Evidence map›Paper›PMID 16271296›Full record

ArticleJournal of the American Society for Mass Spectrometry2005

Characterization of a new qQq-FTICR mass spectrometer for post-translational modification analysis and top-down tandem mass spectrometry of whole proteins.

Judith A Jebanathirajah, Jason L Pittman, Bruce A Thomson, Bogdan A Budnik, Parminder Kaur, Michael Rape, Marc Kirschner, Catherine E Costello, Peter B O'Connor

Abstract readEvaluation Study
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

36 citing papers in PubMed, 58 citations in OpenAlex.

  1. Analysis of RNA and Its Modifications.Annual review of analytical chemistry (Palo Alto, Calif.) · 2024
    Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Unusual fragmentation of β-linked peptides by ExD tandem mass spectrometry.Journal of the American Society for Mass Spectrometry · 2011
    Article
  11. Article
  12. Article
  13. Article
  14. Charge remote fragmentation in electron capture and electron transfer dissociation.Journal of the American Society for Mass Spectrometry · 2010
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The effect of fixed charge modifications on electron capture dissociation.Journal of the American Society for Mass Spectrometry · 2008
    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

9 authors at 3 institutions in 1 country.

Judith A JebanathirajahMass Spectrometry Resource, Department of Biochemistry, Boston University School of Medicine, MA 02115, USA.
Jason L Pittman
Bruce A Thomson
Bogdan A Budnik
Parminder Kaur
Michael Rape
Marc Kirschner
Catherine E Costello
Peter B O'Connor
Boston University · USCenter for Systems Biology · USHarvard University · US

Funding

XI INTERNATIONAL SYMPOSIUM ON AMYLOIDOSISP41RR010888 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 1996 to 2011
$18.6M
NHLBI PROTEOMICS INITIATIVEN01HV28178 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · 2007 to 2008
$2.8M
NHLBI PROTEOMICS INITIATIVE-N01HV28178N01HV028178 · HV · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2002 to 2006
–
NCRR NIH HHS P41 RR10888NHLBI NIH HHS N01 HV28178
6 · The paper itself

Abstract

The use of a new electrospray qQq Fourier transform ion cyclotron mass spectrometer (qQq-FTICR MS) instrument for biologic applications is described. This qQq-FTICR mass spectrometer was designed for the study of post-translationally modified proteins and for top-down analysis of biologically relevant protein samples. The utility of the instrument for the analysis of phosphorylation, a common and important post-translational modification, was investigated. Phosphorylation was chosen as an example because it is ubiquitous and challenging to analyze. In addition, the use of the instrument for top-down sequencing of proteins was explored since this instrument offers particular advantages to this approach. Top-down sequencing was performed on different proteins, including commercially available proteins and biologically derived samples such as the human E2 ubiquitin conjugating enzyme, UbCH10. A good sequence tag was obtained for the human UbCH10, allowing the unambiguous identification of the protein. The instrument was built with a commercially produced front end: a focusing rf-only quadrupole (Q0), followed by a resolving quadrupole (Q1), and a LINAC quadrupole collision cell (Q2), in combination with an FTICR mass analyzer. It has utility in the analysis of samples found in substoichiometric concentrations, as ions can be isolated in the mass resolving Q1 and accumulated in Q2 before analysis in the ICR cell. The speed and efficacy of the Q2 cooling and fragmentation was demonstrated on an LCMS-compatible time scale, and detection limits for phosphopeptides in the 10 amol/muL range (pM) were demonstrated. The instrument was designed to make several fragmentation methods available, including nozzle-skimmer fragmentation, Q2 collisionally activated dissociation (Q2 CAD), multipole storage assisted dissociation (MSAD), electron capture dissociation (ECD), infrared multiphoton induced dissociation (IRMPD), and sustained off resonance irradiation (SORI) CAD, thus allowing a variety of MS(n) experiments. A particularly useful aspect of the system was the use of Q1 to isolate ions from complex mixtures with narrow windows of isolation less than 1 m/z. These features enable top-down protein analysis experiments as well structural characterization of minor components of complex mixtures.

Indexed as

Protein Processing, Post-TranslationalEquipment DesignEquipment Failure AnalysisPeptide MappingPhosphopeptidesPhosphorylationProteinsSequence Analysis, ProteinSpectrometry, Mass, Electrospray IonizationSpectroscopy, Fourier Transform InfraredPhosphopeptidesProteins

Identifiers

PMID16271296
OpenAlexW2108121781

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.