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Glycoproteomics and Glycomics

Edited by Dr Punit Shah & Dr Hui Zhang

Clinical Proteomics published the Glycoproteomics and glycomics thematic series with both solicited and unsolicited content on the topic of protein glycosylation; one of the most common protein modifications in both normal biological processes and diseases. The series focusses on glycoproteomic or glycomic methods and their clinical applications. For further information or to make a pre-submission enquiry, please contact

For previous publications on the topic of glycoproteomics in Clinical Proteomics, you may like to refer to volume 4 which can be accessed via the SpringerLink website.

This collection of articles has not been sponsored and articles have undergone the journal’s standard peer-review process. The Guest Editors declare no competing interests.

  1. Glycoproteins comprise a large portion of the salivary proteome and have great potential for biomarker discovery and disease diagnosis. However, the rate of production and the concentration of whole saliva cha...

    Authors: Shisheng Sun, Fei Zhao, Qinzhe Wang, Yaogang Zhong, Tanxi Cai, Peng Wu, Fuquan Yang and Zheng Li
    Citation: Clinical Proteomics 2014 11:25
  2. Protein glycosylation, as an important post-translational modification, is implicated in a number of ailments. Applying proteomic approaches, including mass spectrometry (MS) analyses that have played a signif...

    Authors: Hu Zhao, Yaojun Li and Ye Hu
    Citation: Clinical Proteomics 2014 11:21
  3. Adipose tissue is both an energy storage depot and an endocrine organ. The impaired regulation of the secreted proteins of adipose tissue, known as adipocytokines, observed during obesity contributes to the on...

    Authors: Jae-Min Lim, Edith E Wollaston-Hayden, Chin Fen Teo, Dorothy Hausman and Lance Wells
    Citation: Clinical Proteomics 2014 11:20
  4. Estrogen has been shown to mediate protection in female hearts against ischemia-reperfusion (I-R) stress. Composed by a Kir6.2 pore and an SUR2 regulatory subunit, cardiac ATP-sensitive potassium channels (KAT...

    Authors: Jianjiong Gao, Dong Xu, Grzegorz Sabat, Hector Valdivia, Wei Xu and Nian-Qing Shi
    Citation: Clinical Proteomics 2014 11:19
  5. Protein glycosylation serves critical roles in the cellular and biological processes of many organisms. Aberrant glycosylation has been associated with many illnesses such as hereditary and chronic diseases li...

    Authors: Deniz Baycin Hizal, Daniel Wolozny, Joseph Colao, Elena Jacobson, Yuan Tian, Sharon S Krag, Michael J Betenbaugh and Hui Zhang
    Citation: Clinical Proteomics 2014 11:15
  6. Glycosylation is one of the most important posttranslational modifications of proteins and plays essential roles in various biological processes. Aberration in the glycan moieties of glycoproteins is associate...

    Authors: Huan Liu, Ningbo Zhang, Debin Wan, Meng Cui, Zhiqiang Liu and Shuying Liu
    Citation: Clinical Proteomics 2014 11:14
  7. It is well known that cell surface glycans or glycocalyx play important roles in sperm motility, maturation and fertilization. A comprehensive profile of the sperm surface glycans will greatly facilitate both ...

    Authors: Ai-Jie Xin, Li Cheng, Hua Diao, Peng Wang, Yi-Hua Gu, Bin Wu, Yan-Cheng Wu, Guo-Wu Chen, Shu-Min Zhou, Shu-Juan Guo, Hui-Juan Shi and Sheng-Ce Tao
    Citation: Clinical Proteomics 2014 11:10
  8. Glycoproteins secreted into plasma from T cells infected with human immunodeficiency virus (HIV) latent infection may provide insight into understanding the host response to HIV infection in vivo. Glycoproteomics...

    Authors: Weiming Yang, Jian-Ying Zhou, Li Chen, Minghui Ao, Shisheng Sun, Paul Aiyetan, Antoine Simmons, Hui Zhang and Jay Brooks Jackson
    Citation: Clinical Proteomics 2014 11:9
  9. O-linked β-D-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) onto serine and threonine residues of proteins is an important post-translational modification (PTM), which is involved in many crucial b...

    Authors: Junfeng Ma and Gerald W Hart
    Citation: Clinical Proteomics 2014 11:8