Evidence map›Paper›PMID 30795648›Full record

ArticleJournal of proteome research2019

SP2: Rapid and Automatable Contaminant Removal from Peptide Samples for Proteomic Analyses.

Matthew Waas, Michaela Pereckas, Rachel A Jones Lipinski, Christopher Ashwood, Rebekah L Gundry

Abstract read
In one paragraph

Article in Journal of proteome research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Enhanced plant bottom-up histone proteomics.Journal of experimental botany · 2026
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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.

Matthew WaasDepartment of Biochemistry , Medical College of Wisconsin , Milwaukee , Wisconsin 53226 , United States.
Michaela PereckasCenter for Biomedical Mass Spectrometry Research , Medical College of Wisconsin , Milwaukee , Wisconsin 53226 , United States.
Rachel A Jones LipinskiDepartment of Biochemistry , Medical College of Wisconsin , Milwaukee , Wisconsin 53226 , United States.
Christopher AshwoodDepartment of Biochemistry , Medical College of Wisconsin , Milwaukee , Wisconsin 53226 , United States.
Rebekah L GundryDepartment of Biochemistry , Medical College of Wisconsin , Milwaukee , Wisconsin 53226 , United States.ORCID 0000-0002-9263-833X

Funding

Cell Surface Phenotyping Human Primary CellsR01HL134010 · NHLBI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI GUNDRY, REBEKAH L. · 2016 to 2020
$1.9M
Cell Surface Proteins in Human CardiomyocytesR01HL126785 · NHLBI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI GUNDRY, REBEKAH L. · 2016 to 2019
$1.5M
Investigating the Utility and Function of a Novel Cardiomyocyte Cell Surface ProteinF31HL140914 · NHLBI · MEDICAL COLLEGE OF WISCONSIN · PI WAAS, MATTHEW R. · 2018 to 2019
$70k
NHLBI NIH HHS F31 HL140914NHLBI NIH HHS R01 HL126785NHLBI NIH HHS R01 HL134010
6 · The paper itself

Abstract

Peptide cleanup is essential for the removal of contaminating substances that may be introduced during sample preparation steps in bottom-up proteomic workflows. Recent studies have described benefits of carboxylate-modified paramagnetic particles over traditional reversed-phase methods for detergent and polymer removal, but challenges with reproducibility have limited the widespread implementation of this approach among laboratories. To overcome these challenges, the current study systematically evaluated key experimental parameters regarding the use of carboxylate-modified paramagnetic particles and determined those that are critical for maximum performance and peptide recovery and those for which the protocol is tolerant to deviation. These results supported the development of a detailed, easy-to-use standard operating protocol, termed SP2, which can be applied to remove detergents and polymers from peptide samples while concentrating the sample in solvent that is directly compatible with typical LC-MS workflows. We demonstrate that SP2 can be applied to phosphopeptides and glycopeptides and that the approach is compatible with robotic liquid handling for automated sample processing. Altogether, the results of this study and accompanying detailed operating protocols for both manual and automated processing are expected to facilitate reproducible implementation of SP2 for various proteomics applications and will especially benefit core or shared resource facilities where unknown or unexpected contaminants may be particularly problematic.

Indexed as

PeptidesChromatography, LiquidDetergentsHEK293 CellsHumansPolymersProteomeProteomicsTandem Mass SpectrometryDetergentsPeptidesPolymersProteomebottom-up proteomicscontaminant removalglycopeptidesLC−MS/MSpeptide cleanupphosphopeptidesTMT

Identifiers

PMID30795648
PMCPMC6571012

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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.