Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Lynne R Prost"'
Autor:
Kevin G Hicks, Scott P Delbecq, Enea Sancho-Vaello, Marie-Pierre Blanc, Katja K Dove, Lynne R Prost, Margaret E Daley, Kornelius Zeth, Rachel E Klevit, Samuel I Miller
Publikováno v:
eLife, Vol 4 (2015)
Salmonella PhoQ is a histidine kinase with a periplasmic sensor domain (PD) that promotes virulence by detecting the macrophage phagosome. PhoQ activity is repressed by divalent cations and induced in environments of acidic pH, limited divalent catio
Externí odkaz:
https://doaj.org/article/54b29335fe3242b998e4cbb942a84163
Autor:
Nathan M. Sherer, Laraine L. Zimdars, Laura L. Kiessling, Cassie M. Jarvis, Lynne R. Prost, Soyeong Park, Jaye C. Gardiner, Daniel B. Zwick, Mohammad Murshid Alam, Joseph C. Grim
Publikováno v:
Proceedings of the National Academy of Sciences. 116:14862-14867
Dendritic cell (DC) lectins mediate the recognition, uptake, and processing of antigens, but they can also be coopted by pathogens for infection. These distinct activities depend upon the routing of antigens within the cell. Antigens directed to endo
Autor:
Laura L. Kiessling, Mohammad Murshid Alam, Soyeong Park, Laraine L. Zimdars, Joseph C. Grim, Cassie M. Jarvis, Lynne R. Prost, Jaye C. Gardiner, Nathan M. Sherer, Daniel B. Zwick
Dendritic cell (DC) lectins mediate the recognition, uptake, and processing of antigens, but they can also be co-opted by pathogens for infection. These distinct activities depend upon the routing of antigens within the cell. Antigens directed to end
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7169692f491e03032a99e294d9294f3
https://doi.org/10.1101/566141
https://doi.org/10.1101/566141
Publikováno v:
ACS Chemical Biology. 7:1603-1608
An understanding of the biological roles of lectins will be advanced by ligands that can inhibit or even recruit lectin function. To this end, glycomimetics, non-carbohydrate ligands that function analogously to endogenous carbohydrates, are being so
Autor:
William Wiley Navarre, Jinglin L. Xie, Michael Ibba, Alex U. Singer, Hervé Roy, Lynne R. Prost, S. Betty Zou, Elena Edvokimova, Ferric C. Fang, Alexei Savchenko, Runjun D. Kumar
Publikováno v:
Molecular Cell. 39:209-221
We report an interaction between poxA, encoding a paralog of lysyl tRNA-synthetase, and the closely linked yjeK gene, encoding a putative 2,3-beta-lysine aminomutase, that is critical for virulence and stress resistance in Salmonella enterica. Salmon
Publikováno v:
Molecular Microbiology. 69:503-519
Summary The PhoQ sensor kinase is essential for Salmonella typhimurium virulence for animals, and a homologue exists in the environmental organism and opportunistic pathogen Pseudomonas aeruginosa. S. typhimurium PhoQ (ST-PhoQ) is repressed by millim
Publikováno v:
Immunological Reviews. 219:55-65
Salmonella enterica is a facultative intracellular pathogen that replicates within macrophages. The interaction of this pathogen with mammalian cells is a complex process involving hundreds of bacterial products that are sensed by and alter mammalian
Autor:
Kornelius Zeth, Lynne R. Prost, Enea Sancho-Vaello, Katja K. Dove, Kevin G. Hicks, Samuel I. Miller, Margaret E Daley, Rachel E. Klevit, Marie-Pierre Blanc, Scott P Delbecq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d2a9fd7f945e2cf41635badac2e704e5
https://doi.org/10.7554/elife.06792.019
https://doi.org/10.7554/elife.06792.019
Autor:
Marie-Pierre Blanc, Scott P Delbecq, Katja K. Dove, Rachel E. Klevit, Kornelius Zeth, Enea Sancho-Vaello, Lynne R. Prost, Samuel I. Miller, Kevin G. Hicks, Margaret E Daley
Publikováno v:
eLife, Vol 4 (2015)
eLife
eLife
Salmonella PhoQ is a histidine kinase with a periplasmic sensor domain (PD) that promotes virulence by detecting the macrophage phagosome. PhoQ activity is repressed by divalent cations and induced in environments of acidic pH, limited divalent catio
The C-type lectin dendritic cell-specific intercellular adhesion molecule 3–grabbing nonintegrin (DC-SIGN) can serve as a docking site for pathogens on the surface of dendritic cells. Pathogen binding to DC-SIGN can have diverse consequences for th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2895eb8b94356fb94a0f34c4460c1fe
https://europepmc.org/articles/PMC3359018/
https://europepmc.org/articles/PMC3359018/