Evidence map›Paper›PMID 22188123›Full record

ArticleJournal of proteome research2012

Proteomic identification of immunoproteasome accumulation in formalin-fixed rodent spinal cords with experimental autoimmune encephalomyelitis.

Mohit Raja Jain, Qing Li, Tong Liu, Joseph Rinaggio, Amit Ketkar, Vincent Tournier, Kiran Madura, Stella Elkabes, Hong Li

Abstract read
In one paragraph

Article in Journal of proteome research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  9. MicroRNA-7 protects against 1-methyl-4-phenylpyridinium-induced cell death by targeting RelA.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  10. The potential role of heat shock proteins in acute spinal cord injury.European spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society · 2014
    Article
  11. Review
  12. 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

9 authors at 4 institutions in 1 country.

Mohit Raja JainCenter For Advanced Proteomics Research and Department of Biochemistry and Molecular Biology, UMDNJ-New Jersey Medical School Cancer Center , 205 S. Orange Ave., Newark, New Jersey 07103, United States.
Qing Li
Tong Liu
Joseph Rinaggio
Amit Ketkar
Vincent Tournier
Kiran Madura
Stella Elkabes
Hong Li
Rutgers, The State University of New Jersey · USJohnson University · USNeurological Surgery · USRutgers New Jersey Medical School

Funding

Rutgers Mass Spectrometry Core for Integrative Neuroscience ResearchP30NS046593 · NINDS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI LOBEL, PETER · 2004 to 2018
$9.9M
FUNCTIONAL ANALYSIS OF RAD23 PROTEINR01CA083875 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI MADURA, KIRAN · 2000 to 2016
$4.4M
NCI NIH HHS R01 CA083875NINDS NIH HHS P30 NS046593NINDS NIH HHS P30NS046593
6 · The paper itself

Abstract

Clinically relevant formalin-fixed and paraffin-embedded (FFPE) tissues have not been widely used in neuroproteomic studies because many proteins are presumed to be degraded during tissue preservation. Recent improvements in proteomics technologies, from the 2D gel analysis of intact proteins to the "shotgun" quantification of peptides and the use of isobaric tags for absolute and relative quantification (iTRAQ) method, have made the analysis of FFPE tissues possible. In recent years, iTRAQ has been one of the main methods of choice for high throughput quantitative proteomics analysis, which enables simultaneous comparison of up to eight samples in one experiment. Our objective was to assess the relative merits of iTRAQ analysis of fresh frozen versus FFPE nervous tissues by comparing experimental autoimmune encephalomyelitis (EAE)-induced proteomic changes in FFPE rat spinal cords and frozen tissues. EAE-induced proteomic changes in FFPE tissues were positively correlated with those found in the frozen tissues, albeit with ∼50% less proteome coverage. Subsequent validation of the enrichment of immunoproteasome (IP) activator 1 in EAE spinal cords led us to evaluate other proteasome and IP-specific proteins. We discovered that many IP-specific (as opposed to constitutive) proteasomal proteins were enriched in EAE rat spinal cords, and EAE-induced IP accumulation also occurred in the spinal cords of an independent mouse EAE model in a disability score-dependent manner. Therefore, we conclude that it is feasible to generate useful information from iTRAQ-based neuroproteomics analysis of archived FFPE tissues for studying neurological disease tissues.

Indexed as

AnimalsAntigen PresentationCysteine EndopeptidasesEncephalomyelitis, Autoimmune, ExperimentalFemaleMetabolic Networks and PathwaysMiceMice, Inbred C57BLProteasome Endopeptidase ComplexProteomeProteomicsRatsRats, Inbred LewSpinal CordUp-RegulationCysteine EndopeptidasesProteasome Endopeptidase ComplexProteome

Identifiers

PMID22188123
PMCPMC3312875
OpenAlexW2135772076

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.