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ProteomicsN-linked glycoproteins from exosome-depleted excretory-secretory products of fourth-stage larval Angiostrongylus cantonensis promotes alternative activation of macrophages through metabolic reprogramming by the PI3K-Akt pathway
Angiostrongylus cantonensis (AC), which parasitizes in the brain of the non-permissive host, such as mouse and human, is an etiologic agent of eosinophilic meningitis. Excretory-secretory (ES) products play an important role in the interaction between parasites and hosts’ immune responses. Inflammat...
ORGANISM(S): Angiostrongylus cantonensis 
2021-07-28 | PXD025218 | Pride
Exosome-depleted excretory-secretory products N-linked glycoproteins Mechanism Angiostrongylus cantonensis Macrophage polarization 
GenomicsN-linked glycoproteins from exosome-depleted excretory-secretory products of fourth-stage larval Angiostrongylus cantonensis promotes alternative activation of macrophages through metabolic reprogramming by the PI3K-Akt pathway
N-linked glycoproteins from exosome-depleted excretory-secretory products of fourth-stage larval Angiostrongylus cantonensis promotes alternative activation of macrophages through metabolic reprogramming by the PI3K-Akt pathway
PRJNA732598 | ENA
TranscriptomicsN-linked glycoproteins from exosome-depleted excretory-secretory products of fourth-stage larval Angiostrongylus cantonensis promotes alternative activation of macrophages through metabolic reprogramming by the PI3K-Akt pathway
In this study, Angiostrongylus cantonensis (AC), which parasitizes in the brain of the non-permissive host, such as mouse and human, is an etiologic agent of eosinophilic meningitis. Excretory-secretory (ES) products play an important role in the interaction between parasites and hosts’ immune respo...
ORGANISM(S): Mus musculus 
2021-07-05 | GSE175497 | GEO
UnknownExosome-Depleted Excretory-Secretory Products of the Fourth-Stage Larval Angiostrongylus cantonensis Promotes Alternative Activation of Macrophages Through Metabolic Reprogramming by the PI3K-Akt Pathway.
Not available
S-EPMC8343011 | biostudies-literature
UnknownProteomic analysis of exosome-like vesicles from Fasciola gigantica adult worm provides support for new vaccine targets against fascioliasis.
Not available
S-EPMC9921414 | biostudies-literature
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