Highly glycosylated MUC1 mediates high affinity L-selectin binding at the human endometrial surface

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dc.citation.articleNumber50en_US
dc.citation.journalTitleJournal of Nanobiotechnologyen_US
dc.citation.volumeNumber19en_US
dc.contributor.authorFrancis, Lewis W.en_US
dc.contributor.authorYao, Seydou N.en_US
dc.contributor.authorPowell, Lydia C.en_US
dc.contributor.authorGriffiths, Seanen_US
dc.contributor.authorBerquand, Alexanderen_US
dc.contributor.authorPiasecki, Thomasen_US
dc.contributor.authorHowe, Williamen_US
dc.contributor.authorGazze, Andrea S.en_US
dc.contributor.authorFarach-Carson, Mary C.en_US
dc.contributor.authorConstantinou, Pamelaen_US
dc.contributor.authorCarson, Danielen_US
dc.contributor.authorMargarit, Laviniaen_US
dc.contributor.authorGonzalez, Deyaen_US
dc.contributor.authorConlan, R. Stevenen_US
dc.date.accessioned2021-03-09T15:44:37Zen_US
dc.date.available2021-03-09T15:44:37Zen_US
dc.date.issued2021en_US
dc.description.abstractSialyl-Lewis X/L-selectin high affinity binding interactions between transmembrane O-glycosylated mucins proteins and the embryo have been implicated in implantation processes within the human reproductive system. However, the adhesive properties of these mucins at the endometrial cell surface are difficult to resolve due to known discrepancies between in vivo models and the human reproductive system and a lack of sensitivity in current in vitro models. To overcome these limitations, an in vitro model of the human endometrial epithelial was interrogated with single molecule force spectroscopy (SMFS) to delineate the molecular configurations of mucin proteins that mediate the high affinity L-selectin binding required for human embryo implantation.en_US
dc.identifier.citationFrancis, Lewis W., Yao, Seydou N., Powell, Lydia C., et al.. "Highly glycosylated MUC1 mediates high affinity L-selectin binding at the human endometrial surface." <i>Journal of Nanobiotechnology,</i> 19, (2021) Springer Nature: https://doi.org/10.1186/s12951-021-00793-9.en_US
dc.identifier.digitals12951-021-00793-9en_US
dc.identifier.doihttps://doi.org/10.1186/s12951-021-00793-9en_US
dc.identifier.urihttps://hdl.handle.net/1911/110162en_US
dc.language.isoengen_US
dc.publisherSpringer Natureen_US
dc.rightsThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.en_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/.en_US
dc.titleHighly glycosylated MUC1 mediates high affinity L-selectin binding at the human endometrial surfaceen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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