Evidence map›Paper›PMID 37012480›Full record

ArticleNature methods2023

Prioritized mass spectrometry increases the depth, sensitivity and data completeness of single-cell proteomics.

R Gray Huffman, Andrew Leduc, Christoph Wichmann, Marco Di Gioia, Francesco Borriello, Harrison Specht, Jason Derks, Saad Khan, Luke Khoury, Edward Emmott and 5 more

Abstract read
In one paragraph

Article in Nature methods, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing 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

64 citing papers in PubMed.

  1. Review
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  11. Review
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  15. Article
  16. Review
  17. Plasma-Derived Extracellular Vesicle Proteomics.Journal of proteome research · 2025
    Review
  18. Article
  19. Article
  20. Article

4 more citing papers are in PubMed but not listed here.

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

15 authors.

R Gray HuffmanDepartments of Bioengineering, Biology, Chemistry and Chemical Biology, Single Cell Center and Barnett Institute, Northeastern University, Boston, MA, USA.
Andrew LeducDepartments of Bioengineering, Biology, Chemistry and Chemical Biology, Single Cell Center and Barnett Institute, Northeastern University, Boston, MA, USA.
Christoph WichmannComputational Systems Biochemistry Research Group, Max Planck Institute of Biochemistry, Martinsried, Germany.
Marco Di GioiaBoston Children's Hospital and Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0001-9499-5771
Francesco BorrielloBoston Children's Hospital and Harvard Medical School, Boston, MA, USA.
Harrison SpechtDepartments of Bioengineering, Biology, Chemistry and Chemical Biology, Single Cell Center and Barnett Institute, Northeastern University, Boston, MA, USA.
Jason DerksDepartments of Bioengineering, Biology, Chemistry and Chemical Biology, Single Cell Center and Barnett Institute, Northeastern University, Boston, MA, USA.ORCID http://orcid.org/0000-0001-9727-9105
Saad KhanDepartments of Bioengineering, Biology, Chemistry and Chemical Biology, Single Cell Center and Barnett Institute, Northeastern University, Boston, MA, USA.
Luke KhouryDepartments of Bioengineering, Biology, Chemistry and Chemical Biology, Single Cell Center and Barnett Institute, Northeastern University, Boston, MA, USA.ORCID http://orcid.org/0000-0001-7794-6812
Edward EmmottDepartments of Bioengineering, Biology, Chemistry and Chemical Biology, Single Cell Center and Barnett Institute, Northeastern University, Boston, MA, USA.ORCID http://orcid.org/0000-0002-3239-8178
Aleksandra A PetelskiDepartments of Bioengineering, Biology, Chemistry and Chemical Biology, Single Cell Center and Barnett Institute, Northeastern University, Boston, MA, USA.
David H PerlmanMerck Exploratory Sciences Center, Merck Sharp and Dohme Corp., Cambridge, MA, USA.
Jürgen CoxComputational Systems Biochemistry Research Group, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0001-8597-205X
Ivan ZanoniBoston Children's Hospital and Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0002-3423-7474
Nikolai SlavovDepartments of Bioengineering, Biology, Chemistry and Chemical Biology, Single Cell Center and Barnett Institute, Northeastern University, Boston, MA, USA. nslavov@northeastern.edu.ORCID http://orcid.org/0000-0003-2035-1820

Funding

Ribosome-mediated translational regulation during stem cell differentiationDP2GM123497 · NIGMS · NORTHEASTERN UNIVERSITY · PI SLAVOV, NIKOLAI · 2016 to 2016
$2.4M
Single-cell proteomic identification of novel markers of senescenceUG3CA268117 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI DOU, ZHIXUN, RAJAGOPAL, JAYARAJ · 2021 to 2022
$1.2M
Collaborative Research: DMS/NIGMS 2: Methods for Systematic Analysis of Post-transcriptional Regulation in Single CellsR01GM144967 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI FRANKS, ALEXANDER, SLAVOV, NIKOLAI · 2021 to 2024
$779k
NCI NIH HHS UG3 CA268117NIGMS NIH HHS DP2 GM123497NIGMS NIH HHS R01 GM144967
6 · The paper itself

Abstract

Major aims of single-cell proteomics include increasing the consistency, sensitivity and depth of protein quantification, especially for proteins and modifications of biological interest. Here, to simultaneously advance all these aims, we developed prioritized Single-Cell ProtEomics (pSCoPE). pSCoPE consistently analyzes thousands of prioritized peptides across all single cells (thus increasing data completeness) while maximizing instrument time spent analyzing identifiable peptides, thus increasing proteome depth. These strategies increased the sensitivity, data completeness and proteome coverage over twofold. The gains enabled quantifying protein variation in untreated and lipopolysaccharide-treated primary macrophages. Within each condition, proteins covaried within functional sets, including phagosome maturation and proton transport, similarly across both treatment conditions. This covariation is coupled to phenotypic variability in endocytic activity. pSCoPE also enabled quantifying proteolytic products, suggesting a gradient of cathepsin activities within a treatment condition. pSCoPE is freely available and widely applicable, especially for analyzing proteins of interest without sacrificing proteome coverage. Support for pSCoPE is available at http://scp.slavovlab.net/pSCoPE .

Indexed as

ProteomeProteomicsMacrophagesMass SpectrometryPeptidesPeptidesProteome

Identifiers

PMID37012480
PMCPMC10172113

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Registered trials

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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.