Protein O-Galnac Glycosylation: Most Complex and Differentially Regulated PTM

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Standard

Protein O-Galnac Glycosylation : Most Complex and Differentially Regulated PTM. / Joshi, Hiren J.; Steentoft, Catharina; Schjoldager, Katrine T.B.G.; Vakhrushev, Sergey Y.; Wandall, Hans H.; Clausen, Henrik.

Glycoscience: Biology and Medicine. Springer, 2015. p. 1049-1064.

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Harvard

Joshi, HJ, Steentoft, C, Schjoldager, KTBG, Vakhrushev, SY, Wandall, HH & Clausen, H 2015, Protein O-Galnac Glycosylation: Most Complex and Differentially Regulated PTM. in Glycoscience: Biology and Medicine. Springer, pp. 1049-1064. https://doi.org/10.1007/978-4-431-54841-6_63

APA

Joshi, H. J., Steentoft, C., Schjoldager, K. T. B. G., Vakhrushev, S. Y., Wandall, H. H., & Clausen, H. (2015). Protein O-Galnac Glycosylation: Most Complex and Differentially Regulated PTM. In Glycoscience: Biology and Medicine (pp. 1049-1064). Springer. https://doi.org/10.1007/978-4-431-54841-6_63

Vancouver

Joshi HJ, Steentoft C, Schjoldager KTBG, Vakhrushev SY, Wandall HH, Clausen H. Protein O-Galnac Glycosylation: Most Complex and Differentially Regulated PTM. In Glycoscience: Biology and Medicine. Springer. 2015. p. 1049-1064 https://doi.org/10.1007/978-4-431-54841-6_63

Author

Joshi, Hiren J. ; Steentoft, Catharina ; Schjoldager, Katrine T.B.G. ; Vakhrushev, Sergey Y. ; Wandall, Hans H. ; Clausen, Henrik. / Protein O-Galnac Glycosylation : Most Complex and Differentially Regulated PTM. Glycoscience: Biology and Medicine. Springer, 2015. pp. 1049-1064

Bibtex

@inbook{87bd457f6bbc4e849e7d6bf6e4b80647,
title = "Protein O-Galnac Glycosylation: Most Complex and Differentially Regulated PTM",
abstract = "Recent advances in O-glycoproteomics strategies have resulted in substantial progress in identification and characterization of O-glycoproteins, and this is particularly true for the mucin-type or GalNAc-type O-glycosylation. Highthroughput mass spectrometric methods have produced large quantities of O-glycosite data, allowing us to finally produce more comprehensive maps of sites of O-glycosylation. In this chapter we discuss this explosion of data, the implication it has upon our understanding of the nature of GalNAc-type O-glycosylation, and the development of bioinformatic tools to aid our comprehension of the O-glycoproteome. As tools to aid comprehension, predictors of O-glycosylation such as NetOGlyc4.0 allow us to make estimates about the nature of the complete O-glycoproteome, while tools such as the Glyco Domain Viewer help us focus on individual proteins and better understand the protein context of the glycosites. We explore some of the concepts that surround these bioinformatics tools and provide some perspective as to how these tools can be further developed to support the study of glycosylation in biology and medicine.",
keywords = "Bioinformatics, GALNT, ISOGlyP, NetOGlyc4.0, Simple Cell",
author = "Joshi, {Hiren J.} and Catharina Steentoft and Schjoldager, {Katrine T.B.G.} and Vakhrushev, {Sergey Y.} and Wandall, {Hans H.} and Henrik Clausen",
year = "2015",
month = jan,
day = "1",
doi = "10.1007/978-4-431-54841-6_63",
language = "English",
isbn = "9784431548409",
pages = "1049--1064",
booktitle = "Glycoscience",
publisher = "Springer",
address = "Switzerland",

}

RIS

TY - CHAP

T1 - Protein O-Galnac Glycosylation

T2 - Most Complex and Differentially Regulated PTM

AU - Joshi, Hiren J.

AU - Steentoft, Catharina

AU - Schjoldager, Katrine T.B.G.

AU - Vakhrushev, Sergey Y.

AU - Wandall, Hans H.

AU - Clausen, Henrik

PY - 2015/1/1

Y1 - 2015/1/1

N2 - Recent advances in O-glycoproteomics strategies have resulted in substantial progress in identification and characterization of O-glycoproteins, and this is particularly true for the mucin-type or GalNAc-type O-glycosylation. Highthroughput mass spectrometric methods have produced large quantities of O-glycosite data, allowing us to finally produce more comprehensive maps of sites of O-glycosylation. In this chapter we discuss this explosion of data, the implication it has upon our understanding of the nature of GalNAc-type O-glycosylation, and the development of bioinformatic tools to aid our comprehension of the O-glycoproteome. As tools to aid comprehension, predictors of O-glycosylation such as NetOGlyc4.0 allow us to make estimates about the nature of the complete O-glycoproteome, while tools such as the Glyco Domain Viewer help us focus on individual proteins and better understand the protein context of the glycosites. We explore some of the concepts that surround these bioinformatics tools and provide some perspective as to how these tools can be further developed to support the study of glycosylation in biology and medicine.

AB - Recent advances in O-glycoproteomics strategies have resulted in substantial progress in identification and characterization of O-glycoproteins, and this is particularly true for the mucin-type or GalNAc-type O-glycosylation. Highthroughput mass spectrometric methods have produced large quantities of O-glycosite data, allowing us to finally produce more comprehensive maps of sites of O-glycosylation. In this chapter we discuss this explosion of data, the implication it has upon our understanding of the nature of GalNAc-type O-glycosylation, and the development of bioinformatic tools to aid our comprehension of the O-glycoproteome. As tools to aid comprehension, predictors of O-glycosylation such as NetOGlyc4.0 allow us to make estimates about the nature of the complete O-glycoproteome, while tools such as the Glyco Domain Viewer help us focus on individual proteins and better understand the protein context of the glycosites. We explore some of the concepts that surround these bioinformatics tools and provide some perspective as to how these tools can be further developed to support the study of glycosylation in biology and medicine.

KW - Bioinformatics

KW - GALNT

KW - ISOGlyP

KW - NetOGlyc4.0

KW - Simple Cell

U2 - 10.1007/978-4-431-54841-6_63

DO - 10.1007/978-4-431-54841-6_63

M3 - Book chapter

AN - SCOPUS:84938909759

SN - 9784431548409

SP - 1049

EP - 1064

BT - Glycoscience

PB - Springer

ER -

ID: 231897821