Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Erin G. Worrall"'
Autor:
Susanne Pettersson, Elizabeth A. Blackburn, Borek Vojtesek, Petr Müller, Jennifer Fraser, Ted R. Hupp, Erin G. Worrall, Yao Lin, Malcolm D. Walkinshaw, Vivien Landre, Kathryn L. Ball
Publikováno v:
Journal of Molecular Biology. 427:1728-1747
Mouse double minute 2 (MDM2) has a phosphorylation site within a lid motif at Ser17 whose phosphomimetic mutation to Asp17 stimulates MDM2-mediated polyubiquitination of p53. MDM2 lid deletion, but not Asp17 mutation, induced a blue shift in the λ(m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bb3859ac7d4302679bdeb1e00c51c17
https://doi.org/10.1016/j.jmb.2014.12.011
https://doi.org/10.1016/j.jmb.2014.12.011
Autor:
Ted R. Hupp, Eva Ruckova, David Argyle, Erin G. Worrall, Borek Vojtesek, Saurabh Jain, Kathryn L. Ball, John Clayton, Jianguo Shi, Paul A. Davis, Petr Müller, Robin Fåhraeus, Sandra Hemmington, Asmare A. Limeneh, Stefano Comazzi, Euan Murray, William H. Humphries, Luca Aresu
Publikováno v:
PLoS ONE
Jain, S, Aresu, L, Comazzi, S, Shi, J, Worrall, E, Clayton, J, Humphries, W, Hemmington, S, Davis, P, Murray, E, Limeneh, A A, Ball, K, Ruckova, E, Muller, P, Vojtesek, B, Fahraeus, R, Argyle, D & Hupp, T R 2016, ' The Development of a Recombinant scFv Monoclonal Antibody Targeting Canine CD20 for Use in Comparative Medicine ', PLoS ONE, vol. 11, no. 2, e0148366 . https://doi.org/10.1371/journal.pone.0148366
PLoS ONE, Vol 11, Iss 2, p e0148366 (2016)
Jain, S, Aresu, L, Comazzi, S, Shi, J, Worrall, E, Clayton, J, Humphries, W, Hemmington, S, Davis, P, Murray, E, Limeneh, A A, Ball, K, Ruckova, E, Muller, P, Vojtesek, B, Fahraeus, R, Argyle, D & Hupp, T R 2016, ' The Development of a Recombinant scFv Monoclonal Antibody Targeting Canine CD20 for Use in Comparative Medicine ', PLoS ONE, vol. 11, no. 2, e0148366 . https://doi.org/10.1371/journal.pone.0148366
PLoS ONE, Vol 11, Iss 2, p e0148366 (2016)
Monoclonal antibodies are leading agents for therapeutic treatment of human diseases, but are limited in use by the paucity of clinically relevant models for validation. Sporadic canine tumours mimic the features of some human equivalents. Developing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dff496da8c10645a58da92865fb48c4
http://europepmc.org/articles/PMC4760772
http://europepmc.org/articles/PMC4760772
Publikováno v:
Journal of Molecular Biology. 398:414-428
The multidomain E3 ubiquitin ligase MDM2 catalyzes p53 ubiquitination by a “dual-site” docking mechanism whereby MDM2 binding to at least two distinct peptide motifs on p53 promotes ubiquitination. One protein–protein interaction occurs between
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52d1a6289fd5bf9ee1cc3e85f6a7c299
https://doi.org/10.1016/j.jmb.2010.03.023
https://doi.org/10.1016/j.jmb.2010.03.023
Autor:
Susanne Pettersson, Janice Bramham, Bartosz Wawrzynow, Alicja Zylicz, Kathryn L. Ball, Erin G. Worrall, Ted R. Hupp
Publikováno v:
Wawrzynow, B, Pettersson, S, Zylicz, A, Bramham, J, Worrall, E, Hupp, T R & Ball, K L 2009, ' A Function for the RING Finger Domain in the Allosteric Control of MDM2 Conformation and Activity ', Journal of Biological Chemistry, vol. 284, no. 17, pp. 11517-11530 . https://doi.org/10.1074/jbc.M809294200
The MDM2 oncoprotein plays multiple regulatory roles in the control of p53-dependent gene expression. A picture of MDM2 is emerging where structurally discrete but interdependent functional domains are linked through changes in conformation. The doma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1936e5af2fdd5fd43543de975d417843
https://doi.org/10.1074/jbc.m809294200
https://doi.org/10.1074/jbc.m809294200
Autor:
Ted R. Hupp, Erin G. Worrall
Publikováno v:
Advances in Cancer Management
1.1 A brief history of basic cancer research driven target discovery The incidence of cancer has risen dramatically over the last century due to the improved treatments of chronic diseases and as a consequence of an ever aging population that results
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c0249e37898e25a09a3957f84bb3a10
http://www.intechopen.com/articles/show/title/using-clinical-proteomics-to-discover-novel-anti-cancer-targets-for-mab-therapeutics-
http://www.intechopen.com/articles/show/title/using-clinical-proteomics-to-discover-novel-anti-cancer-targets-for-mab-therapeutics-
Autor:
Bartosz Wawrzynow, Erin G. Worrall, Liam J. Worrall, Kathryn L. Ball, Malcolm D. Walkinshaw, Ted R. Hupp
Publikováno v:
Worrall, E G, Wawrzynow, B, Worrall, L, Walkinshaw, M, Ball, K L & Hupp, T R 2009, ' Regulation of the E3 ubiquitin ligase activity of MDM2 by an N-terminal pseudo-substrate motif ', Journal of Chemical Biology, vol. 2, no. 3, pp. 113-29 . https://doi.org/10.1007/s12154-009-0019-5
The tumor suppressor p53 has evolved a MDM2-dependent feedback loop that promotes p53 protein degradation through the ubiquitin-proteasome system. MDM2 is an E3-RING containing ubiquitin ligase that catalyzes p53 ubiquitination by a dual-site mechani
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::892257fee00255632790af8e5acc3b63
https://www.pure.ed.ac.uk/ws/files/9332875/JCB_2009.pdf
https://www.pure.ed.ac.uk/ws/files/9332875/JCB_2009.pdf
Publikováno v:
Molecular cell. 23(2)
The control of p53 ubiquitination by MDM2 provides a model system to define how an E3-ligase functions on a conformationally flexible substrate. The mechanism of MDM2-mediated ubiquitination of p53 has been analyzed by deconstructing, in vitro, the M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6acde48124710e7dab41f0fdb38b124
https://pubmed.ncbi.nlm.nih.gov/16857591
https://pubmed.ncbi.nlm.nih.gov/16857591