A Data Set of Ion Mobility Collision Cross Sections and Liquid Chromatography Retention Times from 71 Pyridylaminated N-Linked Oligosaccharides-Reference-Cited by-同舟云学术

A Data Set of Ion Mobility Collision Cross Sections and Liquid Chromatography Retention Times from 71 Pyridylaminated N-Linked Oligosaccharides

Published:2022-08-23 Issue:9 Volume:33 Page:1772-1783
ISSN:1044-0305
Container-title:Journal of the American Society for Mass Spectrometry
language:en
Short-container-title:J. Am. Soc. Mass Spectrom.

Author:

Manabe Noriyoshi¹,Ohno Shiho¹,Matsumoto Kana²,Kawase Taiji³,Hirose Kenji³,Masuda Katsuyoshi⁴,Yamaguchi Yoshiki¹²^ORCID

Affiliation:

1. Division of Structural Glycobiology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi981-8558, Japan

2. Structural Glycobiology Team, RIKEN-Max Planck Joint Research Center, Global Research Cluster, RIKEN, 2-1 Hirosawa, Wako, Saitama351-0198, Japan

3. Nihon Waters KK, Kitashinagawa, Shinagawa, Tokyo140-0001, Japan

4. Graduate School of Engineering, Osaka University, Suita, Osaka565-0871, Japan

Funder

Japan Society for the Promotion of Science

TECHNOVA

Publisher

American Chemical Society (ACS)

Subject

Spectroscopy,Structural Biology

Link

https://pubs.acs.org/doi/pdf/10.1021/jasms.2c00165

Reference22 articles.

1. Biological roles of glycans

2. A synopsis of recent developments defining how N-glycosylation impacts immunoglobulin G structure and function

3. Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy

4. A General Strategy for the Chemoenzymatic Synthesis of Asymmetrically Branched N -Glycans

5. Recognition of Bisecting N-Acetylglucosamine

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