Zobrazeno 1 - 10
of 71
pro vyhledávání: '"Mark J Solomon"'
Autor:
Ruiwen Wang, Mark J Solomon
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e48020 (2012)
The highly orchestrated progression of the cell cycle depends on the degradation of many regulatory proteins at different cell cycle stages. One of the key cell cycle ubiquitin ligases is the Skp1-cullin-F-box (SCF) complex. Acting in concert with th
Externí odkaz:
https://doaj.org/article/301b8132a96b45798551f503b25147cb
Publikováno v:
PLoS ONE, Vol 7, Iss 9, p e45895 (2012)
The Anaphase-Promoting Complex/Cyclosome (APC/C) is an essential ubiquitin ligase that targets numerous proteins for proteasome-mediated degradation in mitosis and G1. To gain further insight into cellular pathways controlled by APC/C(Cdh1), we devel
Externí odkaz:
https://doaj.org/article/99ff6ca8ec6645c6ac628668dbb30d66
Autor:
Deborah A. Enke, Mark J. Solomon
Publikováno v:
BioTechniques, Vol 22, Iss 1, Pp 74-78 (1997)
Externí odkaz:
https://doaj.org/article/c3607113e04947849e90c3a77f9b6b73
Publikováno v:
Cellular Signalling. 33:41-48
The anaphase-promoting complex (APC) is a ubiquitin ligase responsible for promoting the degradation of many cell cycle regulators. One of the activators and substrate-binding proteins for the APC is Cdc20. It has been shown previously that Cdc20 can
Autor:
Mark J. Solomon, Darryl J. Pappin, Arthur Makarenko, James J. Becnel, Catherine Texier, Denis Ostapenko, Dieter Söll, Neil D. Sanscrainte, Sergey Melnikov, Keith Rivera
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 2018, 115 (27), pp.E6245-E6253. ⟨10.1073/pnas.1803208115⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2018, 115 (27), pp.E6245-E6253. ⟨10.1073/pnas.1803208115⟩
Proceedings of the National Academy of Sciences of the United States of America, 2018, 115 (27), pp.E6245-E6253. ⟨10.1073/pnas.1803208115⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2018, 115 (27), pp.E6245-E6253. ⟨10.1073/pnas.1803208115⟩
Microsporidia are parasitic fungi-like organisms that invade the interior of living cells and cause chronic disorders in a broad range of animals, including humans. These pathogens have the tiniest known genomes among eukaryotic species, for which th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00b853bd507231e731205fe56bb2daa5
https://hal.science/hal-01867872
https://hal.science/hal-01867872
Publikováno v:
The EMBO Journal. 30:1818-1829
The anaphase promoting complex (APC) is a ubiquitin ligase that promotes the degradation of cell-cycle regulators by the 26S proteasome. Cdc20 and Cdh1 are WD40-containing APC co-activators that bind destruction boxes (DB) and KEN boxes within substr
Autor:
Mark J. Solomon, Denis Ostapenko
Publikováno v:
Molecular Biology of the Cell
The anaphase-promoting complex is a ubiquitin ligase that promotes the degradation of numerous cell cycle regulators during mitosis and in G1. This report identifies two transcriptional repressors—Nrm1 and Yhp1—as novel APC substrates in budding
Autor:
Mark J. Solomon, Aiyang Cheng
Publikováno v:
Cell Cycle. 7:3037-3047
Cyclin-dependent kinases (CDKs) control cell cycle transitions and progression. In addition to their activation via binding to cyclins, CDKs can be activated via binding to an unrelated class of cell cycle regulators termed Speedy/Ringo (S/R) protein
Publikováno v:
Molecular and Cellular Biology. 28:4653-4664
The ubiquitin ligase activity of the anaphase-promoting complex (APC)/cyclosome needs to be tightly regulated for proper cell cycle progression. Substrates are recruited to the APC by the Cdc20 and Cdh1 accessory proteins. The Cdh1-APC interaction is
Autor:
Ryuichi Nishihama, Nolan Ko, John R. Pringle, Denis Ostapenko, Mark J. Solomon, David O. Morgan, Gregory H. Tully
Publikováno v:
Molecular Biology of the Cell. 18:5139-5153
In the yeast Saccharomyces cerevisiae, a ring of myosin II forms in a septin-dependent manner at the budding site in late G1. This ring remains at the bud neck until the onset of cytokinesis, when actin is recruited to it. The actomyosin ring then co