Evidence map›Paper›PMID 21953200›Full record

ArticleJournal of the American Society for Mass Spectrometry2011

Differentiation of α- or β-aspartic isomers in the heptapeptides by the fragments of [M + Na]+ using ion trap tandem mass spectrometry.

Bing Wang, Jin Zhuo Shang, Yu Jiao Qin, Bing Na Yan, Xin Hua Guo

Abstract read
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In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

1 citing paper in PubMed, 8 citations in OpenAlex.

  1. Article
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

5 authors at 1 institution in 1 country.

Bing WangCollege of Chemistry, Jilin University, Changchun, China.
Jin Zhuo Shang
Yu Jiao Qin
Bing Na Yan
Xin Hua Guo
Jilin University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Electrospray ionization coupled with low energy collision induced dissociation (CID) in an ion trap mass spectrometer was used to examine the fragmentation patterns of the [M + Na](+) of eight pairs of heptapeptides containing α- or β-Asp residues in second and sixth amino acid positions, respectively. Selective cleavages at the peptide backbone C-terminal to two Asp residues were observed, which generated a series of C-terminal y(5) ions and N-terminal b(6) ions. Two typical ions: [y5 + Na - H]+ and [b6 + Na + OH]+, produced by α-Asp containing peptides were noted to be much more abundant than those of the peptides with β-Asp, which could be used for distinction of the isomers in Asp2 and Asp6, respectively. In addition, a series of internal ions generated by simultaneous cleavages at Asp residues were detected. Competitive reactions of carboxylic groups occurred between Asp6 side chain and C-terminus. Formation mechanisms of most product ions are proposed. The results obtained in this work are significant since low energy CID has been demonstrated to be effective for the distinction of Asp isomers.

Indexed as

AnionsAspartic AcidIsomerismOligopeptidesSodiumSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryAnionsAspartic AcidOligopeptidesSodium

Identifiers

PMID21953200
OpenAlexW1980824140

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.