Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Stan A. Burgess"'
Publikováno v:
Nature Reviews Molecular Cell Biology. 14:713-726
Fuelled by ATP hydrolysis, dyneins generate force and movement on microtubules in a wealth of biological processes, including ciliary beating, cell division and intracellular transport. The large mass and complexity of dynein motors have made elucida
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0e81c161edfa711ec1da6fa60f556a0
https://doi.org/10.1038/nrm3667
https://doi.org/10.1038/nrm3667
Autor:
Kazuo Sutoh, Reiko Ohkura, Takahide Kon, Hitoshi Sakakibara, Stan A. Burgess, Thomas A. Edwards, Matt L. Walker, Peter J. Knight, Naoki Numata, Bara Malkova, Kazuhiro Oiwa, Anthony J. Roberts
Publikováno v:
Structure. 20(10):1670-1680
Summary Dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. Dyneins are members of the AAA+ superfamily of ring-shaped en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8987d55612fa867314a43b906e4410dc
Autor:
James R. Sellers, John Trinick, Takeshi Sakamoto, Olusola A. Oke, Howard D. White, Eva Forgacs, Peter J. Knight, Stan A. Burgess
Publikováno v:
Proceedings of the National Academy of Sciences. 107:2509-2514
Using electron microscopy and image processing, we have observed myosin 5a modified with lever arms of different lengths (four, six, and eight calmodulin-binding IQ domains) and orientations walking along actin filaments. Step lengths were dependent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec38b467574f3c2fc21efa5ecc2b4358
https://doi.org/10.1073/pnas.0906907107
https://doi.org/10.1073/pnas.0906907107
Autor:
Anthony J. Roberts, Reiko Ohkura, Peter J. Knight, Kazuo Sutoh, I R Gibbons, Kenji Imamula, Stan A. Burgess, Takahide Kon
Publikováno v:
Nature structural & molecular biology
Coupling between ATPase and track-binding sites is essential for molecular motors to move along cytoskeletal tracks. In dynein, these sites are separated by a long coiled-coil stalk which must mediate communication between them, yet the underlying me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fa9a022ecf42931da19dbac5f77d228
http://europepmc.org/articles/PMC2757048
http://europepmc.org/articles/PMC2757048
Autor:
Matt L. Walker, Fumio Arisaka, Bara Malkova, Anthony J. Roberts, Naoki Numata, Yusuke Kato, Reiko Ohkura, Kazuo Sutoh, Stan A. Burgess, Takahide Kon, Peter J. Knight
Publikováno v:
Cell
Dynein ATPases power diverse microtubule-based motilities. Each dynein motor domain comprises a ring-like head containing six AAA+ modules and N- and C-terminal regions, together with a stalk that binds microtubules. How these subdomains are arranged
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afa87053c07bd747412de1600c6ab425
http://europepmc.org/articles/PMC2706395
http://europepmc.org/articles/PMC2706395
Publikováno v:
Biophysical Journal. 93:886-894
Inner-arm dynein-f of Chlamydomonas flagella is a heterodimeric dynein. We performed conventional in vitro motility assays showing that dynein-f translocates microtubules at the comparatively low velocity of approximately 1.2 microm/s. From the depen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bc30b6777249a708e4c89d01add9af4
https://doi.org/10.1529/biophysj.106.101964
https://doi.org/10.1529/biophysj.106.101964
Autor:
Hiroshi Imai, Matt L. Walker, Stan A. Burgess, Tomohiro Shima, Peter J. Knight, Kazuo Sutoh, Takahide Kon
Publikováno v:
Nature Communications
Cytoplasmic dynein is a dimeric AAA+ motor protein that performs critical roles in eukaryotic cells by moving along microtubules using ATP. Here using cryo-electron microscopy we directly observe the structure of Dictyostelium discoideum dynein dimer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8beb7fd6ad4e2070edf1edb236f2035
Autor:
Dean Clarke, Corine St. Gelais, Mark Harris, Lucy Beales, Stan A. Burgess, Stephen Griffin, David J. Rowlands
Publikováno v:
Journal of Biological Chemistry. 281:37057-37068
The p7 protein of hepatitis C virus functions as an ion channel both in vitro and in cell-based assays and is inhibited by amantadine, long alkyl chain imino-sugar derivatives, and amiloride compounds. Future drug design will be greatly aided by info
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c80306eaf54c32bd5c1785279992abc
https://doi.org/10.1074/jbc.m602434200
https://doi.org/10.1074/jbc.m602434200
Publikováno v:
Journal of Structural Biology. 147:247-258
Flexible macromolecules pose special difficulties for structure determination by crystallography or NMR. Progress can be made by electron microscopy, but electron cryo-microscopy of unstained, hydrated specimens is limited to larger macromolecules be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c618b00071a35d405e307e3e8ebe7d3f
https://doi.org/10.1016/j.jsb.2004.04.004
https://doi.org/10.1016/j.jsb.2004.04.004
Autor:
Kevin Leonard, John C. Sparrow, Stan A. Burgess, John Holt, Belinda Bullard, Stephan Schmitz, Peter J. Knight, Matt L. Walker, John Trinick, Gerald Offer
Publikováno v:
Journal of Molecular Biology. 341:1161-1173
Here, we report on the structure and in situ location of arthrin (monoubiquitinated actin). Labelling of insect muscle thin filaments with a ubiquitin antibody reveals that every seventh subunit along the filament long-pitch helices is ubiquitinated.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42344db48e9b5eb4b483a58e7f83c8ec
https://doi.org/10.1016/j.jmb.2004.06.077
https://doi.org/10.1016/j.jmb.2004.06.077