Citation

BibTex format

@article{Liu:2015:10.1016/j.dib.2015.11.014,
author = {Liu, Y and Cecilio, NT and Carvalho, FC and Roque, Barreira MC and Feizi, T},
doi = {10.1016/j.dib.2015.11.014},
journal = {Data in Brief},
pages = {1035--1047},
title = {Glycan microarray analysis of the carbohydrate-recognition specificity of native and recombinant forms of the lectin ArtinM},
url = {http://dx.doi.org/10.1016/j.dib.2015.11.014},
volume = {5},
year = {2015}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - This article contains data related to the researc.h article entitled “Yeast-derived ArtinM shares structure, carbohydrate recognition, and biological effects with native ArtinM” by Cecílio et al. (2015) [1]. ArtinM, a D-mannose-binding lectin isolated from the seeds of Artocarpus heterophyllus, exerts immunomodulatory and regenerative activities through its Carbohydrate Recognition Domain (CRD) (Souza et al., 2013; Mariano et al., 2014 [2] and [3]). The limited availability of the native lectin (n-ArtinM) led us to characterize a recombinant form of the protein, obtained by expression in Saccharomyces cerevisiae (y-ArtinM). We compared the carbohydrate-binding specificities of y-ArtinM and n-ArtinM by analyzing the binding of biotinylated preparations of the two lectin forms using a neoglycolipid (NGL)-based glycan microarray. Data showed that y-ArtinM mirrored the specificity exhibited by n-ArtinM.
AU - Liu,Y
AU - Cecilio,NT
AU - Carvalho,FC
AU - Roque,Barreira MC
AU - Feizi,T
DO - 10.1016/j.dib.2015.11.014
EP - 1047
PY - 2015///
SN - 2352-3409
SP - 1035
TI - Glycan microarray analysis of the carbohydrate-recognition specificity of native and recombinant forms of the lectin ArtinM
T2 - Data in Brief
UR - http://dx.doi.org/10.1016/j.dib.2015.11.014
UR - http://hdl.handle.net/10044/1/28054
VL - 5
ER -