Results 151 to 160 of about 2,957 (188)

Detection of <i>Aeromonas hydrophila</i> by Basic and Fluorescent MIRA Assays. [PDF]

Microorganisms
Huang Q, Dai F, Su L, Zhang M, Miao X, Ding Y, Xu C, Xu J.   +7 more
europepmc   +1 more source

Protein Design Meets Single-Molecule Detection: Towards Programmable Nanopore Sensors. [PDF]

Int J Mol Sci
Liu X, Xu C.
europepmc   +1 more source

β-Barrel domain swapping in α-hemolysin enables enhanced single-molecule biomolecule sensing

Liu C, Reccia M, Kavalnyte E, Rocca BMd, Chinappi M, Luo J.   +5 more
europepmc   +1 more source

Molecular mechanism of pore formation by aerolysin-like proteins [PDF]

Philosophical Transactions of the Royal Society B: Biological Sciences, 2017
Aerolysin-like pore-forming proteins are an important family of proteins able to efficiently damage membranes of target cells by forming transmembrane pores. They are characterized by a unique domain organization and mechanism of action that involves extensive conformational rearrangements. Although structures of soluble forms of many different members
Marjetka Podobnik, Gregor Anderluh, Matic Kisovec   +2 more
exaly   +3 more sources

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The analysis of single cysteine molecules with an aerolysin nanopore

The Analyst, 2020
Biological nanopore technology has the advantages of high selectivity and high reproducibility for characterizing single biomolecules.
Bo Yuan, Shuang Li, Yi-Lun Ying, Yi-Tao Long   +3 more
openaire   +2 more sources

Aerolysin Nanopore Electrochemistry

Accounts of Chemical Research
Ions are the crucial signaling components for living organisms. In cells, their transportation across pore-forming membrane proteins is vital for regulating physiological functions, such as generating ionic current signals in response to target molecule recognition.
Jun-Ge Li, Yi-Lun Ying, Yi-Tao Long
openaire   +2 more sources

Purification and some properties of the hemolytic toxin aerolysin

Canadian Journal of Biochemistry, 1981
Aerolysin, the hemolytic toxin produced by Aeromonas hydrophila, has been purified by a combination of salt fractionation, gel filtration, and ion-exchange and hydroxyapatite chromatography. The resulting protein has a molecular weight of 51 500 and appears homogeneous by polyacrylamide gel electrophoresis in sodium dodecyl sulphate.
J T, Buckley, L N, Halasa, K D, Lund, S, MacIntyre   +3 more
openaire   +2 more sources

Preliminary crystallographic analysis of two oligomerization-deficient mutants of the aerolysin toxin, H132D and H132N, in their proteolyzed forms [PDF]

Acta Crystallographica Section F: Structural Biology Communications, 2010
Aerolysin is a major virulence factor produced by the Gram-negative bacterium Aeromonas hydrophila and is a member of the beta-pore-forming toxin family.
Gisou van der Goot, F G van der Goot
exaly   +3 more sources

Laetiporus sulphureus Lectin and Aerolysin Protein Family

2010
The parasitic mushroom Laetiporus sulphureus produces a family of lectins (LSL's) sharing 80-90% sequence identity that possesses a low but significant sequence similarity to the bacterial pore-forming toxins mosquitocidal toxin Mtx-2 from Bacillus sphaericus and a toxin from Clostridium septicum.
José Miguel, Mancheño, Hiroaki, Tateno, Daniel, Sher, Irwin J, Goldstein   +3 more
openaire   +2 more sources

Dynamics of Unfolded Protein Transport through an Aerolysin Pore

Journal of the American Chemical Society, 2011
Protein export is an essential mechanism in living cells and exported proteins are usually translocated through a protein-conducting channel in an unfolded state. Here we analyze, by electrical detection, the entry and transport of unfolded proteins, at the single molecule level, with different stabilities through an aerolysin pore, as a function of ...
Pastoriza-Gallego, Manuela, Rabah, Leila, Gibrat, Gabriel, Thiebot, Benedicte, van der Goot, Gisou, Auvray, Loic, Betton, Jean-Michel, Pelta, Juan   +7 more
openaire   +2 more sources