Evidence map›Paper›PMID 25894527›Full record

ArticlePloS one2015

A mass spectrometric-derived cell surface protein atlas.

Damaris Bausch-Fluck, Andreas Hofmann, Thomas Bock, Andreas P Frei, Ferdinando Cerciello, Andrea Jacobs, Hansjoerg Moest, Ulrich Omasits, Rebekah L Gundry, Charles Yoon and 10 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 283 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
283citing papers in PubMed, 1 pooled it
11.0field-weighted citation impact, top 1% 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

283 citing papers in PubMed, 1 synthesis or guideline pooled it, 464 citations in OpenAlex.

  1. Pooled it
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223 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

20 authors at 7 institutions in 5 countries.

Damaris Bausch-FluckInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland; Department of Health Sciences and Technology, BMPP, ETH Zurich, Zurich, Switzerland.
Andreas HofmannInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Thomas BockInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Andreas P FreiInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Ferdinando CercielloInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland; Laboratory of Molecular Oncology, University Hospital Zurich, Zurich, Switzerland.
Andrea JacobsInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Hansjoerg MoestInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Ulrich OmasitsInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland; Department of Health Sciences and Technology, BMPP, ETH Zurich, Zurich, Switzerland.
Rebekah L GundryDepartment of Biochemistry, Medical College of Wisconsin, Wisconsin, Milwaukee, United States of America.
Charles YoonInstitute for Biomaterials & Biomedical Engineering, University of Toronto, Toronto, Canada.
Ralph SchiessInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Alexander SchmidtInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Paulina MirkowskaInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland; Oncology Research Laboratory, University Children Hospital Zurich, Zurich, Switzerland.
Anetta HärtlováCentre of Advanced Studies, Faculty of Military Health Sciences, University of Defense, Hradec Kralove, Czech Republic.
Jennifer E Van EykDepartment of Medicine, Biological Chemistry and Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.
Jean-Pierre BourquinOncology Research Laboratory, University Children Hospital Zurich, Zurich, Switzerland.
Ruedi AebersoldInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland; Center for Systems Physiology and Metabolic Diseases, Zurich, Switzerland; Faculty of Science, University of Zurich, Zurich, Switzerland.
Kenneth R BohelerSCRMC, LKS Faculty of Medicine, Hong Kong University, Hong Kong, Hong Kong SAR; Division of Cardiology, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States of America.
Peter ZandstraInstitute for Biomaterials & Biomedical Engineering, University of Toronto, Toronto, Canada.
Bernd WollscheidInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland; Department of Health Sciences and Technology, BMPP, ETH Zurich, Zurich, Switzerland.
ETH Zurich · CHJohns Hopkins Medicine · USUniversity Children's Hospital Zurich · CHUniversity of Toronto · CACenter for Pediatric Endocrinology Zurich · CHMedical College of Wisconsin · USUniversity of Defence · CZ

Funding

Glycoprotein biomarkers for the early detection of aggressive prostate cancerU01CA152813 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2010 to 2021
$6.2M
NCI NIH HHS U01 CA152813NCI NIH HHS U01CA152813
6 · The paper itself

Abstract

Cell surface proteins are major targets of biomedical research due to their utility as cellular markers and their extracellular accessibility for pharmacological intervention. However, information about the cell surface protein repertoire (the surfaceome) of individual cells is only sparsely available. Here, we applied the Cell Surface Capture (CSC) technology to 41 human and 31 mouse cell types to generate a mass-spectrometry derived Cell Surface Protein Atlas (CSPA) providing cellular surfaceome snapshots at high resolution. The CSPA is presented in form of an easy-to-navigate interactive database, a downloadable data matrix and with tools for targeted surfaceome rediscovery (http://wlab.ethz.ch/cspa). The cellular surfaceome snapshots of different cell types, including cancer cells, resulted in a combined dataset of 1492 human and 1296 mouse cell surface glycoproteins, providing experimental evidence for their cell surface expression on different cell types, including 136 G-protein coupled receptors and 75 membrane receptor tyrosine-protein kinases. Integrated analysis of the CSPA reveals that the concerted biological function of individual cell types is mainly guided by quantitative rather than qualitative surfaceome differences. The CSPA will be useful for the evaluation of drug targets, for the improved classification of cell types and for a better understanding of the surfaceome and its concerted biological functions in complex signaling microenvironments.

Indexed as

AnimalsCell LineDatabases, ProteinHumansMass SpectrometryMembrane ProteinsMiceProteomicsMembrane Proteins

Identifiers

PMID25894527
PMCPMC4404347
OpenAlexW1985255881

What OpenQuestion holds

Textmetadata
LicenceCC0
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.