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dc.rights.licenseCC BY — Creative Commons Attribution
dc.contributor.authorZhao, Xue
dc.contributor.authorYang, Bo
dc.contributor.authorSolakyildirim, Kemal
dc.contributor.authorJoo, Eun Ji
dc.contributor.authorToida, Toshihiko
dc.contributor.authorHigashi, Kyohei
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorLi, Lingyun
dc.date2013
dc.date.accessioned2022-06-21T18:41:56Z
dc.date.available2022-06-21T18:41:56Z
dc.date.issued2013-10-11
dc.identifier.citationSequence analysis and domain motifs in the decorin glycosaminoglycan chain, X. Zhao, B. Yang, K. Solakylidirim, E.-J. Joo, T. Toida, K. Higashi, R. J. Linhardt, L. Li, Journal of Biological Chemistry, 288, 9226-9237, 2013.
dc.identifier.issn1083351X
dc.identifier.issn219258
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5103
dc.identifier.urihttps://doi.org/10.1074/jbc.A112.437236
dc.descriptionJournal of Biological Chemistry, 288, 9226-9237
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.abstractDecorin proteoglycan is comprised of a core protein containing a single O-linked dermatan sulfate/chondroitin sulfate glycosaminoglycan (GAG) chain. Although the sequence of the decorin core protein is determined by the gene encoding its structure, the structure of its GAG chain is determined in the Golgi. The recent application of modern MS to bikunin, a far simpler chondroitin sulfate proteoglycans, suggests that it has a single or small number of defined sequences. On this basis, a similar approach to sequence the decorin of porcine skin much larger and more structurally complex dermatan sulfate/chondroitin sulfate GAG chain was undertaken. This approach resulted in information on the consistency/variability of its linkage region at the reducing end of the GAG chain, its iduronic acid-rich domain, glucuronic acid-rich domain, and non-reducing end. A general motif for the porcine skin decorin GAG chain was established. A single small decorin GAG chain was sequenced using MS/MS analysis. The data obtained in the study suggest that the decorin GAG chain has a small or a limited number of sequences.
dc.languageen_US
dc.language.isoENG
dc.publisherThe American Society for Biochemistry and Molecular Biology (ASBMB) and Elsevier
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofJournal of Biological Chemistry
dc.relation.urihttps://harc.rpi.edu/
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleSequence analysis and domain motifs in the decorin glycosaminoglycan chainen_US
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.accessRightsOpen Access
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1074/jbc.A112.437236
dc.rights.holderCC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
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.pages29713
rpi.description.volume288


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CC BY — Creative Commons Attribution
Except where otherwise noted, this item's license is described as CC BY — Creative Commons Attribution