Search results

  1. 1.
    0585467 - MBÚ 2025 RIV NL eng J - Journal Article
    Lepesheva, Anna - Grobarčíková, Michaela - Osičková, Adriana - Jurnečka, David - Knoblochová, Šárka - Čížková, Monika - Osička, Radim - Šebo, Peter - Mašín, Jiří
    Modification of the RTX domain cap by acyl chains of adapted length rules the formation of functional hemolysin pores.
    Biochimica Et Biophysica Acta-Biomembranes. Roč. 1866, č. 5 (2024), s. 184311. ISSN 0005-2736. E-ISSN 1879-2642
    R&D Projects: GA ČR(CZ) GA22-15825S; GA ČR(CZ) GA22-01558S; GA ČR(CZ) GX19-27630X; GA MŠMT(CZ) LX22NPO5103; GA MŠMT(CZ) EH22_008/0004597
    Research Infrastructure: EATRIS-CZ IV - 90253; CIISB III - 90242
    Institutional support: RVO:61388971
    Keywords : RTX toxin * Adenylate cyclase toxin * α-Hemolysin * Chimera * Fatty acylation * Cytotoxicity
    OECD category: Microbiology
    Impact factor: 3.4, year: 2022
    Method of publishing: Open access
    https://www.sciencedirect.com/science/article/pii/S0005273624000427?via%3Dihub
    Permanent Link: https://hdl.handle.net/11104/0353157
    FileDownloadSizeCommentaryVersionAccess
    Modification of the RTX.pdf23 MBPublisher’s postprintopen-access
     
     
  2. 2.
    0547497 - MBÚ 2022 RIV DE eng J - Journal Article
    Lepesheva, Anna - Osičková, Adriana - Holubová, Jana - Jurnečka, David - Knoblochová, Šárka - Espinosa-Vinals, Carlos Angel - Bumba, Ladislav - Škopová, Karolína - Fišer, Radovan - Osička, Radim - Šebo, Peter - Mašín, Jiří
    Different roles of conserved tyrosine residues of the acylated domains in folding and activity of RTX toxins.
    Scientific Reports. Roč. 11, č. 1 (2021), č. článku 19814. ISSN 2045-2322. E-ISSN 2045-2322
    R&D Projects: GA MŠMT(CZ) LM2018133; GA ČR(CZ) GA19-12695S; GA ČR(CZ) GX19-27630X; GA ČR(CZ) GA19-04607S
    Research Infrastructure: CIISB II - 90127
    Institutional support: RVO:61388971
    Keywords : adenylate-cyclase toxin * escherichia-coli hemolysin * bordetella-pertussis cyaa * cell-invasive activity * alpha-hemolysin * membrane translocation * complement receptor-3 * fatty-acylation * calcium * binding
    OECD category: Biochemistry and molecular biology
    Impact factor: 4.997, year: 2021
    Method of publishing: Open access
    https://www.nature.com/articles/s41598-021-99112-3
    Permanent Link: http://hdl.handle.net/11104/0323712
     
     


  This site uses cookies to make them easier to browse. Learn more about how we use cookies.