Zobrazeno 1 - 10
of 62
pro vyhledávání: '"Douglass J. Forbes"'
Autor:
Matthew S. Nord, Cyril Bernis, Sarah Carmona, Dennis C. Garland, Anna Travesa, Douglass J. Forbes
Publikováno v:
Nucleus, Vol 11, Iss 1, Pp 178-193 (2020)
Xenopus egg extracts are a powerful in vitro tool for studying complex biological processes, including nuclear reconstitution, nuclear membrane and pore assembly, and spindle assembly. Extracts have been further used to demonstrate a moonlighting reg
Externí odkaz:
https://doaj.org/article/d16cb22ca3d94f26ade2b96123e4c8f6
Autor:
Anna Travesa, Sarah Carmona, Dennis C. Garland, Cyril Bernis, Matthew S Nord, Douglass J. Forbes
Publikováno v:
Nucleus, Vol 11, Iss 1, Pp 178-193 (2020)
Nucleus
article-version (VoR) Version of Record
Nucleus
article-version (VoR) Version of Record
Xenopus egg extracts are a powerful in vitro tool for studying complex biological processes, including nuclear reconstitution, nuclear membrane and pore assembly, and spindle assembly. Extracts have been further used to demonstrate a moonlighting reg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c58c6507ea8dffca89ff299818fb7ee9
https://doi.org/10.1080/19491034.2020.1798093
https://doi.org/10.1080/19491034.2020.1798093
Publikováno v:
Current Opinion in Cell Biology. 34:122-134
The unexpected repurposing of nuclear transport proteins from their function in interphase to an equally vital and very different set of functions in mitosis was very surprising. The multi-talented cast when first revealed included the import recepto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::efee2e79fb38943bec650c4b0b28f75b
https://doi.org/10.1016/j.ceb.2015.07.005
https://doi.org/10.1016/j.ceb.2015.07.005
Publikováno v:
Nucleus
Nuclear pore complexes (NPCs) form the gateway to the nucleus, mediating virtually all nucleocytoplasmic trafficking. Assembly of a nuclear pore complex requires the organization of many soluble sub-complexes into a final massive structure embedded i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2850b7fb2247a9de528bcb472dcf64a2
http://europepmc.org/articles/PMC4615246
http://europepmc.org/articles/PMC4615246
Transportin acts to regulate mitotic assembly events by target binding rather than Ran sequestration
Autor:
Yuh Min Chook, Douglass J. Forbes, Sarah Carmona, Beth Swift-Taylor, Cyril Bernis, Matthew S Nord
Publikováno v:
Molecular Biology of the Cell
Transportin-specific molecular tools are used to show that the mitotic cell contains importin β and transportin “global positioning system” pathways that are mechanistically parallel. Transportin works to control where the spindle, nuclear membr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e492bb53df703e5e8e92a2d0104f4c6
http://europepmc.org/articles/PMC3967982
http://europepmc.org/articles/PMC3967982
Publikováno v:
Molecular Biology of the Cell. 21:4197-4211
Nuclear pore complexes (NPCs) are large proteinaceous channels embedded in double nuclear membranes, which carry out nucleocytoplasmic exchange. The mechanism of nuclear pore assembly involves a unique challenge, as it requires creation of a long-liv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6b85584f61ee5b27ea69e3a09a8f2eeb
https://doi.org/10.1091/mbc.e10-04-0309
https://doi.org/10.1091/mbc.e10-04-0309
Autor:
Douglass J. Forbes, Maho Niwa, Daniel K. Nomura, Lindsay S. Roberts, Arvin B. Tam, Io Guane Rivera, Vivek Chandra
Publikováno v:
Developmental Cell. 46:327-343.e7
The unfolded protein response (UPR) is induced by proteotoxic stress of the endoplasmic reticulum (ER). Here we report that ATF6, a major mammalian UPR sensor, is also activated by specific sphingolipids, dihydrosphingosine (DHS) and dihydroceramide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c819f6007f131ad300e7f05b69c51be6
https://doi.org/10.1016/j.devcel.2018.04.023
https://doi.org/10.1016/j.devcel.2018.04.023
Autor:
Jen Hsuan Wei, Jan M. van Deursen, Joachim Seemann, Yaming Wang, Liviu Malureanu, Mary Dasso, Beatriz M. A. Fontoura, Papia Chakraborty, David E. Levy, Douglass J. Forbes, Hongtao Yu
Publikováno v:
Developmental Cell. 15(5):657-667
Summary The Nup107-160 complex, the largest subunit of the nuclear pore, is multifunctional. It mediates mRNA export in interphase, and has roles in kinetochore function, spindle assembly, and postmitotic nuclear pore assembly. We report here that th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60f66f1c51fdc38e4bfa61d76ad7ee02
Publikováno v:
Molecular Biology of the Cell. 19:3982-3996
Assembly of the nuclear pore, gateway to the genome, from its component subunits is a complex process. In higher eukaryotes, nuclear pore assembly begins with the binding of ELYS/MEL-28 to chromatin and recruitment of the large critical Nup107-160 po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63df6b138cf38b1aa3d432614edf5c8c
https://doi.org/10.1091/mbc.e08-01-0012
https://doi.org/10.1091/mbc.e08-01-0012
Publikováno v:
Molecular and Cellular Biology. 28:1755-1769
Centrins in vertebrates have traditionally been associated with microtubule-nucleating centers such as the centrosome. Unexpectedly, we found centrin 2 to associate biochemically with nucleoporins, including the Xenopus laevis Nup107-160 complex, a c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da124611cd4cc63114f872d479a14698
https://doi.org/10.1128/mcb.01697-07
https://doi.org/10.1128/mcb.01697-07