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You searched for: Author "Williamson, Seth" Remove constraint Author: "Williamson, Seth" Subject glycosylation Remove constraint Subject: glycosylation Subject derivatization Remove constraint Subject: derivatization
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1. Advances in mass spectrometry‐based glycomics

Author:
Williamson, Seth D.,   et al.   ; Dong, Xue; Huang, Yifan; Cho, Byeong Gwan; Zhong, Jieqiang; Gautam, Sakshi; Peng, Wenjing; Banazadeh, Alireza; Torres‐Ulloa, Katya Y.; Mechref, Yehia;     Show all 10 Authors
Source:
Electrophoresis 2018 v.39 no.24 pp. 3063-3081
ISSN:
0173-0835
Subject:
chemical bonding; derivatization; electrophoresis; glycomics; glycosylation; ionization; mass spectrometry; physicochemical properties; polysaccharides; proteins
Abstract:
... The diversification of the chemical properties and biological functions of proteins is attained through posttranslational modifications, such as glycosylation. Glycans, which are covalently attached to proteins, play a vital role in cell activities. The microheterogeneity and complexity of glycan structures associated with proteins make comprehensive glycomic analysis challenging. However, recent ...
DOI:
10.1002/elps.201800273

2. Advances in mass spectrometry‐based glycoproteomics

Author:
Williamson, Seth D.,   et al.   ; Yu, Aiying; Zhao, Jingfu; Peng, Wenjing; Banazadeh, Alireza; Goli, Mona; Huang, Yifan; Mechref, Yehia;     Show all 8 Authors
Source:
Electrophoresis 2018 v.39 no.24 pp. 3104-3122
ISSN:
0173-0835
Subject:
bioinformatics; cell communication; derivatization; electrophoresis; glycopeptides; glycoproteins; glycoproteomics; glycosylation; host-pathogen relationships; immune response; inflammation; ionization; mass spectrometry
Abstract:
... Protein glycosylation, an important PTM, plays an essential role in a wide range of biological processes such as immune response, intercellular signaling, inflammation, and host–pathogen interaction. Aberrant glycosylation has been correlated with various diseases. However, studying protein glycosylation remains challenging because of low abundance, microheterogeneities of glycosylation sites, and ...
DOI:
10.1002/elps.201800272