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ProteomicsA hybrid TIM complex mediates protein import into hydrogenosomes of Trichomonas vaginalis
Hydrogenosomes are a specific type of mitochondria that have adapted for life under anaerobiosis. Limited availability of oxygen has resulted in the loss of the membrane- associated respiratory chain, and consequently in the generation of minimal inner membrane potential (), and inefficient ATP synt...
ORGANISM(S): Trichomonas vaginalis 
2024-06-16 | PXD047649 | Pride
Presequence translocase-associated motor Parasite Protein import machinery Tim22 complex Mitochondria Tim23 complex Trichomonas vaginalis Hydrogenosomes 
TranscriptomicsTranscription profiling of Trichomonas vaginalis cultured in the low-iron and high-iron conditions
Transcriptional changes of Trichomonas vaginalis cultured in the low-iron and high-iron conditions.
ORGANISM(S): Trichomonas vaginalis 
2010-07-24 | E-MTAB-126 | biostudies-arrayexpress
UnknownAnaerobic peroxisomes in Mastigamoeba balamuthi.
Not available
S-EPMC6994998 | biostudies-literature
ProteomicsDynamic T. vaginalis secretome and secretion of β-amalyses
During infection of the urogenital tract, the parasite Trichomonas vaginalis is challenged by factors such as nutrient limitation, the host immune response and coexistence with other members of the microbial fauna. Thus establishment of trichomonad infection depends on multifactorial host-parasite i...
ORGANISM(S): Trichomonas vaginalis 
2017-12-19 | PXD007034 | Pride
Trichomonas vaginalis Secretome 
ProteomicsEvolution Anaerobic peroxisome in Mastigamoeba balamuthi
Adaptation of eukaryotic cells to anaerobic condition is reflected by deep changes in mitochondrial metabolism and their functional reduction. The most modified types of mitochondria are hydrogenosomes that generate molecular hydrogen with concomitant ATP synthesis and mitosome that completely lost ...
ORGANISM(S): Mastigamoeba balamuthi ATTC 30984 
2020-03-04 | PXD014205 | Pride
Mastigamoeba balamuthi Peroxisome Anaerobiosis 
ProteomicsTranslocase of the Outer Membrane (TOM complex) of hydrogenosomes in Trichomonas vaginalis
Mitochondria originated from α-proteobacterial endosymbionts, and the endosymbiont-to-organelle transition is tightly linked to the establishment of protein import pathways. The initial import of most proteins is mediated by the translocase of the outer membrane (TOM). Although TOM is common to all ...
ORGANISM(S): Trichomonas vaginalis G3 
2019-01-07 | PXD010850 | Pride
Mitochondria Tom complex Trichomonas vaginalis Protein import/translocation Hydrogenosomes 
ProteomicsProteomic analysis of Trichomonas vaginalis phagolysosome, lysosomal targeting, and unconventional secretion of cysteine peptidases
Lysosomes represent a central degradative compartment of eukaryotes, yet little is known about biogenesis and function of this organelle in parasitic protists. Whereas the mannose-6 phosphate (M6P)-dependent system is dominant for lysosomal targeting in metazoans, oligosaccharide independent sorting...
ORGANISM(S): Trichomonas vaginalis 
2023-07-26 | PXD027545 | Pride
Trichomonas vaginalis Glycosylation Mannose-6-phosphate receptor Phagolysosome Cysteine peptidase Proteome 
UnknownMicrosatellite polymorphism in the sexually transmitted human pathogen Trichomonas vaginalis indicates a genetically diverse parasite.
Not available
S-EPMC2974001 | biostudies-literature
UnknownProteomic Analysis of Trichomonas vaginalis Phagolysosome, Lysosomal Targeting, and Unconventional Secretion of Cysteine Peptidases.
Not available
S-EPMC8717582 | biostudies-literature
UnknownTriplet-pore structure of a highly divergent TOM complex of hydrogenosomes in Trichomonas vaginalis.
Not available
S-EPMC6334971 | biostudies-literature
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