Evidence map›Paper›PMID 19344176›Full record

ArticleJournal of proteome research2009

FLEXIQuant: a novel tool for the absolute quantification of proteins, and the simultaneous identification and quantification of potentially modified peptides.

Sasha Singh, Michael Springer, Judith Steen, Marc W Kirschner, Hanno Steen

Abstract read
In one paragraph

Article in Journal of proteome research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. Article
  3. Proteomic/transcriptomic analysis of erythropoiesis.Current opinion in hematology · 2021
    Review
  4. Review
  5. Quantitative Mass Spectrometry-Based Proteomics: An Overview.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
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  8. Review
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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

5 authors.

Sasha SinghDepartment of Pathology, Harvard Medical School and Children's Hospital Boston, Boston, Massachusetts 02115, USA.
Michael Springer
Judith Steen
Marc W Kirschner
Hanno Steen

Funding

CELL CYCLE REGULATIONR01GM039023 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KIRSCHNER, MARC WALLACE · 1988 to 2017
$10.2M
NIGMS NIH HHS 2 R01 GM039023NIGMS NIH HHS R01 GM039023
6 · The paper itself

Abstract

Measurements of protein abundance and quantitative assessment of multiple post-translational modifications (PTMs) within a single protein are increasingly used to understand the control of protein activity, particularly in metazoan cells. General methods of wide applicability and precision/accuracy for quantitative estimation of protein post-translational regulation are lacking. Protein mass spectrometry has evolved from a high-throughput qualitative technique to a potentially general quantitative tool, but there are still serious limitations in dynamic range and coverage. To address some of these limitations, we introduce a novel MS-based quantitative strategy, FLEXIQuant, (Full-Length Expressed Stable Isotope-labeled Proteins for Quantification), which can track changes in relative peptide abundances as a function of PTM, and determine absolute quantity of a protein from its lysate. We examined two subunits of the anaphase-promoting complex, CDC27 and APC5, as a test of our ability to monitor quantitatively, the PTM status of several peptides over time. We find evidence of differential regulation at different sites, a phenomenon we believe will be very widespread. FLEXIQuant proved itself to be capable of serving as a general quantitative tool.

Indexed as

Amino Acid SequenceAnaphase-Promoting Complex-CyclosomeApc3 Subunit, Anaphase-Promoting Complex-CyclosomeApc5 Subunit, Anaphase-Promoting Complex-CyclosomeCell Cycle ProteinsCloning, MolecularGene ExpressionHeLa CellsHumansIsotope LabelingMass SpectrometryMolecular Sequence DataOligopeptidesProteinsProteomicsReproducibility of ResultsANAPC5 protein, humanAnaphase-Promoting Complex-CyclosomeApc3 Subunit, Anaphase-Promoting Complex-CyclosomeApc5 Subunit, Anaphase-Promoting Complex-CyclosomeCDC27 protein, humanCell Cycle ProteinsOligopeptidesProteinsUbiquitin-Protein Ligase Complexes

Identifiers

PMID19344176
PMCPMC2868505

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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.