Proteomics

Dataset Information

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The analysis of site-specific O-acetylated N-glycans in human, rat, and mouse sera.


ABSTRACT: In this work, we systematically compared O-acetylated sialoglycopeptides (O-AcSGPs) among sera of human, rat, and mouse to reveal differences and diversities of sialic acid types and O-acetylation patterns in different species. We utilized our high-resolution glycoproteomic approaches to identify numerous O-acetylated N-glycans in rat and mouse sera, and described their structures and distributions across different glycoproteins.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Rattus Norvegicus (rat) Homo Sapiens (human) Mus Musculus (mouse)

TISSUE(S): Blood Serum

SUBMITTER: Didi Liu  

LAB HEAD: Shisheng Sun

PROVIDER: PXD053293 | Pride | 2024-12-17

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
HumanSerum_1.raw Raw
HumanSerum_1_result.xlsx Xlsx
HumanSerum_2.raw Raw
HumanSerum_2_result.xlsx Xlsx
HumanSerum_3.raw Raw
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Publications

Distinct <i>O</i>-Acetylation Patterns of Serum Glycoproteins among Humans, Mice, and Rats.

Liu Didi D   Xue Yue Y   Ding Dan D   Zhu Bojing B   Shen Jiechen J   Jin Zhehui Z   Sun Shisheng S  

Journal of proteome research 20241112 12


<i>O</i>-Acetylation is a significant chemical modification of sialic acids on glycoproteins with diverse biological functions. As two important animal models, mice and rats have been widely used for various biomedical studies. In this study, we show that the sialic acid types and their <i>O</i>-acetylation patterns have large differences among serum glycoproteins of humans, rats, and mice. Based on intact <i>N</i>-glycopeptide analyses, all sialoglycopeptides in human sera were modified by Neu5  ...[more]

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