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Maria Panico

Researcher at Imperial College London

Publications -  134
Citations -  11064

Maria Panico is an academic researcher from Imperial College London. The author has contributed to research in topics: Glycosylation & Glycoprotein. The author has an hindex of 52, co-authored 127 publications receiving 10549 citations.

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Sequence and structure of a human glucose transporter

TL;DR: Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and ery Throcyte transporters are highly homologous and may be identical.
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N-Linked Glycosylation in Campylobacter jejuni and Its Functional Transfer into E. coli

TL;DR: It is demonstrated that a functional N-linked glycosylation pathway could be transferred into Escherichia coli and opened up the possibility of engineering permutations of recombinant glycan structures for research and industrial applications.
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Identification of xanthurenic acid as the putative inducer of malaria development in the mosquito

TL;DR: It is shown that low concentrations of xanthurenic acid can act together with pH to induce gametogenesis in vitro, and could form the basis of the rational development of new methods of interrupting the transmission of malaria using drugs or new refractory mosquito genotypes to block parasitegametogenesis.
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Isolation and characterization of human calcitonin gene-related peptide

TL;DR: The human peptide differs significantly from the predicted rat calcitonin gene-related peptide structure in four positions in the amino acid sequence (three effecting charge changes), and the presence of a disulphide bridge and an amide, surmised in the rat work, is proven in the hCGRP molecule as discussed by the authors.
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Human sperm binding is mediated by the sialyl-Lewis(x) oligosaccharide on the zona pellucida.

TL;DR: In this paper, the sialyl-Lewis(x) sequence [NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc], a well-known selectin ligand, is the most abundant terminal sequence on the N- and O-glycans of human ZP.