Evidence map›Paper›PMID 24870543›Full record

ArticleNature2014

Mass-spectrometry-based draft of the human proteome.

Mathias Wilhelm, Judith Schlegl, Hannes Hahne, Amin Moghaddas Gholami, Marcus Lieberenz, Mikhail M Savitski, Emanuel Ziegler, Lars Butzmann, Siegfried Gessulat, Harald Marx and 12 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 912 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
912citing papers in PubMed, 1 pooled it
–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

912 citing papers in PubMed, 1 synthesis or guideline pooled it.

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852 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

22 authors.

Mathias Wilhelm1] Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany [2] SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany [3].
Judith Schlegl1] SAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany [2].
Hannes Hahne1] Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany [2].
Amin Moghaddas Gholami1] Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany [2].
Marcus LieberenzSAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany.
Mikhail M SavitskiCellzome GmbH, Meyerhofstraße 1, 69117 Heidelberg, Germany.
Emanuel ZieglerSAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany.
Lars ButzmannSAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany.
Siegfried GessulatSAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany.
Harald MarxChair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany.
Toby MathiesonCellzome GmbH, Meyerhofstraße 1, 69117 Heidelberg, Germany.
Simone LemeerChair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany.
Karsten SchnatbaumJPT Peptide Technologies GmbH, Volmerstraße 5, 12489 Berlin, Germany.
Ulf ReimerJPT Peptide Technologies GmbH, Volmerstraße 5, 12489 Berlin, Germany.
Holger WenschuhJPT Peptide Technologies GmbH, Volmerstraße 5, 12489 Berlin, Germany.
Martin MollenhauerInstitute of Pathology, Technische Universität München, Trogerstraße 18, 81675 München, Germany.
Julia Slotta-HuspeninaInstitute of Pathology, Technische Universität München, Trogerstraße 18, 81675 München, Germany.
Joos-Hendrik BoeseSAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany.
Marcus BantscheffCellzome GmbH, Meyerhofstraße 1, 69117 Heidelberg, Germany.
Anja GerstmairSAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany.
Franz FaerberSAP AG, Dietmar-Hopp-Allee 16, 69190 Walldorf, Germany.
Bernhard Kuster1] Chair of Proteomics and Bioanalytics, Technische Universität München, Emil-Erlenmeyer Forum 5, 85354 Freising, Germany [2] Center for Integrated Protein Science Munich, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteomes are characterized by large protein-abundance differences, cell-type- and time-dependent expression patterns and post-translational modifications, all of which carry biological information that is not accessible by genomics or transcriptomics. Here we present a mass-spectrometry-based draft of the human proteome and a public, high-performance, in-memory database for real-time analysis of terabytes of big data, called ProteomicsDB. The information assembled from human tissues, cell lines and body fluids enabled estimation of the size of the protein-coding genome, and identified organ-specific proteins and a large number of translated lincRNAs (long intergenic non-coding RNAs). Analysis of messenger RNA and protein-expression profiles of human tissues revealed conserved control of protein abundance, and integration of drug-sensitivity data enabled the identification of proteins predicting resistance or sensitivity. The proteome profiles also hold considerable promise for analysing the composition and stoichiometry of protein complexes. ProteomicsDB thus enables navigation of proteomes, provides biological insight and fosters the development of proteomic technology.

Indexed as

Databases, ProteinMass SpectrometryProteomicsBody FluidsCell LineGene Expression ProfilingGenome, HumanHumansMolecular Sequence AnnotationOrgan SpecificityProteomeRNA, MessengerProteomeRNA, Messenger

Identifiers

PMID24870543

What OpenQuestion holds

Textmetadata
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.