Evidence map›Paper›PMID 40178992›Full record

ReviewChemical reviews2025

Engineered Proteins and Chemical Tools to Probe the Cell Surface Proteome.

Kevin K Leung, Kaitlin Schaefer, Zhi Lin, Zi Yao, James A Wells

Abstract readReview
In one paragraph

Review in Chemical reviews, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Chemical Biology 2025: Highlights From the Ch/Bi145 Course at Caltech.Chembiochem : a European journal of chemical biology · 2026
    Review
  3. Review
  4. Article
  5. Review
  6. AbioRxiv : the preprint server for biology · 2026
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
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

5 authors.

Kevin K LeungDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94158, United States.ORCID 0000-0002-2087-4974
Kaitlin SchaeferDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94158, United States.ORCID 0000-0003-4825-1389
Zhi LinDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94158, United States.
Zi YaoDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94158, United States.
James A WellsDepartment of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94158, United States.ORCID 0000-0001-8267-5519

Funding

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
New protein engineering-based tools and technologies for characterizing cell surface proteolysis in cancer cells for novel neo-epitope biomarkers and drug targetsR01CA248323 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JAMES A WELLS · 2020 to 2026
$2.6M
Mapping tumor specific immunopeptidome for antibody-based targeted therapyF32GM149084 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI YAO, ZI · 2023 to 2024
$143k
NCI NIH HHS R01 CA248323NIGMS NIH HHS F32 GM149084NIGMS NIH HHS R35 GM122451
6 · The paper itself

Abstract

The cell surface proteome, or surfaceome, is the hub for cells to interact and communicate with the outside world. Many disease-associated changes are hard-wired within the surfaceome, yet approved drugs target less than 50 cell surface proteins. In the past decade, the proteomics community has made significant strides in developing new technologies tailored for studying the surfaceome in all its complexity. In this review, we first dive into the unique characteristics and functions of the surfaceome, emphasizing the necessity for specialized labeling, enrichment, and proteomic approaches. An overview of surfaceomics methods is provided, detailing techniques to measure changes in protein expression and how this leads to novel target discovery. Next, we highlight advances in proximity labeling proteomics (PLP), showcasing how various enzymatic and photoaffinity proximity labeling techniques can map protein-protein interactions and membrane protein complexes on the cell surface. We then review the role of extracellular post-translational modifications, focusing on cell surface glycosylation, proteolytic remodeling, and the secretome. Finally, we discuss methods for identifying tumor-specific peptide MHC complexes and how they have shaped therapeutic development. This emerging field of neo-protein epitopes is constantly evolving, where targets are identified at the proteome level and encompass defined disease-associated PTMs, complexes, and dysregulated cellular and tissue locations. Given the functional importance of the surfaceome for biology and therapy, we view surfaceomics as a critical piece of this quest for neo-epitope target discovery.

Indexed as

Membrane ProteinsProtein EngineeringProteomeProteomicsAnimalsHumansProtein Processing, Post-TranslationalMembrane ProteinsProteome

Identifiers

PMID40178992
PMCPMC12022999

What OpenQuestion holds

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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.