Evidence map›Paper›PMID 20828161›Full record

ArticleJournal of proteome research2010

Mapping tissue-specific expression of extracellular proteins using systematic glycoproteomic analysis of different mouse tissues.

Yuan Tian, Karen S Kelly-Spratt, Christopher J Kemp, Hui Zhang

Abstract read
In one paragraph

Article in Journal of proteome research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Long-term temporal stability of circulating proteins in older adults.bioRxiv : the preprint server for biology · 2025
    Article
  3. Mapping the cancer surface proteome in search of target antigens for immunotherapy.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Review
  4. Faster skin wound healing predicts survival after myocardial infarction.American journal of physiology. Heart and circulatory physiology · 2022
    Article
  5. Cell free DNA as a diagnostic and prognostic marker for cardiovascular diseases.Clinica chimica acta; international journal of clinical chemistry · 2020
    Review
  6. Article
  7. Article
  8. Review
  9. Article
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  11. Article
  12. Article
  13. Review
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  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Glycoproteomic and glycomic databases.Clinical proteomics · 2014
    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

4 authors at 2 institutions in 1 country.

Yuan TianDepartment of Pathology, Johns Hopkins University, Baltimore, MD 21287, USA.
Karen S Kelly-Spratt
Christopher J Kemp
Hui Zhang
Johns Hopkins University · USFred Hutch Cancer Center · US

Funding

Glycoprotein biomarkers for the early detection of aggressive prostate cancerU01CA152813 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2010 to 2021
$6.2M
Profile serum proteins by glycopeptide capture and LC-MSR21CA114852 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2005 to 2006
$331k
NCI NIH HHS R21 CA114852NCI NIH HHS R21-CA-114852NCI NIH HHS U01 CA152813
6 · The paper itself

Abstract

Due to their easy accessibility, proteins outside of the plasma membrane represent an ideal but untapped resource for potential drug targets or disease biomarkers. They constitute the major biochemical class of current therapeutic targets and clinical biomarkers. Recent advances in proteomic technologies have fueled interest in analysis of extracellular proteins such as membrane proteins, cell surface proteins, and secreted proteins. However, unlike the gene expression analyses from a variety of tissues and cells using genomic technologies, quantitative proteomic analysis of proteins from various biological sources is challenging due to the high complexity of different proteomes and the lack of robust and consistent methods for analyses of different tissue sources, especially for specific enrichment of extracellular proteins. Since most extracellular proteins are modified by oligosaccharides, the population of glycoproteins therefore represents the majority of extracellular proteomes. Here, we quantitatively analyzed glycoproteins and determined the expression patterns of extracellular proteins from 12 mouse tissues using solid-phase extraction of N-linked glycopeptides and liquid chromatography-tandem mass spectrometry. We identified peptides enclosing 1231 possible N-linked glycosites from 826 unique proteins. We further determined the expression pattern of formerly N-linked glycopeptides and identified extracellular glycoproteins specifically expressed in each tissue. Furthermore, the tissue specificities of the overexpressed glycoproteins in a mouse skin tumor model were determined by comparing them to the quantitative protein expression from the different tissues. These skin tumor-specific extracellular proteins might serve as potential candidates for cell surface drug targets or disease-specific protein markers.

Indexed as

AnimalsBiomarkersGene Expression RegulationGlycoproteinsMiceProteomicsSkin NeoplasmsSolid Phase ExtractionTandem Mass SpectrometryTissue DistributionBiomarkersGlycoproteins

Identifiers

PMID20828161
PMCPMC2988866
OpenAlexW2001323302

What OpenQuestion holds

Textmetadata
LicenceTDM
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.