Evidence map›Paper›PMID 19113943›Full record

ArticleJournal of proteome research2009

Extracting both peptide sequence and glycan structural information by 157 nm photodissociation of N-linked glycopeptides.

Liangyi Zhang, James P Reilly

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

32 citing papers in PubMed, 57 citations in OpenAlex.

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  9. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
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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

2 authors at 1 institution in 1 country.

Liangyi ZhangDepartment of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.
James P Reilly
Indiana University Bloomington · US

Funding

TRAININGP41RR018942 · NCRR · TRUSTEES OF INDIANA UNIVERSITY · PI REILLY, JAMES P. · 2005 to 2008
$3.9M
NCRR NIH HHS P41 RR018942NCRR NIH HHS RR018942
6 · The paper itself

Abstract

The 157 nm photodissociation of N-linked glycopeptides was investigated in MALDI tandem time-of-flight (TOF) and linear ion trap mass spectrometers. Singly charged glycopeptides yielded abundant peptide and glycan fragments. The peptide fragments included a series of x-, y-, v-, and w- ions with the glycan remaining intact. These provide information about the peptide sequence and the glycosylation site. In addition to glycosidic fragments, abundant cross-ring glycan fragments that are not observed in low-energy CID were detected. These fragments provide insight into the glycan sequence and linkages. Doubly charged glycopeptides generated by nanospray in the linear ion trap mass spectrometer also yielded peptide and glycan fragments. However, the former were dominated by low-energy fragments such as b- and y- type ions while glycan was primarily cleaved at glycosidic bonds.

Indexed as

Amino Acid SequenceCarbohydrate ConformationCarbohydrate SequenceGlycopeptidesGlycosylationMolecular Sequence DataPeptide FragmentsPhotochemical ProcessesPolysaccharidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationGlycopeptidesPeptide FragmentsPolysaccharides

Identifiers

PMID19113943
PMCPMC2654178
OpenAlexW2030864700

What OpenQuestion holds

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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.