about
Thioredoxin and glutathione systems differ in parasitic and free-living platyhelminthsLinked thioredoxin-glutathione systems in platyhelminth parasites: alternative pathways for glutathione reduction and deglutathionylation.Discovering Echinococcus granulosus thioredoxin glutathione reductase inhibitors through site-specific dynamic combinatorial chemistry.Selenoproteins of African trypanosomes are dispensable for parasite survival in a mammalian host.Platyhelminth mitochondrial and cytosolic redox homeostasis is controlled by a single thioredoxin glutathione reductase and dependent on selenium and glutathione.Inhibition of Tapeworm Thioredoxin and Glutathione Pathways by an Oxadiazole N-Oxide Leads to Reduced Mesocestoides vogae Infection Burden in Mice.A New Class of Thioredoxin-Related Protein Able to Bind Iron-Sulfur Clusters.Polyamine-Based Thiols in Trypanosomatids: Evolution, Protein Structural Adaptations, and Biological Functions.A glutaredoxin in the mitochondrial intermembrane space has stage-specific functions in the thermo-tolerance and proliferation of African trypanosomes.The lineage-specific, intrinsically disordered N-terminal extension of monothiol glutaredoxin 1 from trypanosomes contains a regulatory regionPhagocyte-specific S100 proteins in the local response to the Echinococcus granulosus larvaAn essential thioredoxin-type protein of Trypanosoma brucei acts as redox-regulated mitochondrial chaperone.Kinetic studies reveal a key role of a redox-active glutaredoxin in the evolution of the thiol-redox metabolism of trypanosomatid parasitesProduction of Recombinant Trypanosoma cruzi Antigens in Leishmania tarentolae
P50
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P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Mariana Bonilla
@ast
Mariana Bonilla
@en
Mariana Bonilla
@es
Mariana Bonilla
@nl
type
label
Mariana Bonilla
@ast
Mariana Bonilla
@en
Mariana Bonilla
@es
Mariana Bonilla
@nl
prefLabel
Mariana Bonilla
@ast
Mariana Bonilla
@en
Mariana Bonilla
@es
Mariana Bonilla
@nl
P106
P21
P31
P4012
P496
0000-0002-9206-345X