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dc.rights.licenseOpen Access
dc.contributor.authorSong, Yuefan
dc.contributor.authorZhang, Fuming
dc.contributor.authorLinhardt, Robert J.
dc.date2021
dc.date.accessioned2022-06-23T04:46:02Z
dc.date.available2022-06-23T04:46:02Z
dc.date.issued2021-02-01
dc.identifier.citationAnalysis of the glycosaminoglycan chains of proteoglycans, Y. Song, F. Zhang, R. J. Linhardt, Journal of Histochemistry & Cytochemistry, 69, 121 –135, 2021.
dc.identifier.issn15515044
dc.identifier.issn221554
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5409
dc.identifier.urihttps://doi.org/10.1369/0022155420937154
dc.descriptionJournal of Histochemistry & Cytochemistry, 69, 121 –135
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractGlycosaminoglycans (GAGs) are heterogeneous, negatively charged, macromolecules that are found in animal tissues. Based on the form of component sugar, GAGs have been categorized into four different families: heparin/heparan sulfate, chondroitin/dermatan sulfate, keratan sulfate, and hyaluronan. GAGs engage in biological pathway regulation through their interaction with protein ligands. Detailed structural information on GAG chains is required to further understanding of GAG–ligand interactions. However, polysaccharide sequencing has lagged behind protein and DNA sequencing due to the non-template-driven biosynthesis of glycans. In this review, we summarize recent progress in the analysis of GAG chains, specifically focusing on techniques related to mass spectroscopy (MS), including separation techniques coupled to MS, tandem MS, and bioinformatics software for MS spectrum interpretation. Progress in the use of other structural analysis tools, such as nuclear magnetic resonance (NMR) and hyphenated techniques, is included to provide a comprehensive perspective.
dc.description.sponsorshipNational Institutes of Health
dc.languageen_US
dc.language.isoENG
dc.publisherSage
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofJournal of Histochemistry and Cytochemistry
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleAnalysis of the glycosaminoglycan chains of proteoglycans
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1369/0022155420937154
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages121-135
rpi.description.volume69


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