Evidence map›Paper›PMID 22356091›Full record

ArticleAnalytical chemistry2012

Nano-LC FTICR tandem mass spectrometry for top-down proteomics: routine baseline unit mass resolution of whole cell lysate proteins up to 72 kDa.

Jeremiah D Tipton, John C Tran, Adam D Catherman, Dorothy R Ahlf, Kenneth R Durbin, Ji Eun Lee, John F Kellie, Neil L Kelleher, Christopher L Hendrickson, Alan G Marshall

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Top Down proteomics: facts and perspectives.Biochemical and biophysical research communications · 2014
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Chemometric data analysis for deconvolution of overlapped ion mobility profiles.Journal of the American Society for Mass Spectrometry · 2012
    Article
  18. Review
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 3 institutions in 1 country.

Jeremiah D TiptonIon Cyclotron Resonance Program, National High Magnetic Field Laboratory, Florida State University, 1800 East Paul Dirac Drive, Tallahassee, Florida 32310-4005, USA.
John C Tran
Adam D Catherman
Dorothy R Ahlf
Kenneth R Durbin
Ji Eun Lee
John F Kellie
Neil L Kelleher
Christopher L Hendrickson
Alan G Marshall
Northwestern University · USFlorida State University · USNational High Magnetic Field Laboratory · US

Funding

Eukaryotic Post-Translational ModificationsR01GM067193 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KELLEHER, NEIL L · 2003 to 2015
$4.0M
Structural Mapping of Protein Complexes by Hydrogen/Deuterium ExchangeR01GM078359 · NIGMS · FLORIDA STATE UNIVERSITY · PI MARSHALL, ALAN G · 2006 to 2009
$1.2M
NIGMS NIH HHS GM-067193-08NIGMS NIH HHS R01 GM067193NIGMS NIH HHS R01 GM078359
6 · The paper itself

Abstract

Current high-throughput top-down proteomic platforms provide routine identification of proteins less than 25 kDa with 4-D separations. This short communication reports the application of technological developments over the past few years that improve protein identification and characterization for masses greater than 25 kDa. Advances in separation science have allowed increased numbers of proteins to be identified, especially by nanoliquid chromatography (nLC) prior to mass spectrometry (MS) analysis. Further, a goal of high-throughput top-down proteomics is to extend the mass range for routine nLC MS analysis up to 80 kDa because gene sequence analysis predicts that ~70% of the human proteome is transcribed to be less than 80 kDa. Normally, large proteins greater than 50 kDa are identified and characterized by top-down proteomics through fraction collection and direct infusion at relatively low throughput. Further, other MS-based techniques provide top-down protein characterization, however at low resolution for intact mass measurement. Here, we present analysis of standard (up to 78 kDa) and whole cell lysate proteins by Fourier transform ion cyclotron resonance mass spectrometry (nLC electrospray ionization (ESI) FTICR MS). The separation platform reduced the complexity of the protein matrix so that, at 14.5 T, proteins from whole cell lysate up to 72 kDa are baseline mass resolved on a nano-LC chromatographic time scale. Further, the results document routine identification of proteins at improved throughput based on accurate mass measurement (less than 10 ppm mass error) of precursor and fragment ions for proteins up to 50 kDa.

Indexed as

Chromatography, High Pressure LiquidNanotechnologySpectrometry, Mass, Electrospray IonizationFourier AnalysisHeLa CellsHumansIsoelectric FocusingMolecular WeightProteinsProteomicsProteins

Identifiers

PMID22356091
PMCPMC3297430
OpenAlexW2028089076

What OpenQuestion holds

Textmetadata
LicenceTDM
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.