Evidence map›Paper›PMID 29476010›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Highly multiplexed and quantitative cell-surface protein profiling using genetically barcoded antibodies.

Samuel B Pollock, Amy Hu, Yun Mou, Alexander J Martinko, Olivier Julien, Michael Hornsby, Lynda Ploder, Jarrett J Adams, Huimin Geng, Markus Müschen and 3 more

Open access · bronzeAbstract readEvaluation Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Proximity-activated DNA scanning encoded sequencing for massive access to membrane proteins nanoscale organization.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Recent methodological advances towards single-cell proteomics.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023
    Review
  6. Review
  7. Engineered molecular sensors for quantifying cell surface crowding.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Deep profiling of protease substrate specificity enabled by dual random and scanned human proteome substrate phage libraries.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Why recombinant antibodies - benefits and applications.Current opinion in biotechnology · 2019
    Review
  19. Article
  20. 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

13 authors at 2 institutions in 2 countries.

Samuel B PollockDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.
Amy HuDonnelly Centre, University of Toronto, Toronto, ON M5S 3E1, Canada.
Yun MouDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.
Alexander J MartinkoDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.
Olivier JulienDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.ORCID 0000-0001-7068-7299
Michael HornsbyDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.ORCID 0000-0002-2304-9961
Lynda PloderDonnelly Centre, University of Toronto, Toronto, ON M5S 3E1, Canada.
Jarrett J AdamsDonnelly Centre, University of Toronto, Toronto, ON M5S 3E1, Canada.
Huimin GengDepartment of Laboratory Medicine, University of California, San Francisco, CA 94143.
Markus MüschenDepartment of Laboratory Medicine, University of California, San Francisco, CA 94143.
Sachdev S SidhuDonnelly Centre, University of Toronto, Toronto, ON M5S 3E1, Canada.
Jason MoffatDonnelly Centre, University of Toronto, Toronto, ON M5S 3E1, Canada.
James A WellsDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143; jim.wells@ucsf.edu.ORCID 0000-0001-8267-5519
University of California, San Francisco · USUniversity of Toronto · CA

Funding

Metabolic gatekeepers in B-cell malignanciesR35CA197628 · NCI · YALE UNIVERSITY · PI Markus Müschen · 2016 to 2026
$11.7M
RESEARCH TRAINING IN CHEMISTRY AND CHEMICAL BIOLOGYT32GM064337 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2002 to 2021
$7.8M
Renewable antibodies to secreted proteins and single and multi-pass cell surfaceP41CA196276 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2014 to 2018
$5.8M
Surfaceomic technologies and antibodies to probe cell surface proteomes and their interactomes at unprecedented small scale and high-resolutionR35GM122451 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JAMES A WELLS · 2017 to 2026
$5.3M
CD25-mediated feedback control of BCR-signaling and its oncogenic mimicsR01CA213138 · NCI · YALE UNIVERSITY · PI MÜSCHEN, MARKUS · 2017 to 2022
$1.9M
Affinity-directed tagging of protein binding partners in signalingR01CA191018 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WELLS, JAMES A · 2014 to 2018
$1.6M
Pacific Biosciences PacBio RS Single Molecule Real Time SequencerS10OD018174 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI ROKHSAR, DANIEL SOLEYMAN · 2014 to 2014
$600k
CIHR 342551CIHR 365646NCI NIH HHS P41 CA196276NCI NIH HHS R01 CA191018NCI NIH HHS R01 CA213138NCI NIH HHS R35 CA197628NIGMS NIH HHS R35 GM122451NIGMS NIH HHS T32 GM064337NIH HHS S10 OD018174
6 · The paper itself

Abstract

Human cells express thousands of different surface proteins that can be used for cell classification, or to distinguish healthy and disease conditions. A method capable of profiling a substantial fraction of the surface proteome simultaneously and inexpensively would enable more accurate and complete classification of cell states. We present a highly multiplexed and quantitative surface proteomic method using genetically barcoded antibodies called phage-antibody next-generation sequencing (PhaNGS). Using 144 preselected antibodies displayed on filamentous phage (Fab-phage) against 44 receptor targets, we assess changes in B cell surface proteins after the development of drug resistance in a patient with acute lymphoblastic leukemia (ALL) and in adaptation to oncogene expression in a Myc-inducible Burkitt lymphoma model. We further show PhaNGS can be applied at the single-cell level. Our results reveal that a common set of proteins including FLT3, NCR3LG1, and ROR1 dominate the response to similar oncogenic perturbations in B cells. Linking high-affinity, selective, genetically encoded binders to NGS enables direct and highly multiplexed protein detection, comparable to RNA-sequencing for mRNA. PhaNGS has the potential to profile a substantial fraction of the surface proteome simultaneously and inexpensively to enable more accurate and complete classification of cell states.

Indexed as

AntibodiesBacteriophagesBurkitt LymphomaCell Line, TumorHigh-Throughput Nucleotide SequencingHumansLeukemiaMembrane ProteinsProteomicsAntibodiesMembrane Proteinsbiomarkerscell surface proteomicsleukemiaNGSphage display

Identifiers

PMID29476010
PMCPMC5856557
OpenAlexW2794384903

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.