Results 161 to 170 of about 2,957 (188)

Puncturing Cell Membranes: Comparison of Colicin A and Aerolysin

1992
Colicin A from Citrobacter freundii and aerolysin from Aeromonas hydrophila are representatives of two classes of pore-forming toxins. Colicin A, an alpha-helical protein, contains a hydrophobic hairpin which is buried inside the structure in solution. It is an “inside out” membrane protein.
N. Didat, J. M. Gonzàlez-Mañas, F. G. Van Der Goot, D. Jeanteur, J. H. Lakey, F. Pattus, D. Massotte, S. Scianimanico, H.-U. Wilmsen   +8 more
openaire   +1 more source

Aerolysin is activated by metalloprotease in Aeromonas veronii biovar sobria

Journal of Medical Microbiology, 2004
Aeromonas veronii is an opportunistic human pathogen that causes diarrhoea and extraintestinal infections, such as wound infection and septicaemia. An A. veronii protease (AVP) from a biovar sobria strain, AeG1, was partially purified and characterized. Mature AVP hydrolysed casein but not elastin, and protease activity was inhibited by metalloprotease
Tianyan, Song, Claudia, Toma, Noboru, Nakasone, Masaaki, Iwanaga   +3 more
openaire   +2 more sources

Unveiling the Heterogenous Dephosphorylation of DNA Using an Aerolysin Nanopore

ACS Nano, 2020
The simultaneous occurrence of multiple heterogeneous DNA phosphorylation statuses, which include 5' end phosphorylation, 5' end dephosphorylation, 3' end phosphorylation, and 3' end dephosphorylation, is crucial for regulating numerous cellular processes.
Meng-Yin Li, Yi-Lun Ying, Shuang Li, Ya-Qian Wang, Xue-Yuan Wu, Yi-Tao Long   +5 more
openaire   +2 more sources

Aerolysin (Aeromonas hydrophila)

1997
Abstract Aerolysin is secreted as a 52 kDa protoxin by Aeromonas sp. (see van der Goot et al. 1994, for a recent review). The protein appears to be primarily responsible for the patho¬ genicity of A. hydrophila to mice (Chakraborty et al. 1987).
openaire   +1 more source

Cucurbituril–aerolysin nanopore interactions for molecular recognition

The European Physical Journal E
Cucurbit[n]urils (CBn, n = 5-8) are macrocyclic hosts that form stable inclusion complexes with a variety of guest molecules, including amino acids and peptides. In this study, we investigate the interactions of CBn homologues with the aerolysin (AeL) protein nanopore using single-molecule ionic current recordings and molecular docking simulations ...
Ouldali, Hadjer, Dejoux, Camille, Pastoriza-Gallego, Manuela, Cojocaru, Corneliu, Farcas, Aurica, Oukhaled, Abdelghani   +5 more
openaire   +3 more sources

[27] Aerolysin from Aeromonas hydrophila

1988
Publisher Summary This chapter describes the purification procedure of aerolysin from Aeromonas hydrophila . Aerolysin is a soluble cytolytic protein produced by the gram-negative bacteria Aeromonas hydrophila. It is released to the extracellular medium as an inactive protoxin (proaerolysin) that is converted to the active protein by one or more ...
J Thomas Buckley, S Peter Howard
openaire   +1 more source

Aerolysin — the ins and outs of a model channel‐forming toxin

Molecular Microbiology, 1996
Aerolysin is one of a large group of bacterial proteins that can kill target cells by forming discrete channels in their plasma membranes. The toxin has many properties in common with the porins of the Gram‐negative bacterial outer membrane, including an extensive amount of β‐structure, a high proportion of hydrophilic amino acid side‐chains and no ...
M W, Parker, F G, van der Goot, J T, Buckley   +2 more
openaire   +2 more sources

Aerolysin and related Aeromonas toxins

2006
Gurcel, L., Iacovache, I., van der Goot, F.G.   +2 more
openaire   +3 more sources

MUTANT AEROLYSIN AND USES THEREOF

2022
DAL PERARO MATTEO, CAO CHAN
openaire   +3 more sources

Palmatine Inhibits the Pathogenicity of Aeromonas hydrophila by Reducing Aerolysin Expression

Foods, 2022
Yongtao Liu, Qiuhong Yang, Xiaohui Ai
exaly