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Membrane-Pore Forming Characteristics of the Bordetella pertussis CyaA-Hemolysin Domain.
Toxins (Basel). 2015 Apr 30;7(5):1486-96. doi: 10.3390/toxins7051486.
Toxins (Basel). 2015.
PMID: 25941766
Free PMC article.
Functional significance of the highly conserved Glu(570) in the putative pore-forming helix 3 of the Bordetella pertussis haemolysin toxin.
Kurehong C, Powthongchin B, Thamwiriyasati N, Angsuthanasombat C.
Kurehong C, et al.
Toxicon. 2011 May;57(6):897-903. doi: 10.1016/j.toxicon.2011.03.010. Epub 2011 Mar 22.
Toxicon. 2011.
PMID: 21419155
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Functional importance of the Gly cluster in transmembrane helix 2 of the Bordetella pertussis CyaA-hemolysin: Implications for toxin oligomerization and pore formation.
Juntapremjit S, Thamwiriyasati N, Kurehong C, Prangkio P, Shank L, Powthongchin B, Angsuthanasombat C.
Juntapremjit S, et al. Among authors: kurehong c.
Toxicon. 2015 Nov;106:14-9. doi: 10.1016/j.toxicon.2015.09.006. Epub 2015 Sep 10.
Toxicon. 2015.
PMID: 26363293
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Functional Contributions of Positive Charges in the Pore-Lining Helix 3 of the Bordetella pertussis CyaA-Hemolysin to Hemolytic Activity and Ion-Channel Opening.
Kurehong C, Kanchanawarin C, Powthongchin B, Prangkio P, Katzenmeier G, Angsuthanasombat C.
Kurehong C, et al.
Toxins (Basel). 2017 Mar 16;9(3):109. doi: 10.3390/toxins9030109.
Toxins (Basel). 2017.
PMID: 28300777
Free PMC article.
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