Results 21 to 30 of about 20,148 (111)

Pore-forming activity of clostridial binary toxins

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2016
Clostridial binary toxins (Clostridium perfringens Iota toxin, Clostridium difficile transferase, Clostridium spiroforme toxin, Clostridium botulinum C2 toxin) as Bacillus binary toxins, including Bacillus anthracis toxins consist of two independent proteins, one being the binding component which mediates the internalization into cell of the ...
Knapp, O., Benz, R., Popoff, Michel Robert   +2 more
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The MACPF/CDC family of pore-forming toxins [PDF]

Cellular Microbiology, 2008
Pore-forming toxins (PFTs) are commonly associated with bacterial pathogenesis. In eukaryotes, however, PFTs operate in the immune system or are deployed for attacking prey (e.g. venoms). This review focuses upon two families of globular protein PFTs: the cholesterol-dependent cytolysins (CDCs) and the membrane attack complex/perforin superfamily ...
Rosado, CJ, Kondos, S, Bull, TE, Kuiper, MJ, Law, RHP, Buckle, AM, Voskoboinik, I, Bird, PI, Trapani, JA, Whisstock, JC, Dunstone, MA   +10 more
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Role of Pore-Forming Toxins in Neonatal Sepsis [PDF]

Clinical and Developmental Immunology, 2013
Protein toxins are important virulence factors contributing to neonatal sepsis. The major pathogens of neonatal sepsis, group B Streptococci,Escherichia coli,Listeria monocytogenes, andStaphylococcus aureus, secrete toxins of different molecular nature, which are key for defining the disease.
Andreas F.-P. Sonnen, Philipp Henneke
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The Pore-forming Toxin Proaerolysin Is Activated by Furin [PDF]

Journal of Biological Chemistry, 1998
Aerolysin is secreted as an inactive dimeric precursor by the bacterium Aeromonas hydrophila. Proteolytic cleavage within a mobile loop near the C terminus of the protoxin is required for oligomerization and channel formation. This loop contains the sequence KVRRAR432, which should be recognized by mammalian proprotein convertases such as furin, PACE4,
Abrami, Laurence, Fivaz, Marc, Decroly, Etienne, Seidah, Nabil, Jean, François, Thomas, Gary, Leppla, Stephen H., Buckley, Thomas, Van Der Goot Grunberg, Françoise G.   +8 more
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Apicomplexan Pore-Forming Toxins

Annual Review of Microbiology
Pore-forming toxins (PFTs) are released by one cell to directly inflict damage on another cell. Hosts use PFTs, including members of the membrane attack complex/perforin protein family, to fight infections and cancer, while bacteria and parasites deploy PFTs to promote infection.
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Pore-forming protein toxins: from structure to function

Progress in Biophysics and Molecular Biology, 2005
Pore-forming protein toxins (PFTs) are one of Nature's most potent biological weapons. An essential feature of their toxicity is the remarkable property that PFTs can exist either in a stable water-soluble state or as an integral membrane pore. In order to convert from the water-soluble to the membrane state, the toxin must undergo large conformational
Michael W, Parker, Susanne C, Feil
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Emerging enterococcus pore-forming toxins with MHC/HLA-I as receptors. [PDF]

Cell, 2022
Xiong X, Tian S, Yang P, Lebreton F, Bao H, Sheng K, Yin L, Chen P, Zhang J, Qi W, Ruan J, Wu H, Chen H, Breault DT, Wu H, Earl AM, Gilmore MS, Abraham J, Dong M.   +18 more
europepmc   +1 more source

Aminopeptidase MNP-1 triggers intestine protease production by activating daf-16 nuclear location to degrade pore-forming toxins in Caenorhabditis elegans. [PDF]

PLoS Pathog, 2023
Chen F, Pang C, Zheng Z, Zhou W, Guo Z, Xiao D, Du H, Bravo A, Soberón M, Sun M, Peng D.   +10 more
europepmc   +1 more source

Antigenic landscapes on Staphylococcus aureus pore-forming toxins reveal insights into specificity and cross-neutralization. [PDF]

MAbs, 2022
Kailasan S, Kant R, Noonan-Shueh M, Kanipakala T, Liao G, Shulenin S, Leung DW, Alm RA, Adhikari RP, Amarasinghe GK, Gross ML, Aman MJ.   +11 more
europepmc   +1 more source

Pore-forming toxins [PDF]

Acta Crystallographica Section A Foundations of Crystallography, 2005
openaire   +1 more source