2011
DOI: 10.4155/fmc.10.290
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Profiling of Influenza Viruses by High-Throughput Carbohydrate Membrane Array

Abstract: This carbohydrate membrane array represents a convenient, reliable and low-cost method to examine the carbohydrate-binding features of various proteins, high-throughput drug screening and the glycan-binding surveillance of influenza viruses.

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Cited by 9 publications
(1 citation statement)
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“…(Horlacher and Seeberger 2008; Krishnamoorthy and Mahal 2009; Lee and Shin 2005; Oyelaran and Gildersleeve 2009; Park et al 2008; Park and Shin 2007; Pei et al 2007c; Tyagi et al 2010; Wu et al 2009) Glycan arrays have thus been used to identify proteins involved in cancer metastasis, (Hatakeyama et al 2009) enzymes involved in wound healing, (Saravanan et al 2010) and glycans modulating T cell death; (Earl et al 2010) to evaluate blood serum glycan binding, (Huflejt et al 2009) antibodies towards HIV, (Luallen et al 2010) and antibodies for use in cancer treatment; (Huang et al 2006; Nagre et al 2010; Sawada et al 2011) to evaluate the binding specificity of glycan-binding proteins and receptors; (Feinberg et al 2010; Gout et al 2010; Hoorelbeke et al 2011; Horlacher et al 2011; Pipirou et al 2011; Porter et al 2010; Singh et al 2009) to investigate the binding specificities of disease causing bacteria, (Hu et al 2011) viruses, (Krishnamoorthy et al 2009; Neu et al 2010; Nilsson et al 2011) and fungi;(Chachadi et al 2011) as well as for the in-depth investigation of avian and swine influenza viruses. (de Vries et al 2011; Lao et al 2011; Liao et al 2010; Pappas et al 2010; Stevens et al 2010; Xu et al 2010) Although such glycan array methodologies yield significant knowledge of glycan interactions, there are still obstacles to overcome in the production of universally valid array methodologies. Since the produced glycan surfaces aim to mimic those of cells, proteins or other biomolecules, the glycan presentation is important to achieve correct binding.…”
Section: Introductionmentioning
confidence: 99%
“…(Horlacher and Seeberger 2008; Krishnamoorthy and Mahal 2009; Lee and Shin 2005; Oyelaran and Gildersleeve 2009; Park et al 2008; Park and Shin 2007; Pei et al 2007c; Tyagi et al 2010; Wu et al 2009) Glycan arrays have thus been used to identify proteins involved in cancer metastasis, (Hatakeyama et al 2009) enzymes involved in wound healing, (Saravanan et al 2010) and glycans modulating T cell death; (Earl et al 2010) to evaluate blood serum glycan binding, (Huflejt et al 2009) antibodies towards HIV, (Luallen et al 2010) and antibodies for use in cancer treatment; (Huang et al 2006; Nagre et al 2010; Sawada et al 2011) to evaluate the binding specificity of glycan-binding proteins and receptors; (Feinberg et al 2010; Gout et al 2010; Hoorelbeke et al 2011; Horlacher et al 2011; Pipirou et al 2011; Porter et al 2010; Singh et al 2009) to investigate the binding specificities of disease causing bacteria, (Hu et al 2011) viruses, (Krishnamoorthy et al 2009; Neu et al 2010; Nilsson et al 2011) and fungi;(Chachadi et al 2011) as well as for the in-depth investigation of avian and swine influenza viruses. (de Vries et al 2011; Lao et al 2011; Liao et al 2010; Pappas et al 2010; Stevens et al 2010; Xu et al 2010) Although such glycan array methodologies yield significant knowledge of glycan interactions, there are still obstacles to overcome in the production of universally valid array methodologies. Since the produced glycan surfaces aim to mimic those of cells, proteins or other biomolecules, the glycan presentation is important to achieve correct binding.…”
Section: Introductionmentioning
confidence: 99%