Evidence map›Paper›PMID 28505427›Full record

ArticleAnalytical chemistry2017

Modification of Sialic Acids on Solid Phase: Accurate Characterization of Protein Sialylation.

Shuang Yang, Lei Zhang, Stefani Thomas, Yingwei Hu, Shuwei Li, John Cipollo, Hui Zhang

Abstract read
In one paragraph

Article in Analytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 42 citations in OpenAlex.

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  5. High sensitivity glycomics in biomedicine.Mass spectrometry reviews · 2022
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Shuang YangDepartment of Pathology, Johns Hopkins University , Baltimore, Maryland 21231, United States.ORCID 0000-0001-7958-0594
Lei ZhangDepartment of Pathology, Johns Hopkins University , Baltimore, Maryland 21231, United States.
Stefani ThomasDepartment of Pathology, Johns Hopkins University , Baltimore, Maryland 21231, United States.ORCID 0000-0003-1679-5453
Yingwei HuDepartment of Pathology, Johns Hopkins University , Baltimore, Maryland 21231, United States.
Shuwei LiInstitute for Bioscience and Biotechnology Research, University of Maryland College Park , Rockville, Maryland 20850, United States.
John CipolloLaboratory for Bacterial Polysaccharides, Center for Biologics Evaluation and Research, Food and Drug Administration , Silver Spring, Maryland 20993, United States.
Hui ZhangDepartment of Pathology, Johns Hopkins University , Baltimore, Maryland 21231, United States.
Johns Hopkins University · USCenter for Biologics Evaluation and Research · USInstitute for Bioscience and Biotechnology Research

Funding

Shared Resource CoresP01HL107153 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2011 to 2017
$16.8M
Proteome Characterization Center: A Genoproteomics Pipeline for Cance ResearchU24CA160036 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI, ZHANG, HUI · 2011 to 2016
$10.7M
Glycoprotein biomarkers for the early detection of aggressive prostate cancerU01CA152813 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2010 to 2021
$6.2M
The Comprehensive Proteome Characterization Center at Johns Hopkins: High Precision Discovery and Confirmation of Genoproteomic TargetsU24CA210985 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI, ZHANG, HUI · 2016 to 2020
$5.3M
Targeting Latently Infected Primary Cells using Integrated GlycoproteomicsR21AI122382 · NIAID · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2016 to 2017
$446k
NCI NIH HHS U01 CA152813NCI NIH HHS U24 CA160036NCI NIH HHS U24 CA210985NHLBI NIH HHS P01 HL107153NIAID NIH HHS R21 AI122382
6 · The paper itself

Abstract

Sialic acids play many important roles in several physiological and pathological processes, including cancers, infection, and blood diseases. Sialic acids are fragile and prone to fragmentation under electrospray ionization and matrix-assisted laser desorption/ionization. It is crucial to modify sialic acids for qualitative and quantitative identification of their change in abundance in complex biological samples. Permethylation is a method of choice for sialic acid stabilization, but the harsh conditions during permethylation may lead to the decomposition of O-acetyl groups. Esterification or amidation in solution effectively protects sialic acids, yet it is not trivial to purify glycans from their reagents. Quantitative analysis of glycans can be achieved by labeling their reducing end using fluorescent tags. Loss of sialic acids during labeling is a major concern. In this study, we demonstrated the utility of sialic acids modification for the analysis of sialyl oligosaccharides and glycopeptides. Without modification, sialic acids are partially or completely lost during sample preparation, leading to the presence of false glycans or glycopeptides in the sample. The stabilized sialic acids not only result in accurate identification of sialylated glycans but also improve the characterization of intact glycopeptides. The modification of sialic acids on the solid support facilitates analysis of glycans and their intact glycoproteins.

Indexed as

Acetic AcidCatalysisGlycopeptidesHydrolysisOligosaccharidesPolysaccharidesSialic AcidsTemperatureAcetic AcidGlycopeptidesOligosaccharidesPolysaccharidesSialic Acids

Identifiers

PMID28505427
PMCPMC5583724
OpenAlexW2615203596

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.