UniCarb-DB: A database resource for glycomic discovery

Catherine A. Hayes; Niclas G. Karlsson; Weston B. Struwe; Frederique Lisacek; Pauline M. Rudd; Nicolle H. Packer; Matthew P. Campbell

doi:10.1093/bioinformatics/btr137

UniCarb-DB: A database resource for glycomic discovery

Catherine A. Hayes, Niclas G. Karlsson, Weston B. Struwe, Frederique Lisacek, Pauline M. Rudd, Nicolle H. Packer, Matthew P. Campbell^*

^*Corresponding author for this work

Macquarie University BioFocus Research Centre

Research output: Contribution to journal › Article › peer-review

115 Citations (Scopus)

Abstract

Summary: Glycosylation is one of the most important post-translational modifications of proteins, known to be involved in pathogen recognition, innate immune response and protection of epithelial membranes. However, when compared to the tools and databases available for the processing of high-throughput proteomic data, the glycomic domain is severely lacking. While tools to assist the analysis of mass spectrometry (MS) and HPLC are continuously improving, there are few resources available to support liquid chromatography (LC)-MS/MS techniques for glycan structure profiling. Here, we present a platform for presenting oligosaccharide structures and fragment data characterized by LC-MS/MS strategies. The database is annotated with high-quality datasets and is designed to extend and reinforce those standards and ontologies developed by existing glycomics databases.

Original language	English
Article number	btr137
Pages (from-to)	1343-1344
Number of pages	2
Journal	Bioinformatics
Volume	27
Issue number	9
DOIs	https://doi.org/10.1093/bioinformatics/btr137
Publication status	Published - May 2011

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abstract = "Summary: Glycosylation is one of the most important post-translational modifications of proteins, known to be involved in pathogen recognition, innate immune response and protection of epithelial membranes. However, when compared to the tools and databases available for the processing of high-throughput proteomic data, the glycomic domain is severely lacking. While tools to assist the analysis of mass spectrometry (MS) and HPLC are continuously improving, there are few resources available to support liquid chromatography (LC)-MS/MS techniques for glycan structure profiling. Here, we present a platform for presenting oligosaccharide structures and fragment data characterized by LC-MS/MS strategies. The database is annotated with high-quality datasets and is designed to extend and reinforce those standards and ontologies developed by existing glycomics databases.",

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AU - Hayes, Catherine A.

AU - Karlsson, Niclas G.

AU - Struwe, Weston B.

AU - Lisacek, Frederique

AU - Rudd, Pauline M.

AU - Packer, Nicolle H.

AU - Campbell, Matthew P.

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AB - Summary: Glycosylation is one of the most important post-translational modifications of proteins, known to be involved in pathogen recognition, innate immune response and protection of epithelial membranes. However, when compared to the tools and databases available for the processing of high-throughput proteomic data, the glycomic domain is severely lacking. While tools to assist the analysis of mass spectrometry (MS) and HPLC are continuously improving, there are few resources available to support liquid chromatography (LC)-MS/MS techniques for glycan structure profiling. Here, we present a platform for presenting oligosaccharide structures and fragment data characterized by LC-MS/MS strategies. The database is annotated with high-quality datasets and is designed to extend and reinforce those standards and ontologies developed by existing glycomics databases.

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UniCarb-DB: A database resource for glycomic discovery

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