Evidence map›Paper›PMID 23718750›Full record

ArticleAnalytical chemistry2013

Spatially-directed protein identification from tissue sections by top-down LC-MS/MS with electron transfer dissociation.

Kevin L Schey, David M Anderson, Kristie L Rose

Abstract read
In one paragraph

Article in Analytical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Review
  2. Article
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  10. Review
  11. Spatial proteomics revealed a CXMucosal immunology · 2020
    Article
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  13. Article
  14. Article
  15. Review
  16. Article
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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

3 authors.

Kevin L ScheyDepartment of Biochemistry and Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA. kevin.schey@vanderbilt.edu
David M Anderson
Kristie L Rose

Funding

A New Imaging Method for Ocular Lens Protein ModificationsR21EY019728 · NEI · VANDERBILT UNIVERSITY · PI SCHEY, KEVIN L · 2009 to 2010
$424k
NEI NIH HHS EY19728NEI NIH HHS R21 EY019728
6 · The paper itself

Abstract

MALDI imaging mass spectrometry (MALDI-IMS) has become a powerful tool for localizing both small molecules and intact proteins in a wide variety of tissue samples in both normal and diseased states. Identification of imaged signals in MALDI-IMS remains a bottleneck in the analysis and limits the interpretation of underlying biology of tissue specimens. In this work, spatially directed tissue microextraction of intact proteins followed by LC-MS/MS with electron transfer dissociation (ETD) was used to identify proteins from specific locations in three tissue types; ocular lens, brain, and kidney. Detection limits were such that a 1 μL extraction volume was sufficient to deliver proteins to the LC-MS/MS instrumentation with sufficient sensitivity to detect 50-100 proteins in a single experiment. Additionally, multiple modified proteins were identified; including truncated lens proteins that would be difficult to assign to an imaged mass using a bottom-up approach. Protein separation and identification are expected to improve with advances in intact protein fractionation/chromatography and advances in interpretation algorithms leading to increased depth of proteome coverage from distinct tissue locations.

Indexed as

AnimalsCattleChromatography, LiquidElectrochemical TechniquesLiquid Phase MicroextractionMass SpectrometryMiceSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryTissue ExtractsTissue Extracts

Identifiers

PMID23718750
PMCPMC3749783

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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.