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@article{Palma:2010,
author = {Palma, AS and Liu, Y and Muhle-Goll, C and Butters, TD and Zhang, Y and Childs, R and Chai, W and Feizi, T},
journal = {Methods Enzymol.},
pages = {265--286},
title = {Multifaceted approaches including neoglycolipid oligosaccharide microarrays to ligand discovery for malectin},
url = {pm:20816485},
volume = {478},
year = {2010}
}

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TY  - JOUR
AB  - In this chapter, we describe the key procedures for isolation of the oligosaccharides and the preparation of neoglycolipid probes together with expression of malectin that have enabled the discovery of the highly selective binding of this newly described protein in the endoplasmic reticulum (ER) to a diglucosyl high-mannose N-glycan. This is the first indication of a bioactivity for a diglucosyl high-mannose N-glycan of the type that occurs in the ER of eukaryotic cells and which is an intermediate in the early steps of the N-glycosylation pathway of nascent proteins. The malectin story is an example of a powerful convergence of disciplines in biological sciences: (i) developmental biology, (ii) bioinformatics, (iii) recombinant protein expression, (iv) protein structural studies, (v) glucan biochemistry, and (vi) drug-assisted engineering of oligosaccharide biosynthesis, culminating in (vii) oligosaccharide "designer" microarrays, to clinch the remarkable selectivity of the binding of this newly discovered ER protein. Thus, the way is open to the identification of the role of malectin in the N-glycosylation pathway
AU  - Palma,AS
AU  - Liu,Y
AU  - Muhle-Goll,C
AU  - Butters,TD
AU  - Zhang,Y
AU  - Childs,R
AU  - Chai,W
AU  - Feizi,T
EP  - 286
PY  - 2010///
SP  - 265
TI  - Multifaceted approaches including neoglycolipid oligosaccharide microarrays to ligand discovery for malectin
T2  - Methods Enzymol.
UR  - pm:20816485
VL  - 478
ER  -

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