Zobrazeno 1 - 10
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pro vyhledávání: '"Karen S. Jakes"'
Autor:
Karen S. Jakes
Publikováno v:
Molecular Microbiology. 92:435-439
The mechanisms by which colicins, protein toxins produced by Escherichia coli, kill other E. coli, have become much better understood in recent years. Most colicins initially bind to an outer membrane protein receptor, and then search for a separate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2351e074aeba54e66573c5bec4fc2b45
https://doi.org/10.1111/mmi.12569
https://doi.org/10.1111/mmi.12569
Autor:
Karen S. Jakes
Publikováno v:
Journal of bacteriology. 199(1)
Colicins are protein toxins made by Escherichia coli to kill related bacteria that compete for scarce resources. All colicins must cross the target cell outer membrane in order to reach their intracellular targets. Normally, the first step in the int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a30ddf8b03a0a5cf8626a868ff5ce193
https://pubmed.ncbi.nlm.nih.gov/27795317
https://pubmed.ncbi.nlm.nih.gov/27795317
Autor:
Karen S. Jakes
Publikováno v:
Biochemical Society Transactions. 40:1443-1448
Of the steps involved in the killing of Escherichia coli by colicins, binding to a specific outer-membrane receptor was the best understood and earliest characterized. Receptor binding was believed to be an indispensable step in colicin intoxication,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8740f72747cef431eb7e12099ff0fabd
https://doi.org/10.1042/bst20120207
https://doi.org/10.1042/bst20120207
Publikováno v:
Biochemistry. 51:6753-6759
TonB-dependent transporters (TBDTs), which transport iron-chelating siderophores and vitamin B12 across the outer membrane of gram negative bacteria, share a conserved architecture of a 22-stranded beta-barrel with an amino-terminal plug domain occlu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71953d400ae94b34c63befc7d405f4f6
https://doi.org/10.1021/bi300493u
https://doi.org/10.1021/bi300493u
Publikováno v:
The Journal of General Physiology
Anthrax toxin consists of three proteins: lethal factor (LF), edema factor (EF), and protective antigen (PA). This last forms a heptameric channel, (PA63)7, in the host cell’s endosomal membrane, allowing the former two (which are enzymes) to be tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7fa1f7dd5c0e1e91977b9da255d6fcf
http://europepmc.org/articles/PMC3068283
http://europepmc.org/articles/PMC3068283
Autor:
Karen S. Jakes, Alan Finkelstein
Publikováno v:
Molecular Microbiology. 75:567-578
Colicin Ia, a channel-forming bactericidal protein, uses the outer membrane protein, Cir, as its primary receptor. To kill E. coli, it must cross this membrane. The crystal structure of Ia receptor-binding domain bound to Cir, a 22-stranded plugged
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::87c70a1e1cc7e52c8a62adf3954beb17
https://doi.org/10.1111/j.1365-2958.2009.06966.x
https://doi.org/10.1111/j.1365-2958.2009.06966.x
Publikováno v:
The Journal of General Physiology
Colicin Ia is a bactericidal protein of 626 amino acid residues that kills its target cell by forming a channel in the inner membrane; it can also form voltage-dependent channels in planar lipid bilayer membranes. The channel-forming activity resides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0a2ca1d8c26d6855264736909844e64
https://doi.org/10.1085/jgp.200810042
https://doi.org/10.1085/jgp.200810042
Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import
Autor:
Paul K. Kienker, Lothar Esser, Petra Lukacik, Travis J. Barnard, Susan K. Buchanan, Sylvestre Grizot, Rodolfo Ghirlando, Karen S. Jakes, Maruf M.U. Ali
Publikováno v:
The EMBO Journal. 26:2594-2604
Colicin Ia is a 69 kDa protein that kills susceptible Escherichia coli cells by binding to a specific receptor in the outer membrane, colicin I receptor (70 kDa), and subsequently translocating its channel forming domain across the periplasmic space,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeaa5852b09faf037c16bd4bf7dbfe66
https://doi.org/10.1038/sj.emboj.7601693
https://doi.org/10.1038/sj.emboj.7601693
Publikováno v:
The Journal of General Physiology
The bacterial toxin colicin Ia forms voltage-gated channels in planar lipid bilayers. The toxin consists of three domains, with the carboxy-terminal domain (C-domain) responsible for channel formation. The C-domain contributes four membrane-spanning
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3f3d16a2fa869b5d1600e0861177a13
http://europepmc.org/articles/PMC2229546
http://europepmc.org/articles/PMC2229546
Publikováno v:
The Journal of Physical Chemistry B. 106:7355-7364
We demonstrate the use of Lee-Goldburg cross-polarization (LG-CP) NMR under fast magic-angle spinning (MAS) to investigate the amplitude and geometry of segmental motions in biomolecular and polymeric solids. Motional geometry information was previou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::effd935690ef17e1bd29fdd9812d42e2
https://doi.org/10.1021/jp0156064
https://doi.org/10.1021/jp0156064