Evidence map›Paper›PMID 33536314›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Mapping proteolytic neo-N termini at the surface of living cells.

Amy M Weeks, James R Byrnes, Irene Lui, James A Wells

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
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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

4 authors at 1 institution in 1 country.

Amy M WeeksDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.
James R ByrnesDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.
Irene LuiDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143.ORCID 0000-0002-6171-5443
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 · US

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
Global Analysis of Proteolysis in ApoptosisR01GM081051 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WELLS, JAMES A · 2007 to 2015
$2.8M
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
Characterizing and Targeting the Hypoxic T Cell Surfaceome to Promote Immune Function in CancerF32CA239417 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BYRNES, JAMES ROBERT · 2019 to 2021
$191k
NCI NIH HHS F32 CA239417NIGMS NIH HHS R01 GM081051
6 · The paper itself

Abstract

N terminomics is a powerful strategy for profiling proteolytic neo-N termini, but its application to cell surface proteolysis has been limited by the low relative abundance of plasma membrane proteins. Here we apply plasma membrane-targeted subtiligase variants (subtiligase-TM) to efficiently and specifically capture cell surface N termini in live cells. Using this approach, we sequenced 807 cell surface N termini and quantified changes in their abundance in response to stimuli that induce proteolytic remodeling of the cell surface proteome. To facilitate exploration of our datasets, we developed a web-accessible Atlas of Subtiligase-Captured Extracellular N Termini (ASCENT; http://wellslab.org/ascent). This technology will facilitate greater understanding of extracellular protease biology and reveal neo-N termini biomarkers and targets in disease.

Indexed as

Cell MembraneHEK293 CellsHumansMutationPeptide MappingPeptide SynthasesProtein Processing, Post-TranslationalProteolysisSubtilisinsPeptide SynthasessubtiligaseSubtilisinsN terminomicsproteolysisproteomics

Identifiers

PMID33536314
PMCPMC7923363
OpenAlexW3127447598

What Socratic holds

Textmetadata
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.