Human disease glycomics: technology advances enabling protein glycosylation analysis - part 1.

@article{EverestDass2018HumanDG,
  title={Human disease glycomics: technology advances enabling protein glycosylation analysis - part 1.},
  author={Arun Everest-Dass and Edward S X Moh and Christopher Ashwood and Abdulrahman M M Shathili and Nicolle H. Packer},
  journal={Expert review of proteomics},
  year={2018},
  volume={15 2},
  pages={
          165-182
        }
}
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… CONTINUE READING
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References

Publications referenced by this paper.
SHOWING 1-10 OF 214 REFERENCES

Oligosaccharides isolated from pig submaxillary mucin.

  • The Journal of biological chemistry
  • 1966
VIEW 12 EXCERPTS
HIGHLY INFLUENTIAL

NMR of glycans: shedding new light on old problems.

  • Progress in nuclear magnetic resonance spectroscopy
  • 2014
VIEW 4 EXCERPTS
HIGHLY INFLUENTIAL

A Dual Pressure Linear Ion Trap Orbitrap Instrument with Very High Sequencing Speed*

  • Molecular & cellular proteomics : MCP
  • 2009
VIEW 6 EXCERPTS
HIGHLY INFLUENTIAL

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