β Scribed by Weston B. Struwe, Eoin F.J. Cosgrave (auth.), Raymond Owens, Joanne Nettleship (eds.)
No coin nor oath required. For personal study only.
It has been predicted that nearly half of all human proteins are glycosylated indicating the significance of glycoproteins in human health and disease. For example, the glycans attached to proteins have emerged as important biomarkers in the diagnosis of diseases such as cancers and play a significant role in how pathogenic viruses gain entry into human cells. The study of glycoproteins has now become a truly proteomic science. In the last few years, technology developments including in silico methods, high throughput separation and detection techniques have accelerated the characterization of glycoproteins in cells and tissues. Glyco-engineering coupled to rapid recombinant protein production has facilitated the determination of glycoprotein structures key to exploring and exploiting their functional roles. Each chapter in this volume is written by experts in the field and together provide a review of the state of the art in the emerging field of glycoproteomics.
Front Matter....Pages i-x
Glycoproteomics in Health and Disease....Pages 1-38
Glyco-engineering of Fc Glycans to Enhance the Biological Functions of Therapeutic IgGs....Pages 39-58
Bioinformatics Databases and Applications Available for Glycobiology and Glycomics....Pages 59-90
Lectin Microarrays: Simple Tools for the Analysis of Complex Glycans....Pages 91-102
The Application of High Throughput Mass Spectrometry to the Analysis of Glycoproteins....Pages 103-125
Solutions to the Glycosylation Problem for Low- and High-Throughput Structural Glycoproteomics....Pages 127-158
Role of Glycoproteins in VirusβHuman Cell Interactions....Pages 159-180
Back Matter....Pages 181-181
Biochemistry, general
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