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Ivan Hrdy

Researcher at Charles University in Prague

Publications -  16
Citations -  1524

Ivan Hrdy is an academic researcher from Charles University in Prague. The author has contributed to research in topics: Gene & Hydrogenosome. The author has an hindex of 9, co-authored 11 publications receiving 1412 citations.

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Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis

Jane M. Carlton, +64 more
- 12 Jan 2007 - 
TL;DR: The genome sequence of the protist Trichomonas vaginalis predicts previously unknown functions for the hydrogenosome, which support a common evolutionary origin of this unusual organelle with mitochondria.
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Trichomonas hydrogenosomes contain the NADH dehydrogenase module of mitochondrial complex I

TL;DR: Recruitment of complex I subunits into a H2-producing pathway provides evidence that mitochondria and hydrogenosomes are aerobic and anaerobic homologues of the same endosymbiotically derived organelle.
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Hepcidin, the hormone of iron metabolism, is bound specifically to α-2-macroglobulin in blood

TL;DR: The demonstration that alpha2-M is the hePCidin transporter could lead to better understanding of hepcidin physiology, methods for its sensitive measurement and the development of novel drugs for the treatment of iron-related diseases.
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Mitochondrial-type assembly of FeS centers in the hydrogenosomes of the amitochondriate eukaryote Trichomonas vaginalis

TL;DR: It is shown that hydrogenosomes of Trichomonas vaginalis, a human genitourinary parasite, contain a key enzyme of FeS center biosynthesis, cysteine desulfurase (TviscS-2), which is phylogenetically related to its mitochondrial homologs.
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Mechanisms of in vitro development of resistance to metronidazole in Trichomonas vaginalis.

TL;DR: Development of resistance against metronidazole and mechanisms responsible for this process were studied in a sexually transmitted pathogen of humans, Trichomonas vaginalis, suggesting involvement of the oxidative decarboxylation of malate in hydrogenosomes, catalysed by NAD(+)-dependent malic enzyme and subsequent transfer of reduced equivalents to the drug via NADH:ferredoxin oxidoreductase and ferredoxin.