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- Volume 8, Issue 4, 2011
Current Proteomics - Volume 8, Issue 4, 2011
Volume 8, Issue 4, 2011
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Editorial
More LessGlycomics and glycoproteomics continue to be highly dynamic and interesting research areas due to the needs to comprehensively understand the biological attributes of glycosylation in many important biological functions such as immune response, cell development, cellular differentiation/adhesion, and host-pathogen interactions. Moreover, aberrant glycosylation for decades has been recognized as the attri Read More
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Lectin Techniques for Glycoproteomics
More LessOne of the greatest challenges of the post-genomic and post-proteomic era is to understand the role of posttranslational modifications in global biological systems. Protein glycosylation is one of the most frequent posttranslational modifications but has been poorly studied in global proteomes because of analytical challenges associated with glycan structural characterization. In recent years, technical advances in the study of p Read More
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Monosaccharide Compositional Analysis of Glycoproteins Using Liquid Chromatography-Mass Spectrometry
Authors: Loubna A. Hammad and Yehia MechrefEffective and accurate analysis of free monosaccharides and monosaccharides bound to glycoconjugates, including glycoproteins and glycolipids have been achieved through the development of different analytical methods. Although all of these analytical methods appears to be applicable to the quantification of monosaccharides, quantification through coupling of liquid chromatography to mass spectrometry (LC-MS) is curre Read More
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Recent Mass Spectrometric Based Methods in Quantitative N-linked Glycoproteomics
Authors: Kathryn R. Rebecchi, Carrie L. Woodin and Heather DesaireGlycoproteomics is an emerging field focused on analysis of glycosylated proteins. Glycoproteins, especially N-linked glycoproteins, have been shown to be increasingly important in biomarker analyses and biopharmaceutical drug development. Thus, relative quantitation of glycoproteins by mass spectrometry is surfacing as a powerful tool. Examples of quantitative glycoproteomic analyses include monitoring changes in prot Read More
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Perspective and Review of Mass Spectrometric Based Sulfoglycomics of N-Linked and O-Linked Oligosaccharides
Authors: Diarmuid Kenny, Catherine A. Hayes, Chunseng Jin and Niclas G. KarlssonThe research area of glycomics is maturing and it is realized that it is as difficult to identify the relevance of glycosylation amongst biological house-keeping as it is with any of the other omics techniques. This review focuses on sulfoglycomics of N-linked and O-linked oligosaccharides to identify relevant biological glycomics questions. The review describes how sulfated oligosaccharides have been analyzed in the past, with the foc Read More
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Structural Characterization of Carbohydrates by Fourier Transform Tandem Mass Spectrometry
Authors: Wen Zhou and Kristina HakanssonFourier transform tandem mass spectrometry (MS/MS) provides high mass accuracy, high sensitivity, and analytical versatility and has therefore emerged as an indispensable tool for structural elucidation of biomolecules. Glycosylation is one of the most common posttranslational modifications, occurring in ∼50% of proteins. However, due to the structural diversity of carbohydrates, arising from non-template drive Read More
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Bioinformatic Approaches in Glycomics and Glycoproteomics
Authors: Anoop M. Mayampurath, Chuan-Yih Yu, Yehia Mechref and Haixu TangGlycans play multiple functional roles in living cells, from acting as energy sources to mediating intracellular signaling and cell-cell communications. Glycosylation is a common post-translational modification (PTM), known to occur in over 50% of human proteins. Understanding the structure of glycans, the nature and functions of protein glycosylation along with studying interactions between glycans and glycan-binding proteins Read More
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Analysis of Glycosaminoglycans Using Mass Spectrometry
Authors: Gregory O. Staples and Joseph ZaiaThe glycosaminoglycans (GAGs) are linear polysaccharides expressed on animal cell surfaces and in extracellular matrices. Their biosynthesis is under complex control and confers a domain structure that is essential to their ability to bind to protein partners. Key to understanding the functions of GAGs are methods to determine accurately and rapidly patterns of sulfation, acetylation and uronic acid epimerization that Read More
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Volumes & issues
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Volume 21 (2024)
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Volume 20 (2023)
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Volume 19 (2022)
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Volume 18 (2021)
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Volume 17 (2020)
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Volume 16 (2019)
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Volume 15 (2018)
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Volume 14 (2017)
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Volume 13 (2016)
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Volume 12 (2015)
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Volume 11 (2014)
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Volume 10 (2013)
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Volume 9 (2012)
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Volume 8 (2011)
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Volume 7 (2010)
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Volume 6 (2009)
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Volume 5 (2008)
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Volume 4 (2007)
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Volume 3 (2006)
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Volume 2 (2005)
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Volume 1 (2004)
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