Evidence map›Paper›PMID 24889823›Full record

ReviewMass spectrometry reviews

Quantitative mass spectrometric analysis of glycoproteins combined with enrichment methods.

Yeong Hee Ahn, Jin Young Kim, Jong Shin Yoo

Open access · bronzeAbstract readReview
In one paragraph

Review in Mass spectrometry reviews. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 86 citations in OpenAlex.

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  6. Bottom-Up Proteomics: Advancements in Sample Preparation.International journal of molecular sciences · 2023
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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

3 authors at 1 institution in 1 country.

Yeong Hee AhnDivision of Mass Spectrometry, Korea Basic Science Institute, Cheongwon-Gun, 363-883, Republic of Korea.
Jin Young Kim
Jong Shin Yoo
Korea Basic Science Institute · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mass spectrometry (MS) has been a core technology for high sensitive and high-throughput analysis of the enriched glycoproteome in aspects of quantitative assays as well as qualitative profiling of glycoproteins. Because it has been widely recognized that aberrant glycosylation in a glycoprotein may involve in progression of a certain disease, the development of efficient analysis tool for the aberrant glycoproteins is very important for deep understanding about pathological function of the glycoprotein and new biomarker development. This review first describes the protein glycosylation-targeting enrichment technologies mainly employing solid-phase extraction methods such as hydrizide-capturing, lectin-specific capturing, and affinity separation techniques based on porous graphitized carbon, hydrophilic interaction chromatography, or immobilized boronic acid. Second, MS-based quantitative analysis strategies coupled with the protein glycosylation-targeting enrichment technologies, by using a label-free MS, stable isotope-labeling, or targeted multiple reaction monitoring (MRM) MS, are summarized with recent published studies.

Indexed as

BiomarkersBoronic AcidsChromatography, AffinityGlycoproteinsGlycosylationHumansHydrazinesIsotope LabelingLectinsMass SpectrometryProteomicsSolid Phase ExtractionBiomarkersBoronic AcidsGlycoproteinsHydrazinesLectinsaffinity enrichmenthydrazidelectinmultiple reaction monitoringprotein glycosylationquantitative mass spectrometrystable isotope labeling

Identifiers

PMID24889823
PMCPMC4340049
OpenAlexW1959493862

What OpenQuestion holds

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LicenceCC BY-NC
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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.