期刊
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 79
卷 79, 期 -, 页码 619-653出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev.biochem.77.070606.100917
关键词
array; glycan; glycomimetic; glycosylation; lectin; multivalency
资金
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R56AI063596, R01AI055258, R01AI063596] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM055984, R01GM049975] Funding Source: NIH RePORTER
- NIAID NIH HHS [AI063596, R01 AI055258-08, AI055258, R01 AI055258, R01 AI063596-07, R01 AI063596] Funding Source: Medline
- NIGMS NIH HHS [GM49974, GM55984, R01 GM049975-17, R01 GM049975] Funding Source: Medline
Glycans are ubiquitous components of all organisms. Efforts to elucidate glycan function and to understand how they are assembled and disassembled can reap benefits in fields ranging from bioenergy to human medicine. Significant advances in our knowledge of glycan biosynthesis and function are emerging, and chemical biology approaches are accelerating the pace of discovery. Novel strategies for assembling oligosaccharides, glycoproteins, and other glycoconjugates are providing access to critical materials for interrogating glycan function. Chemoselective reactions that facilitate the synthesis of glycan-substituted imaging agents, arrays, and materials are yielding compounds to interrogate and perturb glycan function and dysfunction. To complement these advances, small molecules are being generated that inhibit key glycan-binding proteins or biosynthetic enzymes. These examples illustrate how chemical glycobiology is providing new insight into the functional roles of glycans and new opportunities to interfere with or exploit these roles.
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