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Galectin-1 as a fusion partner for the production of soluble and folded human β-1,4-galactosyltransferase-T7 in E. coli

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TLDR
It is shown for the first time that a small soluble lectin, human galectin-1, one member of a large galECTin family, can function as a fusion partner to produce soluble folded recombinant human glycosyltransferase, beta-1-4-galactosyltransfer enzyme-7 (beta4Gal-T7), in E. coli.
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This article is published in Biochemical and Biophysical Research Communications.The article was published on 2010-04-09 and is currently open access. It has received 16 citations till now. The article focuses on the topics: Fusion protein & TEV protease.

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Journal ArticleDOI

Cellular Disulfide Bond Formation in Bioactive Peptides and Proteins

TL;DR: The main pathways that catalyze disulfide bond formation in peptides and proteins in prokaryotes and eukaryotes are remarkably similar and share several mechanistic features.
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Locally anchoring enzymes to tissues via extracellular glycan recognition

TL;DR: G3-mediated anchoring to common tissue glycans is expected to be broadly applicable for improving local pharmacokinetics of various existing and emerging enzyme drugs.
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Crystal Structures of β-1,4-Galactosyltransferase 7 Enzyme Reveal Conformational Changes and Substrate Binding

TL;DR: This study for the first time reveals the molecular interactions between a glycosyltransferase and its donor and acceptor substrates bound together in the same crystal structure and clearly suggests an SN2 type catalytic mechanism for the β4GalT7 enzyme.
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Enzyme and microbial technology for synthesis of bioactive oligosaccharides: an update.

TL;DR: A review of the pros and cons of galactose-containing oligosaccharides and the use of Leloir glycosyltransferases provides an updated view on the status of biocatalysis in this important field.
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Molecular characterization of β1,4-galactosyltransferase 7 genetic mutations linked to the progeroid form of Ehlers―Danlos syndrome (EDS)

TL;DR: It was shown that R270C substitution strongly reduced β4GalT7 affinity towards xyloside acceptor, thus affecting GAG chains formation, and this study establishes the molecular basis for β4 GalT7 defects associated with altered GAG synthesis in EDS.
References
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Journal ArticleDOI

Cation-π interactions in structural biology

TL;DR: In this paper, an energy-based criterion for selecting significant sidechain pairs was used to identify and evaluate cation-pi interactions in protein structures, and it was clearly demonstrated that, when a cationic sidechain (Lys or Arg) is near an aromatic side chain (Phe, Tyr, or Trp), the geometry is biased toward one that would experience a favorable cationpi interaction.
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Recombinant protein folding and misfolding in Escherichia coli.

TL;DR: The past 20 years have seen enormous progress in the understanding of the mechanisms used by the enteric bacterium Escherichia coli to promote protein folding, support protein translocation and handle protein misfolding, and these insights have been exploited to tackle the problems of inclusion body formation, proteolytic degradation and disulfide bond generation.
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Galectins as modulators of tumour progression

TL;DR: Current research indicates that galectins have important roles in cancer; they contribute to neoplastic transformation, tumour cell survival, angiogenesis and tumour metastasis, and might have a key role helping tumours to escape immune surveillance.
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Advanced genetic strategies for recombinant protein expression in Escherichia coli.

TL;DR: Issues addressed include expression systems in general, selection of host strain, mRNA stability, codon bias, inclusion body formation and prevention, fusion protein technology and site-specific proteolysis, compartment directed secretion and finally co-overexpression technology.
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