Abstract
Introduction: Protein glycosylation is recognized as an important post-translational modification, with specific substructures having significant effects on protein folding, conformation, distribution, stability and activity. However, due to the structural complexity of glycans, elucidating glycan structure-function relationships is demanding. The fine detail of glycan structures attached to proteins (including sequence, branching, linkage and anomericity) is still best analysed after the glycans are released from the purified or mixture of glycoproteins (glycomics). The technologies currently available for glycomics are becoming streamlined and standardized and many features of protein glycosylation can now be determined using instruments available in most protein analytical laboratories.
Areas covered: This review focuses on the current glycomics technologies being commonly used for the analysis of the microheterogeneity of monosaccharide composition, sequence, branching and linkage of released N- and O-linked glycans that enable the determination of precise glycan structural determinants presented on secreted proteins and on the surface of all cells.
Expert commentary: Several emerging advances in these technologies enabling glycomics analysis are discussed. The technological and bioinformatics requirements to be able to accurately assign these precise glycan features at biological levels in a disease context are assessed.
| Language | English |
|---|---|
| Pages | 165-182 |
| Number of pages | 18 |
| Journal | Expert Review of Proteomics |
| Volume | 15 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1 Feb 2018 |
Fingerprint
Keywords
- disease glycomics
- glycan analysis
- glycan structure
- Glycomics
- mass spectrometry
Cite this
}
Human disease glycomics : technology advances enabling protein glycosylation analysis – part 1. / Everest-Dass, Arun V.; Moh, Edward S.X.; Ashwood, Christopher; Shathili, Abdulrahman M.M.; Packer, Nicolle H.
In: Expert Review of Proteomics, Vol. 15, No. 2, 01.02.2018, p. 165-182.Research output: Contribution to journal › Review article › Research › peer-review
TY - JOUR
T1 - Human disease glycomics
T2 - Expert Review of Proteomics
AU - Everest-Dass, Arun V.
AU - Moh, Edward S.X.
AU - Ashwood, Christopher
AU - Shathili, Abdulrahman M.M.
AU - Packer, Nicolle H.
PY - 2018/2/1
Y1 - 2018/2/1
N2 - Introduction: Protein glycosylation is recognized as an important post-translational modification, with specific substructures having significant effects on protein folding, conformation, distribution, stability and activity. However, due to the structural complexity of glycans, elucidating glycan structure-function relationships is demanding. The fine detail of glycan structures attached to proteins (including sequence, branching, linkage and anomericity) is still best analysed after the glycans are released from the purified or mixture of glycoproteins (glycomics). The technologies currently available for glycomics are becoming streamlined and standardized and many features of protein glycosylation can now be determined using instruments available in most protein analytical laboratories. Areas covered: This review focuses on the current glycomics technologies being commonly used for the analysis of the microheterogeneity of monosaccharide composition, sequence, branching and linkage of released N- and O-linked glycans that enable the determination of precise glycan structural determinants presented on secreted proteins and on the surface of all cells. Expert commentary: Several emerging advances in these technologies enabling glycomics analysis are discussed. The technological and bioinformatics requirements to be able to accurately assign these precise glycan features at biological levels in a disease context are assessed.
AB - Introduction: Protein glycosylation is recognized as an important post-translational modification, with specific substructures having significant effects on protein folding, conformation, distribution, stability and activity. However, due to the structural complexity of glycans, elucidating glycan structure-function relationships is demanding. The fine detail of glycan structures attached to proteins (including sequence, branching, linkage and anomericity) is still best analysed after the glycans are released from the purified or mixture of glycoproteins (glycomics). The technologies currently available for glycomics are becoming streamlined and standardized and many features of protein glycosylation can now be determined using instruments available in most protein analytical laboratories. Areas covered: This review focuses on the current glycomics technologies being commonly used for the analysis of the microheterogeneity of monosaccharide composition, sequence, branching and linkage of released N- and O-linked glycans that enable the determination of precise glycan structural determinants presented on secreted proteins and on the surface of all cells. Expert commentary: Several emerging advances in these technologies enabling glycomics analysis are discussed. The technological and bioinformatics requirements to be able to accurately assign these precise glycan features at biological levels in a disease context are assessed.
KW - disease glycomics
KW - glycan analysis
KW - glycan structure
KW - Glycomics
KW - mass spectrometry
UR - http://www.scopus.com/inward/record.url?scp=85041239467&partnerID=8YFLogxK
U2 - 10.1080/14789450.2018.1421946
DO - 10.1080/14789450.2018.1421946
M3 - Review article
VL - 15
SP - 165
EP - 182
JO - Expert Review of Proteomics
JF - Expert Review of Proteomics
SN - 1478-9450
IS - 2
ER -