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Modification of the RTX domain cap by acyl chains of adapted length rules the formation of functional hemolysin pores.
Biochim Biophys Acta Biomembr. 2024 Jun;1866(5):184311. doi: 10.1016/j.bbamem.2024.184311. Epub 2024 Apr 1.
Biochim Biophys Acta Biomembr. 2024.
PMID: 38570122
Free article.
A conserved tryptophan in the acylated segment of RTX toxins controls their β2 integrin-independent cell penetration.
Osickova A, Knoblochova S, Bumba L, Man P, Kalaninova Z, Lepesheva A, Jurnecka D, Cizkova M, Biedermannova L, Goldsmith JA, Maynard JA, McLellan JS, Osicka R, Sebo P, Masin J.
Osickova A, et al. Among authors: lepesheva a.
J Biol Chem. 2023 Aug;299(8):104978. doi: 10.1016/j.jbc.2023.104978. Epub 2023 Jun 28.
J Biol Chem. 2023.
PMID: 37390987
Free PMC article.
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Different roles of conserved tyrosine residues of the acylated domains in folding and activity of RTX toxins.
Lepesheva A, Osickova A, Holubova J, Jurnecka D, Knoblochova S, Espinosa-Vinals C, Bumba L, Skopova K, Fiser R, Osicka R, Sebo P, Masin J.
Lepesheva A, et al.
Sci Rep. 2021 Oct 6;11(1):19814. doi: 10.1038/s41598-021-99112-3.
Sci Rep. 2021.
PMID: 34615931
Free PMC article.
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