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Targeting the glycoproteome

Despite numerous original publications describing the structural complexity of N- and O-linked glycans on glycoproteins, only very few answer the basic question of which particular glycans are linked to which amino acid residues along the polypeptide chain. Such structural information is of fundamen...

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Detalles Bibliográficos
Autores principales: Nilsson, Jonas, Halim, Adnan, Grahn, Ammi, Larson, Göran
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3552370/
https://www.ncbi.nlm.nih.gov/pubmed/22886069
http://dx.doi.org/10.1007/s10719-012-9438-6
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author Nilsson, Jonas
Halim, Adnan
Grahn, Ammi
Larson, Göran
author_facet Nilsson, Jonas
Halim, Adnan
Grahn, Ammi
Larson, Göran
author_sort Nilsson, Jonas
collection PubMed
description Despite numerous original publications describing the structural complexity of N- and O-linked glycans on glycoproteins, only very few answer the basic question of which particular glycans are linked to which amino acid residues along the polypeptide chain. Such structural information is of fundamental importance for understanding the biological roles of complex glycosylations as well as deciphering their non-template driven biosynthesis. This review focuses on presenting and commenting on recent strategies, specifically aimed at identifying the glycoproteome of cultured cells and biological samples, using targeted and global enrichment procedures and utilizing the high resolution power, high through-put capacity and complementary fragmentation techniques of tandem mass spectrometry. The goal is to give an update of this emerging field of protein and glyco-sciences and suggest routes to bridge the data gap between the two aspects of glycoprotein characteristics, i.e. glycan structures and their attachment sites.
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spelling pubmed-35523702013-01-24 Targeting the glycoproteome Nilsson, Jonas Halim, Adnan Grahn, Ammi Larson, Göran Glycoconj J Article Despite numerous original publications describing the structural complexity of N- and O-linked glycans on glycoproteins, only very few answer the basic question of which particular glycans are linked to which amino acid residues along the polypeptide chain. Such structural information is of fundamental importance for understanding the biological roles of complex glycosylations as well as deciphering their non-template driven biosynthesis. This review focuses on presenting and commenting on recent strategies, specifically aimed at identifying the glycoproteome of cultured cells and biological samples, using targeted and global enrichment procedures and utilizing the high resolution power, high through-put capacity and complementary fragmentation techniques of tandem mass spectrometry. The goal is to give an update of this emerging field of protein and glyco-sciences and suggest routes to bridge the data gap between the two aspects of glycoprotein characteristics, i.e. glycan structures and their attachment sites. Springer US 2012-08-11 2013 /pmc/articles/PMC3552370/ /pubmed/22886069 http://dx.doi.org/10.1007/s10719-012-9438-6 Text en © The Author(s) 2012 https://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Article
Nilsson, Jonas
Halim, Adnan
Grahn, Ammi
Larson, Göran
Targeting the glycoproteome
title Targeting the glycoproteome
title_full Targeting the glycoproteome
title_fullStr Targeting the glycoproteome
title_full_unstemmed Targeting the glycoproteome
title_short Targeting the glycoproteome
title_sort targeting the glycoproteome
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3552370/
https://www.ncbi.nlm.nih.gov/pubmed/22886069
http://dx.doi.org/10.1007/s10719-012-9438-6
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