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Giulia Bandini

Researcher at Boston University

Publications -  24
Citations -  381

Giulia Bandini is an academic researcher from Boston University. The author has contributed to research in topics: Fucosyltransferase & Fucose. The author has an hindex of 11, co-authored 22 publications receiving 299 citations. Previous affiliations of Giulia Bandini include University of Dundee.

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Differential Roles for Inner Membrane Complex Proteins across Toxoplasma gondii and Sarcocystis neurona Development.

TL;DR: Across asexually dividing Toxoplasma stages, IMC7 is present exclusively in the mother’s cytoskeleton, whereas IMC1 and IMC3 are both present in mother and daughter cytoskeletons, and stage- and development-specific behaviors indicate that their functions are uniquely tailored to each life stage requirement.
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CRISPR/Cas9 and glycomics tools for Toxoplasma glycobiology

TL;DR: The roles of specific glycans in Toxoplasma are investigated using a double-CRISPR/Cas9 strategy, adapted MS-based glycomics workflows to test for effects on glycan formation, and infected fibroblast monolayers to assess cellular effects.
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O-fucosylated glycoproteins form assemblies in close proximity to the nuclear pore complexes of Toxoplasma gondii.

TL;DR: The discovery that assemblies of O-fucosylated proteins localize to thenuclear membrane of Toxoplasma gondii, particularly in proximity to the nuclear pore complexes (NPCs), andalyses of the AAL-enriched fraction indicate that AAL binds O-linked fucose added to Ser/Thr residues present in or adjacent to Ser-rich domains (SRDs).
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Biosynthesis of GDP-fucose and Other Sugar Nucleotides in the Blood Stages of Plasmodium falciparum

TL;DR: The in silico functional reconstruction of the parasite metabolic pathways obtained from the P. falciparum annotated genome exposes new active biosynthetic routes crucial for further glycosylation reactions.
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Phosphoglucomutase is absent in Trypanosoma brucei and redundantly substituted by phosphomannomutase and phospho-N-acetylglucosamine mutase

TL;DR: Analysis of sugar nucleotide levels in parasites with TbPMM or TbPAGM knocked down by RNA interference suggests that, in vivo, PGM activity is catalysed by both enzymes, which explains why, uniquely, T. brucei has been able to lose its PGM gene.