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dc.contributor.authorMurphy, Paul V.
dc.date.accessioned2015-12-10T16:36:16Z
dc.date.available2015-12-10T16:36:16Z
dc.date.issued2015-01-22
dc.identifier.citationAndre, S,Kaltner, H,Manning, JC,Murphy, PV,Gabius, HJ (2015) 'Lectins: getting familiar with translators of the sugar code'. Molecules (Basel, Switzerland), 20 :1788-1823.en_IE
dc.identifier.issn1420-3049
dc.identifier.urihttp://hdl.handle.net/10379/5383
dc.descriptionJournal articleen_IE
dc.description.abstractThe view on the significance of the presence of glycans in glycoconjugates is undergoing a paradigmatic change. Initially mostly considered to be rather inert and passive, the concept of the sugar code identifies glycans as highly versatile platform to store information. Their chemical properties endow carbohydrates to form oligomers with unsurpassed structural variability. Owing to their capacity to engage in hydrogen (and coordination) bonding and C-H/pi-interactions these "code words" can be "read" (in Latin, legere) by specific receptors. A distinct class of carbohydrate-binding proteins are the lectins. More than a dozen protein folds have developed carbohydrate-binding capacity in vertebrates. Taking galectins as an example, distinct expression patterns are traced. The availability of labeled endogenous lectins facilitates monitoring of tissue reactivity, extending the scope of lectin histochemistry beyond that which traditionally involved plant lectins. Presentation of glycan and its cognate lectin can be orchestrated, making a glycan-based effector pathway in growth control of tumor and activated T cells possible. In order to unravel the structural basis of lectin specificity for particular glycoconjugates mimetics of branched glycans and programmable models of cell surfaces are being developed by strategic combination of lectin research with synthetic and supramolecular chemistry.en_IE
dc.description.sponsorshipVerein zur Förderung des biologisch-technologischen Fortschritts in der Medizin e.V. (Heidelberg, Germany); Initial Training Network (EC funding by contract no. 317297 [GLYCOPHARM])en_IE
dc.formatapplication/pdfen_IE
dc.language.isoenen_IE
dc.publisherMDPIen_IE
dc.relation.ispartofMolecules (Basel, Switzerland)en
dc.subjectAdhesionen_IE
dc.subjectGangliosideen_IE
dc.subjectGlycoclusteren_IE
dc.subjectGlycosylationen_IE
dc.subjectKidneyen_IE
dc.subjectSialylationen_IE
dc.subjectGalactoside-binding lectinen_IE
dc.subjectAdhesion/growth-regulatory galectinsen_IE
dc.subjectStructure activity profilesen_IE
dc.subjectPancreatic carcinoma modelen_IE
dc.subjectAcid-free ceruloplasminen_IE
dc.subjectT-cell apoptosisen_IE
dc.subjectCancer in-vitroen_IE
dc.subjectColon canceren_IE
dc.subjectFunctional glycomicsen_IE
dc.subjectPolyporus squamosusen_IE
dc.titleLectins: getting familiar with translators of the sugar codeen_IE
dc.typeArticleen_IE
dc.date.updated2015-12-08T08:43:04Z
dc.identifier.doi10.3390/molecules20021788
dc.local.publishedsourcehttp://dx.doi.org/10.3390/molecules20021788en_IE
dc.description.peer-reviewedpeer-reviewed
dc.contributor.funder|~|
dc.internal.rssid9391508
dc.local.contactPaul Murphy, School Of Chemistry, Room 236, Arts/Science Building, Nui Galway. 2465 Email: paul.v.murphy@nuigalway.ie
dc.local.copyrightcheckedNo Molecules is an open access Journal.
dc.local.versionPUBLISHED
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