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dc.contributor.authorWang, Linlin
dc.contributor.authorCummings, Richard D
dc.contributor.authorSmith, David F
dc.contributor.authorHuflejt, Margaret
dc.contributor.authorCampbell, Christopher T
dc.contributor.authorGildersleeve, Jeffrey C
dc.contributor.authorGerlach, Jared Q
dc.contributor.authorKilcoyne, Michelle
dc.contributor.authorJoshi, Lokesh
dc.contributor.authorSerna, Sonia
dc.contributor.authorReichardt, Niels-Christian
dc.contributor.authorParera Pera, Núria
dc.contributor.authorPieters, Roland J
dc.contributor.authorEng, William
dc.contributor.authorMahal, Lara K
dc.date.accessioned2018-09-20T16:28:06Z
dc.date.available2018-09-20T16:28:06Z
dc.date.issued2014-03-22
dc.identifier.citationWang, Linlin; Cummings, Richard D; Smith, David F; Huflejt, Margaret; Campbell, Christopher T; Gildersleeve, Jeffrey C; Gerlach, Jared Q; Kilcoyne, Michelle; Joshi, Lokesh; Serna, Sonia; Reichardt, Niels-Christian; Parera Pera, Núria; Pieters, Roland J; Eng, William; Mahal, Lara K (2014). Cross-platform comparison of glycan microarray formats. Glycobiology 24 (6), 507-517
dc.identifier.issn0959-6658,1460-2423
dc.identifier.urihttp://hdl.handle.net/10379/14370
dc.description.abstractCarbohydrates participate in almost every aspect of biology from protein sorting to modulating cell differentiation and cell-cell interactions. To date, the majority of data gathered on glycan expression has been obtained via analysis with either anti-glycan antibodies or lectins. A detailed understanding of the specificities of these reagents is critical to the analysis of carbohydrates in biological systems. Glycan microarrays are increasingly used to determine the binding specificity of glycan-binding proteins (GBPs). In this study, six different glycan microarray platforms with different modes of glycan presentation were compared using five well-known lectins; concanavalin A, Helix pomatia agglutinin, Maackia amurensis lectin I, Sambucus nigra agglutinin and wheat germ agglutinin. A new method (universal threshold) was developed to facilitate systematic comparisons across distinct array platforms. The strongest binders of each lectin were identified using the universal threshold across all platforms while identification of weaker binders was influenced by platform-specific factors including presentation of determinants, array composition and self-reported thresholding methods. This work compiles a rich dataset for comparative analysis of glycan array platforms and has important implications for the implementation of microarrays in the characterization of GBPs.
dc.publisherOxford University Press (OUP)
dc.relation.ispartofGlycobiology
dc.subjectcomparison
dc.subjectglycan microarray
dc.subjectlectin
dc.subjectpresentation
dc.subjectwheat-germ-agglutinin
dc.subjectcarbohydrate-protein interactions
dc.subjectlectin microarray
dc.subjectbinding-proteins
dc.subjectcell-binding
dc.subjectarray data
dc.subjectsurface
dc.subjectrecognition
dc.subjectdensity
dc.subjectspecificities
dc.titleCross-platform comparison of glycan microarray formats
dc.typeArticle
dc.identifier.doi10.1093/glycob/cwu019
dc.local.publishedsourcehttps://academic.oup.com/glycob/article-pdf/24/6/507/16657369/cwu019.pdf
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