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Data for identification of GPI-anchored peptides and ω-sites in cancer cell lines

We present data obtained using a focused proteomics approach to identify the glycosylphosphatidylinositol (GPI)-anchored peptides in 19 human cancer cell lines. GPI-anchored proteins (GPI-APs), which localize to the outer leaflet of the membrane microdomains commonly referred to as lipid rafts play...

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Detalles Bibliográficos
Autores principales: Masuishi, Yusuke, Kimura, Yayoi, Arakawa, Noriaki, Hirano, Hisashi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4838930/
https://www.ncbi.nlm.nih.gov/pubmed/27141528
http://dx.doi.org/10.1016/j.dib.2016.04.001
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author Masuishi, Yusuke
Kimura, Yayoi
Arakawa, Noriaki
Hirano, Hisashi
author_facet Masuishi, Yusuke
Kimura, Yayoi
Arakawa, Noriaki
Hirano, Hisashi
author_sort Masuishi, Yusuke
collection PubMed
description We present data obtained using a focused proteomics approach to identify the glycosylphosphatidylinositol (GPI)-anchored peptides in 19 human cancer cell lines. GPI-anchored proteins (GPI-APs), which localize to the outer leaflet of the membrane microdomains commonly referred to as lipid rafts play important roles in diverse biological processes. Due to the complex structure of the GPI-anchor moiety, it has been difficult to identify GPI-anchored peptide sequences on the proteomic scale by database searches using tools such as MASCOT. Here we provide data from 73 ω-sites derived from 49 GPI-APs in 19 human cancer cell lines. This article contains data related to the research article entitled “Identification of glycosylphosphatidylinositol-anchored proteins and ω-sites using TiO(2)-based affinity purification followed by hydrogen fluoride treatment” (Masuishi et al., 2016) [1].
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spelling pubmed-48389302016-05-02 Data for identification of GPI-anchored peptides and ω-sites in cancer cell lines Masuishi, Yusuke Kimura, Yayoi Arakawa, Noriaki Hirano, Hisashi Data Brief Data Article We present data obtained using a focused proteomics approach to identify the glycosylphosphatidylinositol (GPI)-anchored peptides in 19 human cancer cell lines. GPI-anchored proteins (GPI-APs), which localize to the outer leaflet of the membrane microdomains commonly referred to as lipid rafts play important roles in diverse biological processes. Due to the complex structure of the GPI-anchor moiety, it has been difficult to identify GPI-anchored peptide sequences on the proteomic scale by database searches using tools such as MASCOT. Here we provide data from 73 ω-sites derived from 49 GPI-APs in 19 human cancer cell lines. This article contains data related to the research article entitled “Identification of glycosylphosphatidylinositol-anchored proteins and ω-sites using TiO(2)-based affinity purification followed by hydrogen fluoride treatment” (Masuishi et al., 2016) [1]. Elsevier 2016-04-08 /pmc/articles/PMC4838930/ /pubmed/27141528 http://dx.doi.org/10.1016/j.dib.2016.04.001 Text en © 2016 The Authors http://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 Data Article
Masuishi, Yusuke
Kimura, Yayoi
Arakawa, Noriaki
Hirano, Hisashi
Data for identification of GPI-anchored peptides and ω-sites in cancer cell lines
title Data for identification of GPI-anchored peptides and ω-sites in cancer cell lines
title_full Data for identification of GPI-anchored peptides and ω-sites in cancer cell lines
title_fullStr Data for identification of GPI-anchored peptides and ω-sites in cancer cell lines
title_full_unstemmed Data for identification of GPI-anchored peptides and ω-sites in cancer cell lines
title_short Data for identification of GPI-anchored peptides and ω-sites in cancer cell lines
title_sort data for identification of gpi-anchored peptides and ω-sites in cancer cell lines
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4838930/
https://www.ncbi.nlm.nih.gov/pubmed/27141528
http://dx.doi.org/10.1016/j.dib.2016.04.001
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