Wanzhen Feng

Hydrophobic cue-induced appressorium formation depends on MoSep1-mediated MoRgs7 phosphorylation and internalization in Magnaporthe oryzae

Distinctive phosphorylation pattern during mitotic exit network (MEN) regulation is important for the development and pathogenicity of Magnaporthe oryzae

Balancing of the mitotic exit network and cell wall integrity signaling governs the development and pathogenicity in Magnaporthe oryzae

The rice blast fungus MoRgs1 functioning in cAMP signaling and pathogenicity is regulated by casein kinase MoCk2 phosphorylation and modulated by membrane protein MoEmc2

Shedding light on autophagy coordinating with cell wall integrity signaling to govern pathogenicity of <i>Magnaporthe oryzae</i>

Histone acetyltransferase MoHat1 acetylates autophagy-related proteins MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and pathogenicity in <i>Magnaporthe oryzae</i>

MoMip11, a MoRgs7‐interacting protein, functions as a scaffolding protein to regulate cAMP signaling and pathogenicity in the rice blast fungus <i>Magnaporthe oryzae</i>

New findings on phosphodiesterases, MoPdeH and MoPdeL, in <i>Magnaporthe oryzae</i> revealed by structural analysis