About: Assignment of coronavirus spike protein site-specific glycosylation using GlycReSoft

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Assignment of coronavirus spike protein site-specific glycosylation using GlycReSoft
Creator	Klein, Joshua Zaia, Joseph
source	BioRxiv
abstract	Widely-available LC-MS instruments and methods allow users to acquire glycoproteomics data. Complex glycans, however, add a dimension of complexity to the data analysis workflow. In a sense, complex glycans are post-translationally modified post-translational modifications, reflecting a series of biosynthetic reactions in the secretory pathway that are spatially and temporally regulated. One problem is that complex glycan is micro-heterogeneous, multiplying the complexity of the proteome. Another is that glycopeptide glycans undergo dissociation during tandem MS that must be considered for tandem MS interpretation algorithms and quantitative tools. Fortunately, there are a number of algorithmic tools available for analysis of glycoproteomics LC-MS data. We summarize the principles for glycopeptide data analysis and show use of our GlycReSoft tool to analyze SARS-CoV-2 spike protein site-specific glycosylation.
has issue date	2020-05-31(xsd:dateTime)
bibo:doi	10.1101/2020.05.31.125302
has license	biorxiv
sha1sum (hex)	9914dee9ae1a3eaf7e1d1aa016e1485bcf381aeb
schema:url	https://doi.org/10.1101/2020.05.31.125302
resource representing a document's title	Assignment of coronavirus spike protein site-specific glycosylation using GlycReSoft
schema:publication	bioRxiv
resource representing a document's body	covid:9914dee9ae1a3eaf7e1d1aa016e1485bcf381aeb#body_text
is schema:about of	named entity 'secretory pathway' named entity 'dimension' named entity 'data' named entity 'SARS-CoV-2' named entity 'protein' »more»

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