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Author Notes:

Correspondence: David F. Smith, Dept. of Biochemistry, Emory University School of Medicine, 1510 Clifton Rd. NE, Rm. 4035, Atlanta, GA 30322. Telephone: 404-727-6155. Fax: 404-727-2738. Email: dfsmith@emory.edu.

Richard D. Cummings, William Patterson Timmie Professor and Chair, Dept. of Biochemistry, Emory University School of Medicine, 1510 Clifton Rd. NE, Ste. 4001, Atlanta, GA 30322. Telephone: 404-727-0988. Fax: 404-727-2738. Email: rdcummi@emory.edu.

We thank Jamie Heimburg-Molinaro for critical editing assistance.

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Research Funding:

This work was supported, in whole or in part, by National Institutes of Health Grants GM85448 (to D.F.S.) and GM98791 (to R.D.C.).

Application of Microarrays for Deciphering the Structure and Function of the Human Glycome

Tools:

Journal Title:

Molecular & Cellular Proteomics

Volume:

Volume 12, Number 4

Publisher:

, Pages 902-912

Type of Work:

Article | Final Publisher PDF

Abstract:

Glycan structures were defined historically using multiple methods to determine composition, sequence, linkage, and anomericity of component monosaccharides. Such approaches have been replaced by more sensitive MS methods to profile or predict glycan structures, but these methods are limited in their ability to completely define glycan structures. Glycan-binding proteins, including lectins and antibodies, have been found to have exquisite binding specificities that can provide information about glycan structures. Here, we show glycan-binding proteins can be used along with MS to help define glycan linkages and other determinants in unknown glycans printed as shotgun glycan microarrays.

Copyright information:

© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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