Evidence map›Paper›PMID 26133526›Full record

ArticleJournal of the American Society for Mass Spectrometry2015

Visualization and dissemination of multidimensional proteomics data comparing protein abundance during Caenorhabditis elegans development.

Michael Riffle, Gennifer E Merrihew, Daniel Jaschob, Vagisha Sharma, Trisha N Davis, William S Noble, Michael J MacCoss

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Proteoform-Specific Insights into Cellular Proteome Regulation.Molecular & cellular proteomics : MCP · 2016
    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

7 authors.

Michael RiffleDepartment of Biochemistry, University of Washington, Seattle, WA, 98195, USA.
Gennifer E MerrihewDepartment of Genome Sciences, University of Washington, Seattle, WA, 98195, USA.
Daniel JaschobDepartment of Biochemistry, University of Washington, Seattle, WA, 98195, USA.
Vagisha SharmaDepartment of Genome Sciences, University of Washington, Seattle, WA, 98195, USA.
Trisha N DavisDepartment of Biochemistry, University of Washington, Seattle, WA, 98195, USA.
William S NobleDepartment of Genome Sciences, University of Washington, Seattle, WA, 98195, USA.
Michael J MacCossDepartment of Genome Sciences, University of Washington, Seattle, WA, 98195, USA. maccoss@uw.edu.

Funding

TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
Global Identification of transcribed elements in the C. elegans genomeU01HG004263 · NHGRI · UNIVERSITY OF WASHINGTON · PI WATERSTON, ROBERT H · 2007 to 2011
$7.3M
Analysis of Protein Dynamics in C. elegans by mLC/MS/MSR01DK069386 · NIDDK · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2006 to 2013
$2.3M
NHGRI NIH HHS U01 HG004263NIDDK NIH HHS R01 DK069386NIGMS NIH HHS P41 GM103533
6 · The paper itself

Abstract

Regulation of protein abundance is a critical aspect of cellular function, organism development, and aging. Alternative splicing may give rise to multiple possible proteoforms of gene products where the abundance of each proteoform is independently regulated. Understanding how the abundances of these distinct gene products change is essential to understanding the underlying mechanisms of many biological processes. Bottom-up proteomics mass spectrometry techniques may be used to estimate protein abundance indirectly by sequencing and quantifying peptides that are later mapped to proteins based on sequence. However, quantifying the abundance of distinct gene products is routinely confounded by peptides that map to multiple possible proteoforms. In this work, we describe a technique that may be used to help mitigate the effects of confounding ambiguous peptides and multiple proteoforms when quantifying proteins. We have applied this technique to visualize the distribution of distinct gene products for the whole proteome across 11 developmental stages of the model organism Caenorhabditis elegans. The result is a large multidimensional dataset for which web-based tools were developed for visualizing how translated gene products change during development and identifying possible proteoforms. The underlying instrument raw files and tandem mass spectra may also be downloaded. The data resource is freely available on the web at http://www.yeastrc.org/wormpes/ . Graphical Abstract ᅟ.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsElectrophoresis, Polyacrylamide GelPeptide FragmentsProteomeProteomicsTandem Mass SpectrometryUser-Computer InterfaceCaenorhabditis elegans ProteinsPeptide FragmentsProteomeCaenorhabditis elegansDatabaseDevelopmentProtein separationProteoformProteomicsSDS-PAGEVisualization

Identifiers

PMID26133526
PMCPMC4607629

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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.