Publication
Cross-comparison of Protein Recognition of Sialic Acid Diversity on Two Novel Sialoglycan Microarrays
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- Persistent URL
- Last modified
- 02/20/2025
- Type of Material
- Authors
- Language
- English
- Date
- 2012-06-29
- Publisher
- American Society for Biochemistry and Molecular Biology
- Publication Version
- Copyright Statement
- © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
- Final Published Version (URL)
- Title of Journal or Parent Work
- ISSN
- 0021-9258
- Volume
- 287
- Issue
- 27
- Start Page
- 22593
- End Page
- 22608
- Grant/Funding Information
- This work was supported, in whole or in part, by National Institutes of Health Grants R01GM32373 and U01 CA128442 (to A. V.), RO1GM085448 (to D. F. S.), and R01GM076360 (to X. C.) and a bridging grant from the Consortium for Functional Glycomics under National Institutes of Health, NIGMS, Grant GM62116 (to R. D. C.).
- This work was also supported by an International Sepharadic Education Foundation postdoctoral fellowship (to V. P.-K.) and Defense Advanced Research Projects Agency Grant HR0011-10-00 (to R. D. C.).
- Supplemental Material (URL)
- Abstract
- Background: Various glycan microarrays are currently widely used, but systematic cross-comparisons are lacking. Results: We compare and contrast two sialoglycan microarrays using a variety of sialic acid-binding proteins. Conclusion: Diverse array formats can strengthen the quality of information, but differences between arrays may be observed. Significance: Glycan arrays with similar glycan structures cannot be simply assumed to give similar results.
- Author Notes
- Keywords
- Research Categories
- Engineering, Biomedical
- Chemistry, Biochemistry
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