Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Margaret E Daley"'
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
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
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
Publikováno v:
Biochemistry. 43:13012-13017
The dependence of amide proton chemical shifts on temperature is used as an indication of the hydrogen bonding properties in a protein. The amide proton temperature coefficients of the beta-helical antifreeze protein from Tenebrio molitor are examine
Autor:
Margaret E. Daley, Brian D. Sykes
Publikováno v:
Protein Science. 12:1323-1331
Two-dimensional nuclear magnetic resonance spectroscopy was used to investigate the flexibility of the threonine side chains in the beta-helical Tenebrio molitor antifreeze protein (TmAFP) at low temperatures. From measurement of the (3)J(alphabeta)
Publikováno v:
FEBS Letters. 529:261-267
The beetle Tenebrio molitor produces several isoforms of a highly disulfide-bonded β-helical antifreeze protein with one surface comprised of an array of Thr residues that putatively interacts with ice. In order to use mutagenesis to identify the ic
Publikováno v:
Biochemistry. 41:5515-5525
Antifreeze proteins (AFPs) protect many types of organisms from damage caused by freezing. They do this by binding to the ice surface, which causes inhibition of ice crystal growth. However, the molecular mechanism of ice binding leading to growth in
Autor:
Brian D. Sykes, Laurie A. Graham, Yih-Cherng Liou, Cyril M. Kay, Virginia K. Walker, Peter L. Davies, Margaret E Daley
Publikováno v:
Protein Expression and Purification. 19:148-157
The hyperactive antifreeze protein from the beetle, Tenebrio molitor, is an 8.5-kDa, threonine-rich protein containing 16 Cys residues, all of which are involved in disulfide bonds. When produced by Escherichia coli, the protein accumulated in the su
Autor:
Margaret E. Daley, Martin Bader, Valerie Le Sage, Hervé Le Moual, Lynne R. Prost, Samuel I. Miller, Rachel E. Klevit
Publikováno v:
Molecular cell. 26(2)
The Salmonellae PhoQ sensor kinase senses the mammalian phagosome environment to activate a transcriptional program essential for virulence. The PhoQ periplasmic domain binds divalent cations, forming bridges with inner membrane phospholipids to main