N-Glycosidase <i>Rudaea cellulosilytica</i> (PNGase Rc) Column for the Characterization of Glycoprotein Conformational Epitopes by Hydrogen/Deuterium Exchange Mass Spectrometry (HDX-MS)-Reference-Cited by-同舟云学术

N-Glycosidase Rudaea cellulosilytica (PNGase Rc) Column for the Characterization of Glycoprotein Conformational Epitopes by Hydrogen/Deuterium Exchange Mass Spectrometry (HDX-MS)

Published:2024-02-28 Issue: Volume: Page:1-15
ISSN:0003-2719
Container-title:Analytical Letters
language:en
Short-container-title:Analytical Letters

Author:

Deng Ying¹²,Yang Dongyuan¹²,Zheng Wen³,Qi Ao²⁴⁵,Yang Yulin²⁴⁵,Shu Zhulin²⁴⁵,Zhang Fengyi²⁴⁵,Han Hongbo²⁵,Chen Jin²⁵,Zheng Jie¹²⁴⁵

Affiliation:

1. School of Chinese Materia Medica, Nanjing University of Chinese Medicine, Nanjing, Jiangsu, China

2. The Drug Research Center of Immunological Diseases, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China

3. Hubei Yuanda Biotechnology, Wuhan, China

4. School of Pharmaceutical Science and Technology, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou, China

5. University of Chinese Academy of Sciences, Beijing, China

Funder

National Natural Science Foundation of China

Publisher

Informa UK Limited

Link

https://www.tandfonline.com/doi/pdf/10.1080/00032719.2024.2320243

Reference29 articles.

1. Characterisation of peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase A and its N-glycans

2. Well-Tempered Metadynamics: A Smoothly Converging and Tunable Free-Energy Method

3. Molecular Mechanics of Beta-Sheets

4. Hydrogen/Deuterium Exchange Mass Spectrometry with Integrated Electrochemical Reduction and Microchip-Enabled Deglycosylation for Epitope Mapping of Heavily Glycosylated and Disulfide-Bonded Proteins

5. Glycan Side Reaction May Compromise ETD-Based Glycopeptide Identification