Evidence map›Paper›PMID 25714988›Full record

ArticlePLoS computational biology2015

A theoretical justification for single molecule peptide sequencing.

Jagannath Swaminathan, Alexander A Boulgakov, Edward M Marcotte

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

42 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Review
  3. Principles ofbioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Photolysis of the peptide bond at 193 and 222 nm.The Journal of chemical physics · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Recent methodological advances towards single-cell proteomics.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023
    Review
  14. Article
  15. Single-molecule fluorescence methods for protein biomarker analysis.Analytical and bioanalytical chemistry · 2023
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Protein Sequencing, One Molecule at a Time.Annual review of biophysics · 2022
    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

3 authors at 1 institution in 1 country.

Jagannath SwaminathanCenter for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas, United States of America; Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, United States of America.
Alexander A BoulgakovCenter for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas, United States of America; Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, United States of America.
Edward M MarcotteCenter for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas, United States of America; Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, United States of America; Department of Molecular Biosciences, University of Texas at Austin, Austin, Texas, United States of America.
The University of Texas at Austin · US

Funding

Next-Generation Proteomics: Massively Parallel Single-Molecule Protein IdentificaDP1GM106408 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MARCOTTE, EDWARD M · 2012 to 2016
$3.8M
Howard Hughes Medical InstituteNIGMS NIH HHS DP1 GM106408
6 · The paper itself

Abstract

The proteomes of cells, tissues, and organisms reflect active cellular processes and change continuously in response to intracellular and extracellular cues. Deep, quantitative profiling of the proteome, especially if combined with mRNA and metabolite measurements, should provide an unprecedented view of cell state, better revealing functions and interactions of cell components. Molecular diagnostics and biomarker discovery should benefit particularly from the accurate quantification of proteomes, since complex diseases like cancer change protein abundances and modifications. Currently, shotgun mass spectrometry is the primary technology for high-throughput protein identification and quantification; while powerful, it lacks high sensitivity and coverage. We draw parallels with next-generation DNA sequencing and propose a strategy, termed fluorosequencing, for sequencing peptides in a complex protein sample at the level of single molecules. In the proposed approach, millions of individual fluorescently labeled peptides are visualized in parallel, monitoring changing patterns of fluorescence intensity as N-terminal amino acids are sequentially removed, and using the resulting fluorescence signatures (fluorosequences) to uniquely identify individual peptides. We introduce a theoretical foundation for fluorosequencing and, by using Monte Carlo computer simulations, we explore its feasibility, anticipate the most likely experimental errors, quantify their potential impact, and discuss the broad potential utility offered by a high-throughput peptide sequencing technology.

Indexed as

Amino AcidsComputational BiologyComputer SimulationDatabases, ProteinFluorescent DyesPeptidesSequence Analysis, ProteinAmino AcidsFluorescent DyesPeptides

Identifiers

PMID25714988
PMCPMC4341059
OpenAlexW2114169554

What OpenQuestion holds

Textmetadata
LicenceCC0
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.