Separation of the complex asparagine-linked oligosaccharides of the glycoprotein fetuin and elucidation of three triantennary structures having sialic acids linked only to galactose residues
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00441a050
Cited by 66 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Tissue chaperoning—the expanded functions of fetuin-A beyond inhibition of systemic calcification;Pflügers Archiv - European Journal of Physiology;2022-04-11
2. High-pH Anion-Exchange Chromatography (HPAEC) and Pulsed Amperometric Detection (PAD) for Carbohydrate Analysis;Comprehensive Glycoscience;2021
3. Fetuin-A – Alpha2-Heremans-Schmid Glycoprotein: From Structure to a Novel Marker of Chronic Diseases Part 2. Fetuin-A – A Marker of Insulin Resistance and Related Chronic Diseases;Journal of Biomedical and Clinical Research;2018-07-01
4. Site-Specific Glycan Heterogeneity Characterization by Hydrophilic Interaction Liquid Chromatography Solid-Phase Extraction, Reversed-Phase Liquid Chromatography Fractionation, and Capillary Zone Electrophoresis-Electrospray Ionization-Tandem Mass Spectrometry;Analytical Chemistry;2018-01-03
5. Fetuin-A – Alpha2-Heremans-Schmid Glycoprotein: From Structure to a Novel Marker of Chronic Diseases Part 1. Fetuin-A as a Calcium Chaperone and Inflammatory Marker;Journal of Biomedical and Clinical Research;2017-12-01
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