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Carolin M Hoppe

Researcher at Hannover Medical School

Publications -  5
Citations -  82

Carolin M Hoppe is an academic researcher from Hannover Medical School. The author has contributed to research in topics: Intracellular parasite & Thrombospondin. The author has an hindex of 4, co-authored 5 publications receiving 61 citations.

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Apicomplexan C-Mannosyltransferases Modify Thrombospondin Type I-containing Adhesins of the TRAP Family.

TL;DR: It is demonstrated that also the micronemal protein MIC2 secreted by Toxoplasma gondii tachyzoites is C-hexosylated, which may be a common modification in this phylum of apicomplexan parasites.
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Depletion of UDP-Glucose and UDP-Galactose Using a Degron System Leads to Growth Cessation of Leishmania major.

TL;DR: Under destabilising conditions, the absence of both UGP and USP resulted in depletion of UDP-Glc and UDP-Gal and led to growth cessation and cell death, suggesting that either or both of these metabolites is/are essential.
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O-Fucosylation of thrombospondin-like repeats is required for processing of microneme protein 2 and for efficient host cell invasion by Toxoplasma gondii tachyzoites

TL;DR: O-fucosylation of TSRs is required for efficient processing of MIC2 and for normal parasite invasion, consistent with the recent demonstration that Plasmodium falciparum Δpofut2 strain has decreased virulence and also support a conserved role for this glycosylation pathway in quality control of T SR-containing proteins in eukaryotes.
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Leishmania major UDP-sugar pyrophosphorylase salvages galactose for glycoconjugate biosynthesis

TL;DR: In this paper, the role of UDP-sugar pyrophosphorylase (USP) of Leishmania major in UDP-galactose biosynthesis was evaluated. But USP was shown to be dispensable for growth and glycoconjugate biosynthesis under standard growth conditions.
Posted ContentDOI

O-fucosylation of thrombospondin-like repeats is required for processing of MIC2 and for efficient host cell invasion by Toxoplasma gondii tachyzoites

TL;DR: Results, which show O-fucosylation of TSRs is required for efficient processing of MIC2 and for normal parasite invasion, are consistent with the recent demonstration that P. falciparum Δpofut2 has decreased virulence and support a conserved role for this glycosylation pathway in quality control of T SRs in eukaryotes.