Results 31 to 40 of about 20,967 (222)

Characteristics of the Protein Complexes and Pores Formed by Bacillus cereus Hemolysin BL [PDF]

open access: yesToxins, 2020
Bacillus cereus Hemolysin BL is a tripartite toxin responsible for a diarrheal type of food poisoning. Open questions remain regarding its mode of action, including the extent to which complex formation prior to cell binding contributes to pore-forming activity, how these complexes are composed, and the properties of the pores formed in the target cell
Nadja Jessberger   +5 more
openaire   +3 more sources

Unfoldase-mediated protein translocation through an α-hemolysin nanopore [PDF]

open access: yesNature Biotechnology, 2013
Using nanopores to sequence biopolymers was proposed more than a decade ago. Recent advances in enzyme-based control of DNA translocation and in DNA nucleotide resolution using modified biological pores have satisfied two technical requirements of a functional nanopore DNA sequencing device. Nanopore sequencing of proteins was also envisioned. Although
Jeff, Nivala   +2 more
openaire   +2 more sources

Antibiotics shaping bacterial genome: deletion of an IS91 flanked virulence determinant upon exposure to subinhibitory antibiotic concentrations. [PDF]

open access: yesPLoS ONE, 2011
The nucleoid-associated proteins Hha and YdgT repress the expression of the toxin α-hemolysin. An Escherichia coli mutant lacking these proteins overexpresses the toxin α-hemolysin encoded in the multicopy recombinant plasmid pANN202-312R.
Laura Pedró   +5 more
doaj   +1 more source

Subunit Dimers of α-Hemolysin Expand the Engineering Toolbox for Protein Nanopores [PDF]

open access: yesJournal of Biological Chemistry, 2011
Staphylococcal α-hemolysin (αHL) forms a heptameric pore that features a 14-stranded transmembrane β-barrel. We attempted to force the αHL pore to adopt novel stoichiometries by oligomerizing subunit dimers generated by in vitro transcription and translation of a tandem gene.
Hammerstein, A, Jayasinghe, L, Bayley, H
openaire   +2 more sources

Functions of a hemolysin-like protein in the cyanobacterium Synechocystis sp. PCC 6803 [PDF]

open access: yesArchives of Microbiology, 2011
A glucose-tolerant strain of the cyanobacterium Synechocystis sp. PCC 6803, generally referred to as wild type, produces a hemolysin-like protein (HLP) located on the cell surface. To analyze the function of HLP, we constructed a mutant in which the hlp gene was disrupted.
Tetsushi, Sakiyama   +3 more
openaire   +2 more sources

A portable lipid bilayer system for environmental sensing with a transmembrane protein. [PDF]

open access: yesPLoS ONE, 2014
This paper describes a portable measurement system for current signals of an ion channel that is composed of a planar lipid bilayer. A stable and reproducible lipid bilayer is formed in outdoor environments by using a droplet contact method with a ...
Ryuji Kawano   +6 more
doaj   +1 more source

Effect of Iron Limitation, Elevated Temperature, and Florfenicol on the Proteome and Vesiculation of the Fish Pathogen Aeromonas salmonicida

open access: yesMicroorganisms, 2022
We analyzed the proteomic response of the Gram-negative fish pathogen A. salmonicida to iron limitation, an elevated incubation temperature, and the antibiotic florfenicol.
Tobias Kroniger   +5 more
doaj   +1 more source

Natural channel protein inserts and functions in a completely artificial, solid-supported bilayer membrane [PDF]

open access: yes, 2013
Reconstitution of membrane proteins in artificial membrane systems creates a platform for exploring their potential for pharmacological or biotechnological applications.
Fu, Wangyang   +3 more
core   +1 more source

Elizabethkingia anophelis: Physiologic and Transcriptomic Responses to Iron Stress

open access: yesFrontiers in Microbiology, 2020
In this study, we investigated the global gene expression responses of Elizabethkingia anophelis to iron fluxes in the midgut of female Anopheles stephensi mosquitoes fed sucrose or blood, and in iron-poor or iron-rich culture conditions.
Shicheng Chen   +5 more
doaj   +1 more source

Conserved Omp85 lid-lock structure and substrate recognition in FhaC [PDF]

open access: yes, 2015
Omp85 proteins mediate translocation of polypeptide substrates across and into cellular membranes. They share a common architecture comprising substrate-interacting POTRA domains, a C-terminal 16-stranded β-barrel pore and two signature motifs located on
Delattre, Anne-Sophie   +7 more
core   +1 more source

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