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dc.contributor.authorLi, L.
dc.contributor.authorLy, M.
dc.contributor.authorLinhardt, Robert J.
dc.date2012
dc.date.accessioned2022-06-23T04:11:24Z
dc.date.available2022-06-23T04:11:24Z
dc.date.issued2012
dc.identifier.citationProteoglycan Sequence, L. Li, M. Ly, R. J. Linhardt, Molecular BioSystems, 8, 1613–1625, 2012.
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5265
dc.identifier.urihttps://doi.org/10.1039/c2mb25021g
dc.descriptionMolecular BioSystems, 8, 1613–1625
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.abstractProteoglycans (PGs) are among the most structurally complex biomacromolecules in nature. They are present in all animal cells and frequently exert their critical biological functions through interactions with protein ligands and receptors. PGs are comprised of a core protein to which one or multiple, heterogeneous, and polydisperse glycosaminoglycan (GAG) chains are attached. Proteins, including the protein core of PGs, are now routinely sequenced either directly using proteomics or indirectly using molecular biology through their encoding DNA. The sequencing of the GAG component of PGs poses a considerably more difficult challenge because of the relatively underdeveloped state of glycomics and because the control of their biosynthesis in the endoplasmic reticulum and the Golgi is poorly understood and not believed to be template driven. Recently, the GAG chain of the simplest PG has been suggested to have a defined sequence based on its top-down Fourier transform mass spectral sequencing. This review examines the advances made over the past decade in the sequencing of GAG chains and the challenges the field face in sequencing complex PGs having critical biological functions in developmental biology and pathogenesis.
dc.languageen_US
dc.language.isoENG
dc.publisherRoyal Society of Chemistry
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleProteoglycan Sequence
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isVersionOfhttps://doi.org/10.1039/c2mb25021g
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)


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