress. Activation of MEKK1 can trigger various responses, including mitogen activated protein (MAP) kinases, NF-κB signalling, or cell migration. Notably, MEKK1 activity is tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d7a4cd00abcecb375324326e855b019
https://doi.org/10.1101/2020.04.07.030676
https://doi.org/10.1101/2020.04.07.030676