Evidence map›Paper›PMID 34985940›Full record

ReviewAnnual review of biophysics2022

Protein Sequencing, One Molecule at a Time.

Brendan M Floyd, Edward M Marcotte

Open access · bronzeAbstract readReview
In one paragraph

Review in Annual review of biophysics, 2022. 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
3.6field-weighted citation impact, top 6% 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, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Photolysis of the peptide bond at 193 and 222 nm.The Journal of chemical physics · 2025
    Article
  6. Paleoproteomics sheds light on million-year-old fossils.Nature reviews. Molecular cell biology · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Single-molecule fluorescence methods for protein biomarker analysis.Analytical and bioanalytical chemistry · 2023
    Review
  15. Review
  16. Article
  17. Uncovering biology by single-cell proteomics.Communications biology · 2023
    Review
  18. Cell-Free Production Systems in Droplet Microfluidics.Advances in biochemical engineering/biotechnology · 2023
    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

2 authors at 1 institution in 1 country.

Brendan M FloydDepartment of Molecular Biosciences, Center for Systems and Synthetic Biology, University of Texas, Austin, Texas, USA; email: bmfloyd@utexas.edu, marcotte@utexas.edu.
Edward M MarcotteDepartment of Molecular Biosciences, Center for Systems and Synthetic Biology, University of Texas, Austin, Texas, USA; email: bmfloyd@utexas.edu, marcotte@utexas.edu.
The University of Texas at Austin · US

Funding

Mapping the CPLANE interactome, an extensive protein interaction network underlying human ciliopathiesR01HD085901 · NICHD · UNIVERSITY OF TEXAS AT AUSTIN · PI EDWARD M MARCOTTE, John B Wallingford · 2016 to 2026
$6.2M
Proteomics and model organism humanization to decode human geneticsR35GM122480 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI EDWARD M MARCOTTE · 2017 to 2026
$5.4M
NICHD NIH HHS R01 HD085901NIGMS NIH HHS R35 GM122480
6 · The paper itself

Abstract

Despite tremendous gains over the past decade, methods for characterizing proteins have generally lagged behind those for nucleic acids, which are characterized by extremely high sensitivity, dynamic range, and throughput. However, the ability to directly characterize proteins at nucleic acid levels would address critical biological challenges such as more sensitive medical diagnostics, deeper protein quantification, large-scale measurement, and discovery of alternate protein isoforms and modifications and would open new paths to single-cell proteomics. In response to this need, there has been a push to radically improve protein sequencing technologies by taking inspiration from high-throughput nucleic acid sequencing, with a particular focus on developing practical methods for single-molecule protein sequencing (SMPS). SMPS technologies fall generally into three categories: sequencing by degradation (e.g., mass spectrometry or fluorosequencing), sequencing by transit (e.g., nanopores or quantum tunneling), and sequencing by affinity (as in DNA hybridization-based approaches). We describe these diverse approaches, which range from those that are already experimentally well-supported to the merely speculative, in this nascent field striving to reformulate proteomics.

Indexed as

NanoporesNucleic AcidsHigh-Throughput Nucleotide SequencingNanotechnologyProteinsSequence Analysis, ProteinNucleic AcidsProteinsDNA nanotechnologyfluorescencefluorosequencingnanoporesproteomicssingle-molecule protein sequencingSMPS

Identifiers

PMID34985940
PMCPMC9809159
OpenAlexW4205214909

What Socratic 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 Socratic graph.