Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Hedda U. Ferris"'
Publikováno v:
Journal of Structural Biology. 186:349-356
Bacterial chemotaxis receptors are elongated homodimeric coiled-coil bundles, which transduce signals generated in an N-terminal sensor domain across 15–20 nm to a conserved C-terminal signaling subdomain. This signal transduction regulates the act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57468e41302dee006cb0dd6664d8e1d7
https://doi.org/10.1016/j.jsb.2014.03.015
https://doi.org/10.1016/j.jsb.2014.03.015
Publikováno v:
Journal of Structural Biology. 186(3):376-379
Sensor histidine kinases are important sensors of the extracellular environment and relay signals via conformational changes that trigger autophosphorylation of the kinase and subsequent phosphorylation of a response regulator. The exact mechanism an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ddbd84ee4293052f33b09dcd1a7db21
Autor:
Tohru Minamino, Yusuke V. Morimoto, Takayuki Kato, Masamichi Ashihara, Hedda U. Ferris, Nao Moriya, Keiichi Namba
Publikováno v:
Biophysics
The bacterial flagellar hook acts as a universal joint to smoothly transmit torque produced by the motor to the filament. The hook protein FlgE assembles into a 55 nm tubular structure with the help of the hook cap (FlgD). FlgE consists of four domai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b3d3d13c5b5c32081d6c41a67257e5f
http://europepmc.org/articles/PMC4629672
http://europepmc.org/articles/PMC4629672
Autor:
Hedda U. Ferris, Tohru Minamino
Publikováno v:
Trends in Microbiology. 14:519-526
The bacterial flagellum is a complex self-assembling nanomachine that contains its own type III protein export apparatus. Upon completion of early flagellar structure, this apparatus switches substrate specificity to export late structural subunits,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76f6c447bf54e149a6977d6fe715aa16
https://doi.org/10.1016/j.tim.2006.10.006
https://doi.org/10.1016/j.tim.2006.10.006
Publikováno v:
Journal of Molecular Biology. 362:1148-1158
The switch in export specificity of the type III flagellar protein export apparatus from rod/hook type to filament type is believed to occur upon completion of hook assembly by way of an interaction of the type III secretion substrate specificity swi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3147989a2f7a2e9b76e80ff9ec0fcae
https://doi.org/10.1016/j.jmb.2006.08.004
https://doi.org/10.1016/j.jmb.2006.08.004
Autor:
May Kihara, Robert M. Macnab, Gillian M. Fraser, Takanori Hirano, Lara L. Devgan, Hedda U. Ferris
Publikováno v:
Molecular Microbiology. 48:1043-1057
FlhB, an integral membrane protein, gates the type III flagellar export pathway of Salmonella. It permits export of rod/hook-type proteins before hook completion, whereupon it switches specificity to recognize filament-type proteins. The cytoplasmic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::071509920523e49134419aeb00e4611e
https://doi.org/10.1046/j.1365-2958.2003.03487.x
https://doi.org/10.1046/j.1365-2958.2003.03487.x
Autor:
Gillian M, Fraser, Takanori, Hirano, Hedda U, Ferris, Lara L, Devgan, May, Kihara, Robert M, Macnab
Publikováno v:
Molecular microbiology. 48(4)
FlhB, an integral membrane protein, gates the type III flagellar export pathway of Salmonella. It permits export of rod/hook-type proteins before hook completion, whereupon it switches specificity to recognize filament-type proteins. The cytoplasmic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::64f4df0c5148681f6d25574f17ec6e93
https://pubmed.ncbi.nlm.nih.gov/12753195
https://pubmed.ncbi.nlm.nih.gov/12753195
Publikováno v:
Seibutsu Butsuri. 46:S193
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4397deab27cea3e550169dab7d876a0b
https://doi.org/10.2142/biophys.46.s193_3
https://doi.org/10.2142/biophys.46.s193_3
Autor:
Michael Hulko, Joachim E. Schultz, Hedda U. Ferris, Jörg Martin, Andrei N. Lupas, Kornelius Zeth, Klaus Hantke, Laura Garcia Mondejar, Stanislaw Dunin-Horkawicz, Murray Coles
Publikováno v:
Structure. (3):378-385
SummaryHAMP domains mediate signal transduction in over 7500 enzyme-coupled receptors represented in all kingdoms of life. The HAMP domain of the putative archaeal receptor Af1503 has a parallel, dimeric, four-helical coiled coil structure, but with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::155088ca4209fcfb0b8d9825722bdf53