A conserved dimorphism-regulating histidine kinase controls the dimorphic switching in Paracoccidioides brasiliensis.
Chaves, Alison F A; Navarro, Marina V; Castilho, Daniele G; Calado, Juliana C P; Conceição, Palloma M; Batista, Wagner L.
FEMS Yeast Res
; 16(5)2016 08.
Artigo em Inglês | MEDLINE | ID: mdl-27268997
Alternative oxidase plays an important role in Paracoccidioides brasiliensis cellular homeostasis and morphological transition.
α-(1,4)-Amylase, but not α- and ß-(1,3)-glucanases, may be responsible for the impaired growth and morphogenesis of Paracoccidioides brasiliensis induced by N-glycosylation inhibition.
Morphological heterogeneity of Paracoccidioides brasiliensis: relevance of the Rho-like GTPase PbCDC42.
Molecular and morphological data support the existence of a sexual cycle in species of the genus Paracoccidioides.
Distinct chitinases are expressed during various growth phases of the human pathogen Paracoccidioides brasiliensis.
The cell wall of Paracoccidioides brasiliensis: insights from its transcriptome.
Analysis of Paracoccidioides secreted proteins reveals fructose 1,6-bisphosphate aldolase as a plasminogen-binding protein.
Hsp90 regulates Paracoccidioides brasiliensis proliferation and ROS levels under thermal stress and cooperates with calcineurin to control yeast to mycelium dimorphism.
Virulence factors of Paracoccidioides brasiliensis as therapeutic targets: a review.
Characterization of the Paracoccidioides beta-1,3-glucanosyltransferase family.