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

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dc.citation.articleNumber50
dc.citation.journalTitleJournal of Nanobiotechnology
dc.citation.volumeNumber19
dc.contributor.authorFrancis, Lewis W.
dc.contributor.authorYao, Seydou N.
dc.contributor.authorPowell, Lydia C.
dc.contributor.authorGriffiths, Sean
dc.contributor.authorBerquand, Alexander
dc.contributor.authorPiasecki, Thomas
dc.contributor.authorHowe, William
dc.contributor.authorGazze, Andrea S.
dc.contributor.authorFarach-Carson, Mary C.
dc.contributor.authorConstantinou, Pamela
dc.contributor.authorCarson, Daniel
dc.contributor.authorMargarit, Lavinia
dc.contributor.authorGonzalez, Deya
dc.contributor.authorConlan, R. Steven
dc.date.accessioned2021-03-09T15:44:37Z
dc.date.available2021-03-09T15:44:37Z
dc.date.issued2021
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.
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.
dc.identifier.digitals12951-021-00793-9
dc.identifier.doihttps://doi.org/10.1186/s12951-021-00793-9
dc.identifier.urihttps://hdl.handle.net/1911/110162
dc.language.isoeng
dc.publisherSpringer Nature
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.
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/.
dc.titleHighly glycosylated MUC1 mediates high affinity L-selectin binding at the human endometrial surface
dc.typeJournal article
dc.type.dcmiText
dc.type.publicationpublisher version
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