Evidence map›Paper›PMID 19199571›Full record

ArticleAnalytical chemistry2009

Top-down protein identification/characterization of a priori unknown proteins via ion trap collision-induced dissociation and ion/ion reactions in a quadrupole/time-of-flight tandem mass spectrometer.

Jian Liu, Teng-Yi Huang, Scott A McLuckey

Abstract read
In one paragraph

Article in Analytical chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

  1. Gas-Phase Oxidation of Neutral Basic Residues in Polypeptide Cations by Periodate.Journal of the American Society for Mass Spectrometry · 2016
    Article
  2. Article
  3. Oxidation of methionine residues in polypeptide ions via gas-phase ion/ion chemistry.Journal of the American Society for Mass Spectrometry · 2014
    Article
  4. Solution versus gas-phase modification of peptide cations with NHS-ester reagents.Journal of the American Society for Mass Spectrometry · 2012
    Article
  5. Analysis of intact protein isoforms by mass spectrometry.The Journal of biological chemistry · 2011
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Gas-phase chemistry of multiply charged bioions in analytical mass spectrometry.Annual review of analytical chemistry (Palo Alto, Calif.) · 2010
    Review
  12. 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

3 authors.

Jian LiuDepartment of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, Indiana 47907-2084, USA.
Teng-Yi Huang
Scott A McLuckey

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

The identification and characterization of a priori unknown proteins from an Escherichia coli (E. coli) soluble protein lysate using ion trap collision-induced dissociation of intact protein ions followed by ion/ion reactions in a quadrupole/time-of-flight tandem mass spectrometer is illustrated. The procedure involved the submission of uninterpreted product ion spectra to a peak-picking program and then to ProSightPTM for searching against an E. coli database. Examples are provided for the identification and characterization of both modified and unmodified unknown proteins with masses up to approximately 28 kDa. The availability of protein intact mass along with sequence information makes possible the characterization of proteins with post-translational modifications, such as disulfide linkages, as well as protein isoforms whose sequences are absent from a database, provided that a related form of the gene product is present in the database. This work demonstrates that the quadrupole/time-of-flight platform, in conjunction with ion-ion proton transfer reactions, can be adapted to obtain primary structure information from entire protein ions, rather than simply N- or C-terminal information from low mass-to-charge products, for proteins as large as several tens of kilodaltons.

Indexed as

Amino Acid SequenceCell ExtractsComplex MixturesDatabases, ProteinEscherichia coliEscherichia coli ProteinsMolecular Sequence DataProtein Processing, Post-TranslationalSensitivity and SpecificityTandem Mass SpectrometryCell ExtractsComplex MixturesEscherichia coli Proteins

Identifiers

PMID19199571
PMCPMC2667219

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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.