Evidence map›Paper›PMID 24495006›Full record

ArticleJournal of proteome research2014

Deep proteome mapping of mouse kidney based on OFFGel prefractionation reveals remarkable protein post- translational modifications.

Sameh Magdeldin, Keiko Yamamoto, Yutaka Yoshida, Bo Xu, Ying Zhang, Hidehiko Fujinaka, Eishin Yaoita, John R Yates, Tadashi Yamamoto

Abstract read
In one paragraph

Article in Journal of proteome research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Proteoform-Specific Insights into Cellular Proteome Regulation.Molecular & cellular proteomics : MCP · 2016
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
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.

Sameh MagdeldinDepartment of Structural Pathology, Institute of Nephrology, Graduate School of Medical and Dental Sciences, Niigata University , Niigata, Japan.
Keiko Yamamoto
Yutaka Yoshida
Bo Xu
Ying Zhang
Hidehiko Fujinaka
Eishin Yaoita
John R Yates
Tadashi Yamamoto

Funding

Quantitative Biology CoreU19AI063603 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI KWOK, PUI-YAN · 2004 to 2015
$26.4M
TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
Quantitative Proteome Analysis of Brain DevelopmentR01MH067880 · NIMH · SCRIPPS RESEARCH INSTITUTE, THE · PI YATES III, JOHN R · 2003 to 2017
$7.1M
NIAID NIH HHS U19 AI063603NIAID NIH HHS V19 AI063603NIGMS NIH HHS P41 GM103533NIMH NIH HHS R01 MH067880
6 · The paper itself

Abstract

Performing a comprehensive nonbiased proteome analysis is an extraordinary challenge due to sample complexity and wide dynamic range, especially in eukaryotic tissues. Thus, prefractionation steps conducted prior to mass spectrometric analysis are critically important to reduce complex biological matrices and allow in-depth analysis. Here we demonstrated the use of OFFGel prefractionation to identify more low abundant and hydrophobic proteins than in a nonfractionated sample. Moreover, OFFGel prefractionation of a kidney protein sample was able to unveil protein functional relevance by detecting PTMs, especially when prefractionation was augmented with a targeted enrichment strategy such as TiO₂ phospho-enrichment. The OFFGel-TiO₂ combination used in this study was comparable to other global phosphoproteomics approaches (SCX-TiO₂, ERLIC-TiO₂, or HILIC-TiO₂). The detailed mouse kidney proteome with the phosphopeptide enrichment presented here serves as a useful platform for a better understanding of how the renal protein modification machinery works and, ultimately, will contribute to our understanding of pathological processes as well as normal physiological renal functions.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsChemical FractionationElectrophoresis, Gel, Two-DimensionalHydrophobic and Hydrophilic InteractionsIsoelectric FocusingKidneyMaleMiceMice, Inbred C57BLMolecular Sequence DataPhosphopeptidesPhosphorylationProteomeTandem Mass SpectrometryPhosphopeptidesProteomeTitaniumtitanium dioxide

Identifiers

PMID24495006
PMCPMC3993965

What OpenQuestion holds

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Registered trials

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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.