期刊
GLYCOCONJUGATE JOURNAL
卷 37, 期 5, 页码 513-531出版社
SPRINGER
DOI: 10.1007/s10719-020-09940-0
关键词
Desialylation; Neuraminidase; Sialic acid; Sialidase; sialylation; Chromophore; fluorophore and chemiluminescent substrate
资金
- Faculty Research Fund from the Center for Gene Regulation in Health and Disease (GRHD)
- Faculty Research Development (FRD) Fund
- Cleveland State University
- China Scholarship Council
Sialidases are glycosidases responsible for the removal of sialic acid (Sia) residues (desialylation) from glycan portions of either glycoproteins or glycolipids. By desialylation, sialidases are able to modulate the functionality and stability of the Sia-containing molecules and are involved in both physiological and pathological pathways. Therefore, evaluation of sialidase activity and specificity is important for understanding the biological significance of desialylation by sialidases and its function and the related molecular mechanisms of the physiological and pathological pathways. In addition, it is essential for developing novel mechanisms and approaches for disease treatment and diagnosis and pathogen detection as well. This review summarizes the most recent sialidase substrates for evaluating sialidase activity and specificity and screening sialidase inhibitors, including (i) general sialidase substrates, (ii) specific sialidase substrates, (iii) native sialidase substrates and (iv) cellular sialidase substrates. This review also provides a brief introduction of recent instrumental methods for quantifying the sialidase activity, such as UV, fluorescence, HPLC and LC-MS methods.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据