Cargando…
OGP: A Repository of Experimentally Characterized O-glycoproteins to Facilitate Studies on O-glycosylation
Numerous studies on cancers, biopharmaceuticals, and clinical trials have necessitated comprehensive and precise analysis of protein O-glycosylation. However, the lack of updated and convenient databases deters the storage of and reference to emerging O-glycoprotein data. To resolve this issue, an O...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9039567/ https://www.ncbi.nlm.nih.gov/pubmed/33581334 http://dx.doi.org/10.1016/j.gpb.2020.05.003 |
_version_ | 1784694157364690944 |
---|---|
author | Huang, Jiangming Wu, Mengxi Zhang, Yang Kong, Siyuan Liu, Mingqi Jiang, Biyun Yang, Pengyuan Cao, Weiqian |
author_facet | Huang, Jiangming Wu, Mengxi Zhang, Yang Kong, Siyuan Liu, Mingqi Jiang, Biyun Yang, Pengyuan Cao, Weiqian |
author_sort | Huang, Jiangming |
collection | PubMed |
description | Numerous studies on cancers, biopharmaceuticals, and clinical trials have necessitated comprehensive and precise analysis of protein O-glycosylation. However, the lack of updated and convenient databases deters the storage of and reference to emerging O-glycoprotein data. To resolve this issue, an O-glycoprotein repository named OGP was established in this work. It was constructed with a collection of O-glycoprotein data from different sources. OGP contains 9354 O-glycosylation sites and 11,633 site-specific O-glycans mapping to 2133 O-glycoproteins, and it is the largest O-glycoprotein repository thus far. Based on the recorded O-glycosylation sites, an O-glycosylation site prediction tool was developed. Moreover, an OGP-based website is already available (https://www.oglyp.org/). The website comprises four specially designed and user-friendly modules: statistical analysis, database search, site prediction, and data submission. The first version of OGP repository and the website allow users to obtain various O-glycoprotein-related information, such as protein accession Nos., O-glycosylation sites, O-glycopeptide sequences, site-specific O-glycan structures, experimental methods, and potential O-glycosylation sites. O-glycosylation data mining can be performed efficiently on this website, which will greatly facilitate related studies. In addition, the database is accessible from OGP website (https://www.oglyp.org/download.php). |
format | Online Article Text |
id | pubmed-9039567 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-90395672022-04-27 OGP: A Repository of Experimentally Characterized O-glycoproteins to Facilitate Studies on O-glycosylation Huang, Jiangming Wu, Mengxi Zhang, Yang Kong, Siyuan Liu, Mingqi Jiang, Biyun Yang, Pengyuan Cao, Weiqian Genomics Proteomics Bioinformatics Database Numerous studies on cancers, biopharmaceuticals, and clinical trials have necessitated comprehensive and precise analysis of protein O-glycosylation. However, the lack of updated and convenient databases deters the storage of and reference to emerging O-glycoprotein data. To resolve this issue, an O-glycoprotein repository named OGP was established in this work. It was constructed with a collection of O-glycoprotein data from different sources. OGP contains 9354 O-glycosylation sites and 11,633 site-specific O-glycans mapping to 2133 O-glycoproteins, and it is the largest O-glycoprotein repository thus far. Based on the recorded O-glycosylation sites, an O-glycosylation site prediction tool was developed. Moreover, an OGP-based website is already available (https://www.oglyp.org/). The website comprises four specially designed and user-friendly modules: statistical analysis, database search, site prediction, and data submission. The first version of OGP repository and the website allow users to obtain various O-glycoprotein-related information, such as protein accession Nos., O-glycosylation sites, O-glycopeptide sequences, site-specific O-glycan structures, experimental methods, and potential O-glycosylation sites. O-glycosylation data mining can be performed efficiently on this website, which will greatly facilitate related studies. In addition, the database is accessible from OGP website (https://www.oglyp.org/download.php). Elsevier 2021-08 2021-02-10 /pmc/articles/PMC9039567/ /pubmed/33581334 http://dx.doi.org/10.1016/j.gpb.2020.05.003 Text en © 2021 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Database Huang, Jiangming Wu, Mengxi Zhang, Yang Kong, Siyuan Liu, Mingqi Jiang, Biyun Yang, Pengyuan Cao, Weiqian OGP: A Repository of Experimentally Characterized O-glycoproteins to Facilitate Studies on O-glycosylation |
title | OGP: A Repository of Experimentally Characterized O-glycoproteins to Facilitate Studies on O-glycosylation |
title_full | OGP: A Repository of Experimentally Characterized O-glycoproteins to Facilitate Studies on O-glycosylation |
title_fullStr | OGP: A Repository of Experimentally Characterized O-glycoproteins to Facilitate Studies on O-glycosylation |
title_full_unstemmed | OGP: A Repository of Experimentally Characterized O-glycoproteins to Facilitate Studies on O-glycosylation |
title_short | OGP: A Repository of Experimentally Characterized O-glycoproteins to Facilitate Studies on O-glycosylation |
title_sort | ogp: a repository of experimentally characterized o-glycoproteins to facilitate studies on o-glycosylation |
topic | Database |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9039567/ https://www.ncbi.nlm.nih.gov/pubmed/33581334 http://dx.doi.org/10.1016/j.gpb.2020.05.003 |
work_keys_str_mv | AT huangjiangming ogparepositoryofexperimentallycharacterizedoglycoproteinstofacilitatestudiesonoglycosylation AT wumengxi ogparepositoryofexperimentallycharacterizedoglycoproteinstofacilitatestudiesonoglycosylation AT zhangyang ogparepositoryofexperimentallycharacterizedoglycoproteinstofacilitatestudiesonoglycosylation AT kongsiyuan ogparepositoryofexperimentallycharacterizedoglycoproteinstofacilitatestudiesonoglycosylation AT liumingqi ogparepositoryofexperimentallycharacterizedoglycoproteinstofacilitatestudiesonoglycosylation AT jiangbiyun ogparepositoryofexperimentallycharacterizedoglycoproteinstofacilitatestudiesonoglycosylation AT yangpengyuan ogparepositoryofexperimentallycharacterizedoglycoproteinstofacilitatestudiesonoglycosylation AT caoweiqian ogparepositoryofexperimentallycharacterizedoglycoproteinstofacilitatestudiesonoglycosylation |