ArticleNature biotechnology2018
Highly parallel single-molecule identification of proteins in zeptomole-scale mixtures.
Article in Nature biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.
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.
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.
Who cites it
104 citing papers in PubMed, 223 citations in OpenAlex.
- Optimization of the Quantum-Si Platinum Single-Molecule Protein Sequencing Platform Toward Improved Complex-Matrix Protein Identification.ACS omega · 2026Article
- Monitoring in vivo transcription with synthetic serum markers.Nature communications · 2026Article
- Nanopore Fingerprinting of Neurodegenerative Proteins and Phosphoproteins within a Minute.JACS Au · 2026Article
- Label-Free Optical Differentiation of Single Diffusing Amino Acids at Picomolar Concentrations.Research square · 2026Article
- Unlocking the Silent Proteome: Chemoselective Asn/Gln Activation for Multidimensional Protein Diversification.Journal of the American Chemical Society · 2026Article
- Proteoforms as the true units of physiological function.European journal of applied physiology · 2026Review
- Principles ofbioRxiv : the preprint server for biology · 2026Article
- A Graphene Field-Effect Transistor-Based Biosensor Platform for the Electrochemical Profiling of Amino Acids.Biosensors · 2026Article
- Protein abundance inference via expectation-maximization in fluorosequencing.Bioinformatics advances · 2026Article
- Full-length protein classification via cysteine fingerprinting in solid-state nanopores.Nature nanotechnology · 2025Article
- Article
- Protein Sequencing with Single Amino Acid Resolution Discerns Peptides That Discriminate Tropomyosin Proteoforms.Journal of proteome research · 2025Article
- Single-Molecule Enzyme Activity Analysis for Illuminating Pathological Proteoforms.ACS central science · 2025Review
- Exploring a solid-state nanopore approach for single-molecule protein detection from single cells.Chemical science · 2025Article
- After 75 Years, an Alternative to Edman Degradation: A Mechanistic and Efficiency Study of a Base-Induced Method for N-Terminal Peptide Sequencing.Journal of the American Chemical Society · 2025Article
- Article
- Virolithopanspermia: Might viruses be transported in rocks through space?PLoS pathogens · 2025Article
- Towards improved biofilm models.Nature reviews. Microbiology · 2025Review
- A generalized protein identification method for novel and diverse sequencing technologies.NAR genomics and bioinformatics · 2024Article
- Article
44 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
The identification and quantification of proteins lags behind DNA-sequencing methods in scale, sensitivity, and dynamic range. Here, we show that sparse amino acid-sequence information can be obtained for individual protein molecules for thousands to millions of molecules in parallel. We demonstrate selective fluorescence labeling of cysteine and lysine residues in peptide samples, immobilization of labeled peptides on a glass surface, and imaging by total internal reflection microscopy to monitor decreases in each molecule's fluorescence after consecutive rounds of Edman degradation. The obtained sparse fluorescent sequence of each molecule was then assigned to its parent protein in a reference database. We tested the method on synthetic and naturally derived peptide molecules in zeptomole-scale quantities. We also fluorescently labeled phosphoserines and achieved single-molecule positional readout of the phosphorylated sites. We measured >93% efficiencies for dye labeling, survival, and cleavage; further improvements should enable studies of increasingly complex proteomic mixtures, with the high sensitivity and digital quantification offered by single-molecule sequencing.
Identifiers
What OpenQuestion holds
Registered trials
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.