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Functional aspects of the solution structure and dynamics of PAF--a highly-stable antifungal protein from Penicillium chrysogenum.

Batta G, Barna T, Gáspári Z, Sándor S, Kövér KE, Binder U, Sarg B, Kaiserer L, Chhillar AK, Eigentler A, Leiter E, Hegedüs N, Pócsi I, Lindner H, Marx F.

FEBS J. 2009 May;276(10):2875-90. doi: 10.1111/j.1742-4658.2009.07011.x.


Antifungal protein PAF severely affects the integrity of the plasma membrane of Aspergillus nidulans and induces an apoptosis-like phenotype.

Leiter E, Szappanos H, Oberparleiter C, Kaiserer L, Csernoch L, Pusztahelyi T, Emri T, Pócsi I, Salvenmoser W, Marx F.

Antimicrob Agents Chemother. 2005 Jun;49(6):2445-53.


Proper folding of the antifungal protein PAF is required for optimal activity.

Marx F, Salvenmoser W, Kaiserer L, Graessle S, Weiler-Görz R, Zadra I, Oberparleiter C.

Res Microbiol. 2005 Jan-Feb;156(1):35-46.


Active internalization of the Penicillium chrysogenum antifungal protein PAF in sensitive aspergilli.

Oberparleiter C, Kaiserer L, Haas H, Ladurner P, Andratsch M, Marx F.

Antimicrob Agents Chemother. 2003 Nov;47(11):3598-601.


Characterization of the Penicillium chrysogenum antifungal protein PAF.

Kaiserer L, Oberparleiter C, Weiler-Görz R, Burgstaller W, Leiter E, Marx F.

Arch Microbiol. 2003 Sep;180(3):204-10. Epub 2003 Jul 10.


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