Evidence map›Paper›PMID 18396915›Full record

ArticleAnalytical chemistry2008

Rapidly alternating transmission mode electron-transfer dissociation and collisional activation for the characterization of polypeptide ions.

Hongling Han, Yu Xia, Min Yang, Scott A McLuckey

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 52 citations in OpenAlex.

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  14. Gas-phase chemistry of multiply charged bioions in analytical mass spectrometry.Annual review of analytical chemistry (Palo Alto, Calif.) · 2010
    Review
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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

4 authors at 1 institution in 1 country.

Hongling HanDepartment of Chemistry, Purdue University, West Lafayette, Indiana 47907-2084, USA.
Yu Xia
Min Yang
Scott A McLuckey
Purdue University West Lafayette · US

Funding

Gas-phase Bio-conjugation in the Tandem Mass Spectrometry of Peptides, Proteins,R37GM045372 · NIGMS · PURDUE UNIVERSITY · PI MCLUCKEY, SCOTT A · 2014 to 2023
$3.1M
INSTRUMENTATION FOR ANALYSIS OF HIGH MASS BIOMOLECULESR01GM045372 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI MCLUCKEY, SCOTT A · 1991 to 2012
$2.8M
NIGMS NIH HHS GM 45372NIGMS NIH HHS R01 GM045372NIGMS NIH HHS R37 GM045372
6 · The paper itself

Abstract

Cation transmission/electron-transfer reagent anion storage mode electron-transfer ion/ion reactions and beam-type collisional activation of the polypeptide ions are performed in rapid succession in the high-pressure collision cell (Q2) of a quadrupole/time-of-flight tandem mass spectrometer (QqTOF), where the electron-transfer reagent anions are accumulated. Duty cycles for both electron-transfer dissociation (ETD) and collision-induced dissociation (CID) experiments are improved relative to ion trapping approaches since there are no discrete ion storage and reaction steps for ETD experiments and no discrete ion storage step and frequency tuning for CID experiments. For this technique, moderately high resolution and mass accuracy are also obtained due to mass analysis via the TOF analyzer. This relatively simple approach has been demonstrated with a triply charged tryptic peptide, a triply charged tryptic phosphopeptide, and a triply charged tryptic N-linked glycopeptide. For the tryptic peptide, the sequence is identified with more certainty than would be available from a single method alone due to the complementary information provided by these two dissociation methods. Because of the complementary information derived from both ETD and CID dissociation methods, peptide sequence and post-translational modification (PTM) sites for the phosphopeptide are identified. This combined ETD and CID approach is particularly useful for characterizing glycopeptides because ETD generates information about both peptide sequence and locations of the glycosylation sites, whereas CID provides information about the glycan structure.

Indexed as

AnimalsCaseinsCattleGlycopeptidesHorsesMyoglobinPeptidesPlant LectinsTandem Mass SpectrometryTosylphenylalanyl Chloromethyl KetoneTrypsinCaseinserythrina lectinGlycopeptidesMyoglobinPeptidesPlant LectinsTosylphenylalanyl Chloromethyl KetoneTrypsin

Identifiers

PMID18396915
PMCPMC2661565
OpenAlexW1972737162

What OpenQuestion holds

Textmetadata
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.