Zobrazeno 1 - 10
of 53
pro vyhledávání: '"Ellis Jaffray"'
Autor:
João Ferreira, Ronald T. Hay, Ellis Jaffray, José Rino, Inês Pinheiro, Joana Cardoso, Rafael Costa, Fernando Ferreira, Vera Santos, Marta Agostinho
Type 2 topoisomerases, in particular the α isoform in human cells, play a key role in cohesion and sister chromatid separation during mitosis. These enzymes are thus vital for cycling cells and are obvious targets in cancer chemotherapy. Evidence ob
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bcab1efe70b422fe935943f78d98b59e
https://doi.org/10.1158/0008-5472.c.6497592
https://doi.org/10.1158/0008-5472.c.6497592
Autor:
João Ferreira, Ronald T. Hay, Ellis Jaffray, José Rino, Inês Pinheiro, Joana Cardoso, Rafael Costa, Fernando Ferreira, Vera Santos, Marta Agostinho
Supplementary Figure 1 from Conjugation of Human Topoisomerase 2α with Small Ubiquitin-like Modifiers 2/3 in Response to Topoisomerase Inhibitors: Cell Cycle Stage and Chromosome Domain Specificity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2018392bcef34187f7c2325b5133435c
https://doi.org/10.1158/0008-5472.22374813
https://doi.org/10.1158/0008-5472.22374813
Autor:
João Ferreira, Ronald T. Hay, Ellis Jaffray, José Rino, Inês Pinheiro, Joana Cardoso, Rafael Costa, Fernando Ferreira, Vera Santos, Marta Agostinho
Supplementary Figure 1 Legend from Conjugation of Human Topoisomerase 2α with Small Ubiquitin-like Modifiers 2/3 in Response to Topoisomerase Inhibitors: Cell Cycle Stage and Chromosome Domain Specificity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bab2a4939213c094927a832dc2eda7c
https://doi.org/10.1158/0008-5472.22374816
https://doi.org/10.1158/0008-5472.22374816
Autor:
Ellis Jaffray, Steve Matthews, Anna Plechanovová, Paul Murphy, Yingqi Xu, Ronald T. Hay, Sarah L. Rouse, J. Carlos Penedo
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
The human genome contains an estimated 600 ubiquitin E3 ligases, many of which are single-subunit E3s (ssE3s) that can bind to both substrate and ubiquitin-loaded E2 (E2~Ub). Within ssE3s structural disorder tends to be located in substrate binding a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf5806855838dded5420bcf80b7148d4
http://europepmc.org/articles/PMC7393505
http://europepmc.org/articles/PMC7393505
Meiotic spindles in most species lack centrosomes and the mechanisms that underlie faithful chromosome segregation in acentrosomal meiotic spindles are not well understood. In C. elegans oocytes, spindle microtubules exert a poleward force on chromos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b06aa7f3842c15e5dc9dd3178eaace69
Publikováno v:
Journal of Cell Science.
Oocyte meiotic spindles in most species lack centrosomes and the mechanisms that underlie faithful chromosome segregation in acentrosomal meiotic spindles are not well understood. In C. elegans oocytes, spindle microtubules exert a poleward force on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1af9ee7cd87792400fabbe241b998d2
https://doi.org/10.1242/jcs.232330
https://doi.org/10.1242/jcs.232330
Autor:
Peter Groitl, Peter Wimmer, Sabrina Schreiner, Wing Hang Ip, Ronald T. Hay, Ellis Jaffray, Tim Horlacher, Thomas Dobner, Julia Berscheminski, Juliane Brun
Publikováno v:
Journal of Virology. 88:6076-6092
Promyelocytic leukemia nuclear bodies (PML-NBs) are nuclear structures that accumulate intrinsic host factors to restrict viral infections. To ensure viral replication, these must be limited by expression of viral early regulatory proteins that funct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84c287660d8eea3af9510649cac85be6
https://doi.org/10.1128/jvi.00469-14
https://doi.org/10.1128/jvi.00469-14
Publikováno v:
Nature
Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2 conjugating enzyme linked to ubiquitin via a thioester bond
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69fbc764309d091dca3c1d044a189aa0
http://europepmc.org/articles/PMC3442243
http://europepmc.org/articles/PMC3442243
Autor:
Senga K. Oxenham, Michael J. Groves, Nicola R. Stanley-Wall, Ronald T. Hay, Ivan Matic, Ellis Jaffray, Christopher L.R. Barratt, Sudhir Tauro
Publikováno v:
Journal of Proteome Research
J Proteome Res
J Proteome Res
Quantitative mass spectrometry-based proteomics is a vital tool in modern life science research. In contrast to the popularity of approaches for relative protein quantitation, the widespread use of absolute quantitation has been hampered by inefficie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44a16e3af782d4a0b082b6db80d4c2c8
https://doi.org/10.1021/pr2004715
https://doi.org/10.1021/pr2004715
Autor:
Kenneth A. Johnson, Ronald T. Hay, Stephen A. McMahon, Ellis Jaffray, Iva Navratilova, James H. Naismith, Anna Plechanovová
Publikováno v:
Nature Structural & Molecular Biology. 18:1052-1059
Mammalian RNF4 is a dimeric RING ubiquitin E3 ligase that ubiquitylates poly-SUMOylated proteins. We found that RNF4 bound ubiquitin-charged UbcH5a tightly but free UbcH5a weakly. To provide insight into the mechanism of RING-mediated ubiquitylation,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c6c1a7a20db867c56e715e049f2c385
https://doi.org/10.1038/nsmb.2108
https://doi.org/10.1038/nsmb.2108