Analysis of Protein Post-Translational Modifications by Mass Spectrometry

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John Wiley & Sons, Oct 12, 2016 - Science - 416 pages
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  • Covers all major modifications, including phosphorylation, glycosylation, acetylation, ubiquitination, sulfonation and and glycation
  • Discussion of the chemistry behind each modification, along with key methods and references
  • Contributions from some of the leading researchers in the field
  • A valuable reference source for all laboratories undertaking proteomics, mass spectrometry and post-translational modification research
 

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Contents

Chapter 1 Introduction
1
Chapter 2 Identification and Analysis of Protein Phosphorylation by Mass Spectrometry
17
Chapter 3 Analysis of Protein Glycosylation by Mass Spectrometry
89
Chapter 4 Protein Acetylation and Methylation
161
Chapter 5 Tyrosine Nitration
197
Chapter 6 Mass Spectrometry Methods for the Analysis of Isopeptides Generated from Mammalian Protein Ubiquitination and SUMOylation
235
Chapter 7 The Deimination of Arginine to Citrulline
275
Chapter 8 Glycation of Proteins
307
Chapter 9 Biological Significance and Analysis of Tyrosine Sulfation
333
Chapter 10 The Application of Mass Spectrometry for the Characterization of Monoclonal AntibodyBased Therapeutics
351
Index
387
EULA
396
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