Evidence map›Paper›PMID 25665708›Full record

ArticleAnalytical and bioanalytical chemistry2015

A method to prevent protein delocalization in imaging mass spectrometry of non-adherent tissues: application to small vertebrate lens imaging.

David M G Anderson, Kyle A Floyd, Stephen Barnes, Judy M Clark, John I Clark, Hassane Mchaourab, Kevin L Schey

Open access · greenAbstract readEvaluation Study
In one paragraph

Article in Analytical and bioanalytical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Quantitative mass spectrometry imaging: therapeutics & biomolecules.Chemical communications (Cambridge, England) · 2024
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Bringing SEM and MSI Closer Than Ever Before: VisualizingJournal of fungi (Basel, Switzerland) · 2020
    Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Functional sequences in human alphaB crystallin.Biochimica et biophysica acta · 2016
    Review
  17. Mass spectrometry imaging for plant biology: a review.Phytochemistry reviews : proceedings of the Phytochemical Society of Europe
    Review
  18. 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

7 authors at 3 institutions in 1 country.

David M G AndersonDepartment of Biochemistry, Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN, 37205-0146, USA.
Kyle A Floyd
Stephen Barnes
Judy M Clark
John I Clark
Hassane Mchaourab
Kevin L Schey
Vanderbilt University · USUniversity of Alabama at Birmingham · USUniversity of Washington · US

Funding

Vision Research CoreP30EY001730 · NEI · UNIVERSITY OF WASHINGTON · PI MAUREEN E NEITZ · 1985 to 2026
$23.5M
Training (pp 214-245)P41GM103391 · NIGMS · VANDERBILT UNIVERSITY · PI REYZER, MICHELLE L · 2012 to 2020
$17.7M
MOLECULAR BASIS OF LENS TRANSPARENCYR01EY012018 · NEI · VANDERBILT UNIVERSITY · PI MCHAOURAB, HASSANE S · 2003 to 2023
$10.4M
DEVELOPMENT AND MAINTENANCE OF TRANSPARENCY IN LENSESR01EY004542 · NEI · UNIVERSITY OF WASHINGTON · PI CLARK, JOHN IRWIN · 1985 to 2013
$7.1M
A New Imaging Method for Ocular Lens Protein ModificationsR21EY019728 · NEI · VANDERBILT UNIVERSITY · PI SCHEY, KEVIN L · 2009 to 2010
$424k
Lens crystallins: spatial location and properties in the ICR/f rat cataract modelR21EY020963 · NEI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BARNES, STEPHEN · 2010 to 2011
$417k
MOLECULAR BASIS OF LENS TRANSPARENCYR29EY012018 · NEI · VANDERBILT UNIVERSITY · PI MCHAOURAB, HASSANE S · 1998 to 2002
$291k
NEI NIH HHS EY019728NEI NIH HHS EY020963NEI NIH HHS EY04542NEI NIH HHS EY12018NEI NIH HHS P30 EY001730NEI NIH HHS R01 EY004542NEI NIH HHS R01 EY012018NEI NIH HHS R21 EY019728NEI NIH HHS R21 EY020963NEI NIH HHS R29 EY012018NIGMS NIH HHS GM103391NIGMS NIH HHS P41 GM103391
6 · The paper itself

Abstract

MALDI imaging requires careful sample preparation to obtain reliable, high-quality images of small molecules, peptides, lipids, and proteins across tissue sections. Poor crystal formation, delocalization of analytes, and inadequate tissue adherence can affect the quality, reliability, and spatial resolution of MALDI images. We report a comparison of tissue mounting and washing methods that resulted in an optimized method using conductive carbon substrates that avoids thaw mounting or washing steps, minimizes protein delocalization, and prevents tissue detachment from the target surface. Application of this method to image ocular lens proteins of small vertebrate eyes demonstrates the improved methodology for imaging abundant crystallin protein products. This method was demonstrated for tissue sections from rat, mouse, and zebrafish lenses resulting in good-quality MALDI images with little to no delocalization. The images indicate, for the first time in mouse and zebrafish, discrete localization of crystallin protein degradation products resulting in concentric rings of distinct protein contents that may be responsible for the refractive index gradient of vertebrate lenses.

Indexed as

Analytic Sample Preparation MethodsAnimalsCrystallinsFemaleLens, CrystallineMaleMiceMice, Inbred C57BLMice, Inbred ICRMolecular ImagingProtein TransportRatsRats, WistarSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationZebrafishCrystallins

Identifiers

PMID25665708
PMCPMC4379205
OpenAlexW1964435465

What OpenQuestion holds

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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.