Determination of glycosylation sites and site-specific heterogeneity in glycoproteins

Hyun Joo An, John W. Froehlich, Carlito B Lebrilla

Research output: Contribution to journalArticle

129 Citations (Scopus)

Abstract

Glycosylation is one of the most common post-translational modifications (PTMs) of proteins. At least 50% of human proteins are glycosylated with some estimates being as high as 70%. Glycoprotein analysis requires determining both the sites of glycosylation as well as the glycan structures associated with each site. Recent advances have led to the development of new analytical methods that employ mass spectrometry extensively making it possible to obtain the glycosylation site and the site microheterogeneity. These tools will be important for the eventual development of glycoproteomics.

Original languageEnglish (US)
Pages (from-to)421-426
Number of pages6
JournalCurrent Opinion in Chemical Biology
Volume13
Issue number4
DOIs
StatePublished - Oct 2009

Fingerprint

Glycosylation
Glycoproteins
Post Translational Protein Processing
Mass spectrometry
Polysaccharides
Mass Spectrometry
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Analytical Chemistry

Cite this

Determination of glycosylation sites and site-specific heterogeneity in glycoproteins. / An, Hyun Joo; Froehlich, John W.; Lebrilla, Carlito B.

In: Current Opinion in Chemical Biology, Vol. 13, No. 4, 10.2009, p. 421-426.

Research output: Contribution to journalArticle

An, Hyun Joo ; Froehlich, John W. ; Lebrilla, Carlito B. / Determination of glycosylation sites and site-specific heterogeneity in glycoproteins. In: Current Opinion in Chemical Biology. 2009 ; Vol. 13, No. 4. pp. 421-426.
@article{cd4450b3e41347e4a03ed85648245543,
title = "Determination of glycosylation sites and site-specific heterogeneity in glycoproteins",
abstract = "Glycosylation is one of the most common post-translational modifications (PTMs) of proteins. At least 50{\%} of human proteins are glycosylated with some estimates being as high as 70{\%}. Glycoprotein analysis requires determining both the sites of glycosylation as well as the glycan structures associated with each site. Recent advances have led to the development of new analytical methods that employ mass spectrometry extensively making it possible to obtain the glycosylation site and the site microheterogeneity. These tools will be important for the eventual development of glycoproteomics.",
author = "An, {Hyun Joo} and Froehlich, {John W.} and Lebrilla, {Carlito B}",
year = "2009",
month = "10",
doi = "10.1016/j.cbpa.2009.07.022",
language = "English (US)",
volume = "13",
pages = "421--426",
journal = "Current Opinion in Chemical Biology",
issn = "1367-5931",
publisher = "Elsevier Limited",
number = "4",

}

TY - JOUR

T1 - Determination of glycosylation sites and site-specific heterogeneity in glycoproteins

AU - An, Hyun Joo

AU - Froehlich, John W.

AU - Lebrilla, Carlito B

PY - 2009/10

Y1 - 2009/10

N2 - Glycosylation is one of the most common post-translational modifications (PTMs) of proteins. At least 50% of human proteins are glycosylated with some estimates being as high as 70%. Glycoprotein analysis requires determining both the sites of glycosylation as well as the glycan structures associated with each site. Recent advances have led to the development of new analytical methods that employ mass spectrometry extensively making it possible to obtain the glycosylation site and the site microheterogeneity. These tools will be important for the eventual development of glycoproteomics.

AB - Glycosylation is one of the most common post-translational modifications (PTMs) of proteins. At least 50% of human proteins are glycosylated with some estimates being as high as 70%. Glycoprotein analysis requires determining both the sites of glycosylation as well as the glycan structures associated with each site. Recent advances have led to the development of new analytical methods that employ mass spectrometry extensively making it possible to obtain the glycosylation site and the site microheterogeneity. These tools will be important for the eventual development of glycoproteomics.

UR - http://www.scopus.com/inward/record.url?scp=70349113034&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=70349113034&partnerID=8YFLogxK

U2 - 10.1016/j.cbpa.2009.07.022

DO - 10.1016/j.cbpa.2009.07.022

M3 - Article

C2 - 19700364

AN - SCOPUS:70349113034

VL - 13

SP - 421

EP - 426

JO - Current Opinion in Chemical Biology

JF - Current Opinion in Chemical Biology

SN - 1367-5931

IS - 4

ER -