Evidence map›Paper›PMID 26126808›Full record

ArticleScientific reports2015

Low-bias phosphopeptide enrichment from scarce samples using plastic antibodies.

Jing Chen, Sudhirkumar Shinde, Markus-Hermann Koch, Martin Eisenacher, Sara Galozzi, Thilo Lerari, Katalin Barkovits, Prabal Subedi, Rejko Krüger, Katja Kuhlmann and 3 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

18 citing papers in PubMed, 63 citations in OpenAlex.

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  10. Synthesis and Evaluation of Non-Hydrolyzable Phospho-Lysine Peptide Mimics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021
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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

13 authors at 3 institutions in 2 countries.

Jing ChenMedizinisches Proteom-Center, Ruhr-University Bochum, Universitätsstr. 150, 44801 Bochum, Germany.
Sudhirkumar ShindeDepartment of Biomedical Sciences, Faculty of Health and Society, Malmö University, SE 205 06 Malmö, Sweden.
Markus-Hermann KochMedizinisches Proteom-Center, Ruhr-University Bochum, Universitätsstr. 150, 44801 Bochum, Germany.
Martin EisenacherMedizinisches Proteom-Center, Ruhr-University Bochum, Universitätsstr. 150, 44801 Bochum, Germany.
Sara GalozziMedizinisches Proteom-Center, Ruhr-University Bochum, Universitätsstr. 150, 44801 Bochum, Germany.
Thilo LerariMedizinisches Proteom-Center, Ruhr-University Bochum, Universitätsstr. 150, 44801 Bochum, Germany.
Katalin BarkovitsMedizinisches Proteom-Center, Ruhr-University Bochum, Universitätsstr. 150, 44801 Bochum, Germany.
Prabal SubediMedizinisches Proteom-Center, Ruhr-University Bochum, Universitätsstr. 150, 44801 Bochum, Germany.
Rejko KrügerFunctional Neurogenomics Laboratory, Hertie-Institute for Clinical Brain Research, Eberhard Karls Universität Tuebingen and DZNE Tuebingen, Hoppe-Seyler-Str.3, 72076 Tuebingen, Germany.
Katja KuhlmannMedizinisches Proteom-Center, Ruhr-University Bochum, Universitätsstr. 150, 44801 Bochum, Germany.
Börje SellergrenDepartment of Biomedical Sciences, Faculty of Health and Society, Malmö University, SE 205 06 Malmö, Sweden.
Stefan HellingMedizinisches Proteom-Center, Ruhr-University Bochum, Universitätsstr. 150, 44801 Bochum, Germany.
Katrin MarcusMedizinisches Proteom-Center, Ruhr-University Bochum, Universitätsstr. 150, 44801 Bochum, Germany.
Ruhr University Bochum · DEMalmö University · SEHertie Institute for Clinical Brain Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphospecific enrichment techniques and mass spectrometry (MS) are essential tools for comprehending the cellular phosphoproteome. Here, we report a fast and simple approach for low sequence-bias phosphoserine (pS) peptide capture and enrichment that is compatible with low biological or clinical sample input. The approach exploits molecularly imprinted polymers (MIPs, "plastic antibodies") featuring tight neutral binding sites for pS or pY that are capable of cross-reacting with phosphopeptides of protein proteolytic digests. The versatility of the resulting method was demonstrated with small samples of whole-cell lysate from human embryonic kidney (HEK) 293T cells, human neuroblastoma SH-SY5Y cells, mouse brain or human cerebrospinal fluid (CSF). Following pre-fractionation of trypsinized proteins by strong cation exchange (SCX) chromatography, pS-MIP enrichment led to the identification of 924 phosphopeptides in the HEK 293T whole-cell lysate, exceeding the number identified by TiO2-based enrichment (230). Moreover, the phosphopeptides were extracted with low sequence bias and showed no evidence for the characteristic preference of TiO2 for acidic amino acids (aspartic and glutamic acid). Applying the method to human CSF led to the discovery of 47 phosphopeptides belonging to 24 proteins and revealed three previously unknown phosphorylation sites.

Indexed as

Amino Acid SequenceAnimalsAntibodiesCerebrospinal FluidChromatography, Ion ExchangeChromatography, LiquidHEK293 CellsHumansMiceMolecular ImprintingMolecular Sequence DataPhosphopeptidesPhosphorylationPhosphoserinePlasticsProteomicsAntibodiesPhosphopeptidesPhosphoserinePlastics

Identifiers

PMID26126808
PMCPMC4486973
OpenAlexW795592238

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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.