Zobrazeno 1 - 10
of 59
pro vyhledávání: '"David F, Blair"'
Autor:
Svenja Hüsing, Manuel Halte, Ulf van Look, Alina Guse, Eric J. C. Gálvez, Emmanuelle Charpentier, David F. Blair, Marc Erhardt, Thibaud T. Renault
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Type-III secretion systems (T3SSs) are capable of translocating proteins with high speed while maintaining the membrane barrier for small molecules. Here, a structure-function analysis of the T3SS pore complex elucidates the precise mechanisms enabli
Externí odkaz:
https://doaj.org/article/b4b81677e4d248c0b18979bbe7b55964
Autor:
David F, Blair, Michael D, Manson
Publikováno v:
Current Biology. 32:R252-R254
David Blair and Michael Manson commemorate the late Howard Berg, who studied, among other things, the biophysics of bacterial motion.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e660eda81485506075aa3d315d397eb
https://doi.org/10.1016/j.cub.2022.02.054
https://doi.org/10.1016/j.cub.2022.02.054
Autor:
Sayan Gupta, Yan Chen, David F. Blair, Alessandro Pandini, Christopher J. Petzold, Paige Wheatley, Shahid Khan, Corie Y. Ralston
Publikováno v:
Biophys J
Phosphorylation ofEscherichia coliCheY protein transduces chemoreceptor stimulation to a highly cooperative flagellar motor response. CheY binds to the N-terminal peptide of the FliM motor protein (FliMN). Constitutively active D13K-Y106W CheY has be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67b29ce13446664e6c4d574cbfb0ee08
https://doi.org/10.1016/j.bpj.2020.08.009
https://doi.org/10.1016/j.bpj.2020.08.009
Autor:
Svenja Hüsing, Ulf van Look, Eric J. C. Gálvez, Alina Guse, Emmanuelle Charpentier, Marc Erhardt, David F. Blair, Thibaud T. Renault
Type-III secretion systems (T3SSs) of the bacterial flagellum and the evolutionarily related injectisome are capable of translocating proteins with a remarkable speed of several thousand amino acids per second. Here, we investigated how T3SSs are abl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0ecdac71dd60e7d4e5433b574bcad74
https://hal.archives-ouvertes.fr/hal-03033199
https://hal.archives-ouvertes.fr/hal-03033199
Publikováno v:
Molecular Microbiology. 107:94-103
During assembly of the bacterial flagellum, protein subunits that form the exterior structures are exported through a specialized secretion apparatus energized by the proton gradient. This category of protein transport, together with the similar proc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6b8091ba29d44087feab78378431020e
https://doi.org/10.1111/mmi.13870
https://doi.org/10.1111/mmi.13870
Autor:
Kelly T. Hughes, Paige Wheatley, Mayukh K. Sarkar, Takanori Hirano, Yang Zhang, Marc Erhardt, Eun A Kim, David F. Blair
Publikováno v:
Molecular Microbiology. 104:234-249
Summary The bacterial flagellum contains a specialized secretion apparatus in its base that pumps certain protein subunits through the growing structure to their sites of installation beyond the membrane. A related apparatus functions in the injectis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3fb4d5d429f914c8cd415ecbcae3924b
https://doi.org/10.1111/mmi.13623
https://doi.org/10.1111/mmi.13623
Autor:
George Ordal, Trevor Meyer, Elizabeth Ward, Joseph Panushka, David F. Blair, Tayson Botelho, Daniel B. Kearns, Eun A Kim
Publikováno v:
Journal of Bacteriology. 201
While the protein complex responsible for controlling the direction (clockwise [CW] or counterclockwise [CCW]) of flagellar rotation has been fairly well studied in Escherichia coli and Salmonella, less is known about the switch complex in Bacillus s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a9087763ae89d14b5d00a732aa6e231
https://doi.org/10.1128/jb.00626-18
https://doi.org/10.1128/jb.00626-18
Publikováno v:
Proceedings of the National Academy of Sciences. 112:4755-4760
Physiological properties of the flagellar rotary motor have been taken to indicate a tightly coupled mechanism in which each revolution is driven by a fixed number of energizing ions. Measurements that would directly test the tight-coupling hypothesi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cab4940afae3bf65c51fddcf75ca4b3
https://doi.org/10.1073/pnas.1419955112
https://doi.org/10.1073/pnas.1419955112
Autor:
Elizabeth, Ward, Thibaud T, Renault, Eun A, Kim, Marc, Erhardt, Kelly T, Hughes, David F, Blair
Publikováno v:
Molecular microbiology. 107(1)
During assembly of the bacterial flagellum, protein subunits that form the exterior structures are exported through a specialized secretion apparatus energized by the proton gradient. This category of protein transport, together with the similar proc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::00180b0434b423a26d25c6ba907ac40c
https://pubmed.ncbi.nlm.nih.gov/29076571
https://pubmed.ncbi.nlm.nih.gov/29076571
Autor:
Ryan Carlisle, Joseph Panushka, Nicholas Ide, Trevor Meyer, Eun A Kim, David F. Blair, Samantha Baker
Publikováno v:
Journal of molecular biology. 429(15)
Direction switching in the flagellar motor of Escherichia coli is under the control of a complex on the rotor formed from the proteins FliG, FliM, and FliN. FliG lies at the top of the switch complex (i.e., nearest the membrane) and is arranged with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29ed1b91a48de0750b4788deadd1543d
https://pubmed.ncbi.nlm.nih.gov/28625846
https://pubmed.ncbi.nlm.nih.gov/28625846