Evidence map›Paper›PMID 18930411›Full record

ArticleJournal of the American Society for Mass Spectrometry2009

Analysis of the trypanosome flagellar proteome using a combined electron transfer/collisionally activated dissociation strategy.

Sarah R Hart, King Wai Lau, Zhiqi Hao, Richard Broadhead, Neil Portman, Andreas Hühmer, Keith Gull, Paul G McKean, Simon J Hubbard, Simon J Gaskell

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

13 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Cilium transition zone proteome reveals compartmentalization and differential dynamics of ciliopathy complexes.Proceedings of the National Academy of Sciences of the United States of America · 2016
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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

10 authors at 4 institutions in 2 countries.

Sarah R HartMichael Barber Centre for Mass Spectrometry, School of Chemistry and Manchester Interdisciplinary Biocentre, University of Manchester, Manchester, United Kingdom.
King Wai Lau
Zhiqi Hao
Richard Broadhead
Neil Portman
Andreas Hühmer
Keith Gull
Paul G McKean
Simon J Hubbard
Simon J Gaskell
University of Manchester · GBLancaster University · GBThermo Fisher Scientific (United States) · USUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council EGH17729Biotechnology and Biological Sciences Research Council EGH17741Biotechnology and Biological Sciences Research Council EGH17742Biotechnology and Biological Sciences Research Council EGM17685
6 · The paper itself

Abstract

The use of electron-transfer dissociation as an alternative peptide ion activation method for generation of protein sequence information is examined here in comparison with the conventional method of choice, collisionally activated dissociation, using a linear ion trapping instrument. Direct comparability between collisionally and electron-transfer-activated product ion data were ensured by employing an activation-switching method during acquisition, sequentially activating precisely the same precursor ion species with each fragmentation method in turn. Sequest (Thermo Fisher Scientific, San Jose, CA) searching of product ion data generated an overlapping yet distinct pool of polypeptide identifications from the products of collisional and electron-transfer-mediated activation products. To provide a highly confident set of protein recognitions, identification data were filtered using parameters that achieved a peptide false discovery rate of 1%, with two or more independent peptide assignments required for each protein. The use of electron transfer dissociation (ETD) has allowed us to identify additional peptides where the quality of product ion data generated by collisionally activated dissociation (CAD) was insufficient to infer peptide sequence. Thus, a combined ETD/CAD approach leads to the recognition of more peptides and proteins than are achieved using peptide analysis by CAD- or ETD-based tandem mass spectrometry alone.

Indexed as

Amino Acid SequenceAnimalsFlagellaProteomeProteomicsSequence Analysis, ProteinSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryTrypanosomaProteome

Identifiers

PMID18930411
OpenAlexW2043776679

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.