Evidence map›Paper›PMID 24475910›Full record

ArticleAnalytical chemistry2014

Neutron-encoded mass signatures for quantitative top-down proteomics.

Timothy W Rhoads, Christopher M Rose, Derek J Bailey, Nicholas M Riley, Rosalynn C Molden, Amelia J Nestler, Anna E Merrill, Lloyd M Smith, Alexander S Hebert, Michael S Westphall and 3 more

Abstract read
In one paragraph

Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Analytical and bioanalytical chemistry · 2024
    Article
  3. Article
  4. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Top-Down Proteomics: Ready for Prime Time?Analytical chemistry · 2018
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

13 authors.

Timothy W RhoadsDepartment of Chemistry, ‡Department of Biomolecular Chemistry, §Genome Center, and ∇Department of Biochemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.
Christopher M Rose
Derek J Bailey
Nicholas M Riley
Rosalynn C Molden
Amelia J Nestler
Anna E Merrill
Lloyd M Smith
Alexander S Hebert
Michael S Westphall
David J Pagliarini
Benjamin A Garcia
Joshua J Coon

Funding

Research Training for Computation and Informatics in Biology and MedicineT15LM007359 · NLM · UNIVERSITY OF WISCONSIN-MADISON · PI Mark W. Craven, Colin Noel Dewey · 2002 to 2026
$22.6M
GRADUATE TRAINING IN MOLECULAR BIOSCIENCEST32GM007215 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HULL, CHRISTINA M · 1985 to 2018
$22.5M
Institutional Training in the Genomic SciencesT32HG002760 · NHGRI · UNIVERSITY OF WISCONSIN-MADISON · PI Qiongshi Lu · 2003 to 2026
$17.7M
Chemistry-Biology Interface Training ProgramT32GM008505 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BLACKWELL, HELEN E. · 1993 to 2023
$9.8M
Regulation of Mitochondrial Metabolism by Post-Translational ModificationsR01DK098672 · NIDDK · WASHINGTON UNIVERSITY · PI David J Pagliarini · 2013 to 2026
$4.8M
Sequential Ion/Ion Reactions for Large Peptide and Whole Protein CharacterizationR01GM080148 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J · 2007 to 2015
$3.0M
Novel Methodology for Quantitative High-throughput Cancer EpigeneticsDP2OD007447 · OD · UNIVERSITY OF PENNSYLVANIA · PI GARCIA, BENJAMIN A · 2010 to 2010
$2.4M
NHGRI NIH HHS T32 HG002760NIDDK NIH HHS R01 DK098672NIDDK NIH HHS R01DK098672NIGMS NIH HHS 5T32GM007215-37NIGMS NIH HHS R01 GM080148NIGMS NIH HHS R01GM080148NIGMS NIH HHS T32 GM007215NIGMS NIH HHS T32 GM008505NIGMS NIH HHS T32GM008505NIH HHS DP2 OD007447NIH HHS DP2OD007447NLM NIH HHS T15 LM007359
6 · The paper itself

Abstract

The ability to acquire highly accurate quantitative data is an increasingly important part of any proteomics experiment, whether shotgun or top-down approaches are used. We recently developed a quantitation strategy for peptides based on neutron encoding, or NeuCode SILAC, which uses closely spaced heavy isotope-labeled amino acids and high-resolution mass spectrometry to provide quantitative data. We reasoned that the strategy would also be applicable to intact proteins and could enable robust, multiplexed quantitation for top-down experiments. We used yeast lysate labeled with either (13)C6(15)N2-lysine or (2)H8-lysine, isotopologues of lysine that are spaced 36 mDa apart. Proteins having such close spacing cannot be distinguished during a medium resolution scan, but upon acquiring a high-resolution scan, the two forms of the protein with each amino acid are resolved and the quantitative information revealed. An additional benefit NeuCode SILAC provides for top down is that the spacing of the isotope peaks indicates the number of lysines present in the protein, information that aids in identification. We used NeuCode SILAC to quantify several hundred isotope distributions, manually identify and quantify proteins from 1:1, 3:1, and 5:1 mixed ratios, and demonstrate MS(2)-based quantitation using ETD.

Indexed as

NeutronsProteomicsMass SpectrometrySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID24475910
PMCPMC3983007

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.