Evidence map›Paper›PMID 22304307›Full record

ArticleAnalytical chemistry2012

Glycan analysis by reversible reaction to hydrazide beads and mass spectrometry.

Shuang J Yang, Hui Zhang

Abstract read
In one paragraph

Article in Analytical chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
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  11. Review
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  17. Article
  18. Solid-phase glycan isolation for glycomics analysis.Proteomics. Clinical applications · 2012
    Review
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

2 authors.

Shuang J YangDepartment of Pathology, Johns Hopkins University, Baltimore, Maryland 21231, USA.
Hui Zhang

Funding

Glycoprotein biomarkers for the early detection of aggressive prostate cancerU01CA152813 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2010 to 2021
$6.2M
NCI NIH HHS U01 CA152813NCI NIH HHS U01CA152813NHLBI NIH HHS N01-HV-00240
6 · The paper itself

Abstract

Investigation into glycoproteins and their associated glycans is the key to understanding the function of glycoproteins in biological pathways and disease development. Current methods for glycan analysis are generally based on multiple preparation processes to separate glycans from proteins and other molecules prior to analysis. During the multistep purification processes, glycans are continuously lost and the procedure increases the difficulty for accurate quantitative analysis of glycans. Here we describe the development of a novel technique, which uses hydrazide beads to capture glycans. It is based on the conjugation of glycans to hydrazide beads through the formation of reversible hydrazone, washing out unbound nonglycans, then releasing captured glycans by acids. The results showed that the glycans were able to be isolated from concatenate peptides by using hydrazide beads. This technique was also applied to the analysis of glycans from sera sample. The integrated capture-release on the solid-phase simplifies the procedure for glycan preparation from a complex mixture and can be a powerful tool for glycan analysis.

Indexed as

Spectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAdipatesAngiotensin IChromatography, High Pressure LiquidHumansHydrogen-Ion ConcentrationHydrolysisNeurotensinPolysaccharidesSolid Phase ExtractionAdipatesadipic dihydrazideAngiotensin INeurotensinPolysaccharides

Identifiers

PMID22304307
PMCPMC4876039

What OpenQuestion holds

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Registered trials

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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.