Zobrazeno 1 - 10
of 174
pro vyhledávání: '"Wesley I. Sundquist"'
Autor:
Ronald Swanstrom, Wesley I. Sundquist
Publikováno v:
Viruses, Vol 13, Iss 11, p 2218 (2021)
Steve Oroszlan determined the sequences at the ends of virion proteins for a number of different retroviruses. This work led to the insight that the amino-terminal amino acid of the mature viral CA protein is always proline. In this remembrance, we r
Externí odkaz:
https://doaj.org/article/2d76e02f51164c92af5b9bafc7cba578
Autor:
Elliott L Paine, Jack J Skalicky, Frank G Whitby, Douglas R Mackay, Katharine S Ullman, Christopher P Hill, Wesley I Sundquist
Publikováno v:
eLife, Vol 12 (2023)
The Endosomal Sorting Complexes Required for Transport (ESCRT) machinery mediates the membrane fission step that completes cytokinetic abscission and separates dividing cells. Filaments composed of ESCRT-III subunits constrict membranes of the interc
Externí odkaz:
https://doaj.org/article/2fc3d4be4cff4d3e80b6e77ad5bf983b
Autor:
Dawn M Wenzel, Douglas R Mackay, Jack J Skalicky, Elliott L Paine, Matthew S Miller, Katharine S Ullman, Wesley I Sundquist
Publikováno v:
eLife, Vol 11 (2022)
The 12 related human ESCRT-III proteins form filaments that constrict membranes and mediate fission, including during cytokinetic abscission. The C-terminal tails of polymerized ESCRT-III subunits also bind proteins that contain Microtubule-Interacti
Externí odkaz:
https://doaj.org/article/cc5c47a4664040128fa579ea2adf3aa6
Autor:
Lauren K Strohacker, Douglas R Mackay, Madeline A Whitney, Genevieve C Couldwell, Wesley I Sundquist, Katharine S Ullman
Publikováno v:
eLife, Vol 10 (2021)
The abscission checkpoint regulates the ESCRT membrane fission machinery and thereby delays cytokinetic abscission to protect genomic integrity in response to residual mitotic errors. The checkpoint is maintained by Aurora B kinase, which phosphoryla
Externí odkaz:
https://doaj.org/article/a56c544995e947659cbf56d6a5b966f3
Autor:
Han Han, James M Fulcher, Venkata P Dandey, Janet H Iwasa, Wesley I Sundquist, Michael S Kay, Peter S Shen, Christopher P Hill
Publikováno v:
eLife, Vol 8 (2019)
Many AAA+ ATPases form hexamers that unfold protein substrates by translocating them through their central pore. Multiple structures have shown how a helical assembly of subunits binds a single strand of substrate, and indicate that translocation res
Externí odkaz:
https://doaj.org/article/d6a79491d33f44f68941cb6081b14f95
Publikováno v:
eLife, Vol 6 (2017)
The hexameric AAA ATPase Vps4 drives membrane fission by remodeling and disassembling ESCRT-III filaments. Building upon our earlier 4.3 Å resolution cryo-EM structure (Monroe et al., 2017), we now report a 3.2 Å structure of Vps4 bound to an ESCRT
Externí odkaz:
https://doaj.org/article/6d1153d527ba467ba364d4589a44c4f8
Autor:
Elliott L. Paine, Jack J. Skalicky, Frank G. Whitby, Douglas R. Mackay, Katharine S. Ullman, Christopher P. Hill, Wesley I. Sundquist
The Endosomal Sorting Complexes Required for Transport (ESCRT) machinery mediates the membrane fission step that completes cytokinetic abscission and separates dividing cells. Filaments composed of ESCRT-III subunits constrict membranes of the interc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5da5714884e80fb696494f6ec8eef075
https://doi.org/10.1101/2022.10.18.512775
https://doi.org/10.1101/2022.10.18.512775
Autor:
Michael D Schaller, Gary McDowell, André Porter, Dorothy Shippen, Katherine L Friedman, Matthew S Gentry, Tricia R Serio, Wesley I Sundquist
Publikováno v:
eLife, Vol 6 (2017)
Numerous concerns have been raised about the sustainability of the biomedical research enterprise in the United States. Improving the postdoctoral training experience is seen as a priority in addressing these concerns, but even identifying who the po
Externí odkaz:
https://doaj.org/article/4a22288ddf17473281626fa8a17bebaf
Publikováno v:
eLife, Vol 6 (2017)
Many important cellular membrane fission reactions are driven by ESCRT pathways, which culminate in disassembly of ESCRT-III polymers by the AAA ATPase Vps4. We report a 4.3 Å resolution cryo-EM structure of the active Vps4 hexamer with its cofactor
Externí odkaz:
https://doaj.org/article/fb2cf80aebc546e4a4fa2f988b2f49e8