4.7 Review

Advances in Tools to Determine the Glycan-Binding Specificities of Lectins and Antibodies

Journal

MOLECULAR & CELLULAR PROTEOMICS
Volume 19, Issue 2, Pages 224-232

Publisher

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.R119.001836

Keywords

-

Funding

  1. National Cancer Institute (Alliance of Glycobiologists for Cancer Detection) [U01CA168896]
  2. National Cancer Institute (Innovative Molecular Analysis Technology Program) [R21CA225474]
  3. National Institute for General Medical Sciences (STTR/SBIR Program) [R43GM131430, R41GM112750]

Ask authors/readers for more resources

Proteins that bind carbohydrate structures can serve as tools to quantify or localize specific glycans in biological specimens. Such proteins, including lectins and glycan-binding antibodies, are particularly valuable if accurate information is available about the glycans that a protein binds. Glycan arrays have been transformational for uncovering rich information about the nuances and complexities of glycan-binding specificity. A challenge, however, has been the analysis of the data. Because protein-glycan interactions are so complex, simplistic modes of analyzing the data and describing glycan-binding specificities have proven inadequate in many cases. This review surveys the methods for handling high-content data on protein-glycan interactions. We contrast the approaches that have been demonstrated and provide an overview of the resources that are available. We also give an outlook on the promising experimental technologies for generating new insights into protein-glycan interactions, as well as a perspective on the limitations that currently face the field.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available