Evidence map›Paper›PMID 17915963›Full record

ArticleAnalytical chemistry2007

Top-down proteomics on a chromatographic time scale using linear ion trap fourier transform hybrid mass spectrometers.

Bryan A Parks, Lihua Jiang, Paul M Thomas, Craig D Wenger, Michael J Roth, Michael T Boyne, Patricia V Burke, Kurt E Kwast, Neil L Kelleher

Abstract read
In one paragraph

Article in Analytical chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

54 citing papers in PubMed, 120 citations in OpenAlex.

  1. Review
  2. Article
  3. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Progress in Top-Down Proteomics and the Analysis of Proteoforms.Annual review of analytical chemistry (Palo Alto, Calif.) · 2016
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Top Down proteomics: facts and perspectives.Biochemical and biophysical research communications · 2014
    Review
  19. Article
  20. 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

9 authors at 1 institution in 1 country.

Bryan A ParksDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Lihua Jiang
Paul M Thomas
Craig D Wenger
Michael J Roth
Michael T Boyne
Patricia V Burke
Kurt E Kwast
Neil L Kelleher
University of Illinois Urbana-Champaign · US

Funding

The UIUC Neuroproteomics Center on Cell-Cell SignalingP30DA018310 · NIDA · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI Elena V Romanova · 2004 to 2026
$24.9M
Training Program in Chemistry-Interface with BiologyT32GM070421 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HERGENROTHER, PAUL · 2005 to 2019
$5.4M
Eukaryotic Post-Translational ModificationsR01GM067193 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KELLEHER, NEIL L · 2003 to 2015
$4.0M
OXYGEN SENSING BY THE RESPIRATORY CHAINR01GM059826 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KWAST, KURT ERIC · 2001 to 2005
$1.1M
NIDA NIH HHS P30 DA018310NIGMS NIH HHS 5 T32 GM070421NIGMS NIH HHS GM59826NIGMS NIH HHS R01 GM059826NIGMS NIH HHS R01 GM067193NIGMS NIH HHS T32 GM070421
6 · The paper itself

Abstract

Proteomics has grown significantly with the aid of new technologies that consistently are becoming more streamlined. While processing of proteins from a whole cell lysate is typically done in a bottom-up fashion utilizing MS/MS of peptides from enzymatically digested proteins, top-down proteomics is becoming a viable alternative that until recently has been limited largely to offline analysis by tandem mass spectrometry. Here we describe a method for high-resolution tandem mass spectrometery of intact proteins on a chromatographic time scale. In a single liquid chromatography-tandem mass spectrometry (LC-MS/MS) run, we have identified 22 yeast proteins with molecular weights from 14 to 35 kDa. Using anion exchange chromatography to fractionate a whole cell lysate before online LC-MS/MS, we have detected 231 metabolically labeled (14N/15N) protein pairs from Saccharomyces cerevisiae. Thirty-nine additional proteins were identified and characterized from LC-MS/MS of selected anion exchange fractions. Automated localization of multiple acetylations on Histone H4 was also accomplished on an LC time scale from a complex protein mixture. To our knowledge, this is the first demonstration of top-down proteomics (i.e., many identifications) on linear ion trap Fourier transform (LTQ FT) systems using high-resolution MS/MS data obtained on a chromatographic time scale.

Indexed as

ProteomicsChromatography, LiquidFourier AnalysisMolecular WeightSaccharomyces cerevisiae ProteinsSensitivity and SpecificityTandem Mass SpectrometryTime FactorsSaccharomyces cerevisiae Proteins

Identifiers

PMID17915963
PMCPMC2361135
OpenAlexW2023959652

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.