Modification of the RTX domain cap by acyl chains of adapted length rules the formation of functional hemolysin pores-Reference-Cited by-同舟云学术

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Modification of the RTX domain cap by acyl chains of adapted length rules the formation of functional hemolysin pores

Published:2024-06 Issue:5 Volume:1866 Page:184311
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Lepesheva Anna,Grobarcikova Michaela,Osickova Adriana,Jurnecka David,Knoblochova Sarka,Cizkova Monika,Osicka Radim,Sebo Peter,Masin Jiri

Funder

Ministerstvo školství mládeže a tělovýchovy

Publisher

Elsevier BV

Reference83 articles.

1. RTX proteins: a highly diverse family secreted by a common mechanism;Linhartova;FEMS Microbiol. Rev.,2010

2. Structure-function relationships underlying the capacity of bordetella adenylate cyclase toxin to disarm host phagocytes;Novak;Toxins,2017

3. Adenylate cyclase toxin-hemolysin relevance for pertussis vaccines;Sebo;Expert Rev. Vaccines,2014

4. Bordetella adenylate cyclase toxin: a swift saboteur of host defense;Vojtova;Curr. Opin. Microbiol.,2006

5. The adenylate cyclase toxin of Bordetella pertussis binds to target cells via the alpha(M)beta(2) integrin (CD11b/CD18);Guermonprez;J. Exp. Med.,2001

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