Evidence map›Paper›PMID 19708673›Full record

ArticleAnalytical chemistry2009

Ultrafast differential ion mobility spectrometry at extreme electric fields coupled to mass spectrometry.

Alexandre A Shvartsburg, Keqi Tang, Richard D Smith, Martin Holden, Martyn Rush, Andrew Thompson, Danielle Toutoungi

Open access · greenAbstract 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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.0field-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, 57 citations in OpenAlex.

  1. Review
  2. Maximizing Ion Transmission in Differential Mobility Spectrometry.Journal of the American Society for Mass Spectrometry · 2017
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Differential ion mobility separations in up to 100% helium using microchips.Journal of the American Society for Mass Spectrometry · 2014
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. A high voltage asymmetric waveform generator for FAIMS.Journal of the American Society for Mass Spectrometry · 2010
    Article
  13. 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

7 authors at 2 institutions in 2 countries.

Alexandre A ShvartsburgBiological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, Richland, Washington 99352, USA.
Keqi Tang
Richard D Smith
Martin Holden
Martyn Rush
Andrew Thompson
Danielle Toutoungi
Pacific Northwest National Laboratory · USOwlstone Medical (United Kingdom) · GB

Funding

WORKSHOP AND TRAINING ACTIVITIESP41RR018522 · NCRR · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2003 to 2011
$25.1M
NCRR NIH HHS P41 RR018522
6 · The paper itself

Abstract

Microchip-based field asymmetric waveform ion mobility spectrometry (FAIMS) analyzers featuring a grid of 35 mum-wide channels have allowed electric field intensity (E) over 60 kV/cm, or about twice that in previous devices with >0.5 mm gaps. Since the separation speed scales as E4 to E6, these chips filter ions in just approximately 20 micros (or approximately 100-10,000 times faster than "macroscopic" designs), although with reduced resolution. Here we report integration of these chips into electrospray ionization (ESI) mass spectrometry, with ESI coupled to FAIMS via a curtain plate/orifice interface with edgewise ion injection into the gap. Adjusting gas flows in the system permits control of ion residence time in FAIMS, which affects resolving power independently of ion desolvation after the ESI source. The results agree with a priori simulations and scaling rules. Applications illustrated include analyses of amino acids and peptides. Because of limited resolving power, the present FAIMS units are more suitable for distinguishing compound classes than individual species. In particular, peptides separate from many other classes, including PEGs that are commonly encountered in proteomic analyses. In practical analyses with realistic time constraints, the effective separation power of present FAIMS may approach that of "macroscopic" systems.

Indexed as

Amino AcidsIonsLeucinePeptidesSpectrometry, Mass, Electrospray IonizationAmino AcidsIonsLeucinePeptides

Identifiers

PMID19708673
PMCPMC2951030
OpenAlexW1974287152

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.