Selective Identification of α-Galactosyl Epitopes in N-Glycoproteins Using Characteristic Fragment Ions from Higher-Energy Collisional Dissociation-Reference-Cited by-同舟云学术

Selective Identification of α-Galactosyl Epitopes in N-Glycoproteins Using Characteristic Fragment Ions from Higher-Energy Collisional Dissociation

Published:2020-09-09 Issue:19 Volume:92 Page:13144-13154
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Lee Hyun Kyoung¹²,Ha Dae-In³⁴,Kang Jeong Gu³,Park Gun Wook¹,Lee Ju Yeon¹,Cho Kun¹^ORCID,Bin Moon Su³⁴,Shin Jong Hwan¹²,Kim Yong-Sam³⁴,An Hyun Joo¹²,Kim Jin Young¹,Yoo Jong Shin¹²^ORCID,Ko Jeong-Heon³⁴

Affiliation:

1. Research Center of Bioconvergence Analysis, Korea Basic Science Institute, Ochang-eup, Cheongju 28119, Republic of Korea

2. Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon 34134, Republic of Korea

3. Genome Editing Research Center, KRIBB, 125 Gwahak-ro, Daejeon 34141, Republic of Korea

4. Department of Biomolecular Science, KRIBB School of Bioscience, Korea University of Science and Technology (UST), 217 Gajeong-ro, Daejeon 34113, Republic of Korea

Funder

National Research Council of Science and Technology

Korea Basic Science Institute

Publisher

American Chemical Society (ACS)

Subject

Analytical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.0c02276

Reference39 articles.

1. The Galα1,3Galβ1,4GlcNAc-R (α-Gal) epitope: A carbohydrate of unique evolution and clinical relevance

2. Anti-Gal: an abundant human natural antibody of multiple pathogeneses and clinical benefits

3. Characteristics of α-Gal epitope, anti-Gal antibody, α1,3 galactosyltransferase and its clinical exploitation (Review)

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