Evidence map›Paper›PMID 37047281›Full record

ArticleInternational journal of molecular sciences2023

Comparison of SPEED, S-Trap, and In-Solution-Based Sample Preparation Methods for Mass Spectrometry in Kidney Tissue and Plasma.

Evelyn M Templeton, Anna P Pilbrow, Torsten Kleffmann, John W Pickering, Miriam T Rademaker, Nicola J A Scott, Leigh J Ellmers, Christopher J Charles, Zoltan H Endre, A Mark Richards and 2 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

5 citing papers in PubMed, 13 citations in OpenAlex.

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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

12 authors at 3 institutions in 3 countries.

Evelyn M TempletonChristchurch Heart Institute, Department of Medicine, University of Otago, Christchurch 8014, New Zealand.ORCID 0000-0002-5767-794X
Anna P PilbrowChristchurch Heart Institute, Department of Medicine, University of Otago, Christchurch 8014, New Zealand.ORCID 0000-0003-1949-9449
Torsten KleffmannResearch Infrastructure Centre, Division of Health Sciences, University of Otago, Dunedin 9016, New Zealand.
John W PickeringChristchurch Heart Institute, Department of Medicine, University of Otago, Christchurch 8014, New Zealand.
Miriam T RademakerChristchurch Heart Institute, Department of Medicine, University of Otago, Christchurch 8014, New Zealand.
Nicola J A ScottChristchurch Heart Institute, Department of Medicine, University of Otago, Christchurch 8014, New Zealand.ORCID 0000-0002-5685-9151
Leigh J EllmersChristchurch Heart Institute, Department of Medicine, University of Otago, Christchurch 8014, New Zealand.
Christopher J CharlesChristchurch Heart Institute, Department of Medicine, University of Otago, Christchurch 8014, New Zealand.ORCID 0000-0001-9807-8022
Zoltan H EndreDepartment of Nephrology, Prince of Wales Hospital, Sydney, NSW 2031, Australia.ORCID 0000-0002-4782-8695
A Mark RichardsChristchurch Heart Institute, Department of Medicine, University of Otago, Christchurch 8014, New Zealand.
Vicky A CameronChristchurch Heart Institute, Department of Medicine, University of Otago, Christchurch 8014, New Zealand.ORCID 0000-0003-3147-683X
Moritz LasséChristchurch Heart Institute, Department of Medicine, University of Otago, Christchurch 8014, New Zealand.
University of Otago · NZNational University of Singapore · SGPrince of Wales Hospital · AU

Funding

Canterbury Medical Research Foundation #2017PRONicola ScottHealth Research Council of New Zealand #14/521, #11/170, #17/562Lotteries Health Research #R-LHR-2017-49246National Heart Foundation of New Zealand #1562, #1879National Heart Foundation of New Zealand #1693, #1736
6 · The paper itself

Abstract

Mass spectrometry is a powerful technique for investigating renal pathologies and identifying biomarkers, and efficient protein extraction from kidney tissue is essential for bottom-up proteomic analyses. Detergent-based strategies aid cell lysis and protein solubilization but are poorly compatible with downstream protein digestion and liquid chromatography-coupled mass spectrometry, requiring additional purification and buffer-exchange steps. This study compares two well-established detergent-based methods for protein extraction (in-solution sodium deoxycholate (SDC); suspension trapping (S-Trap)) with the recently developed sample preparation by easy extraction and digestion (SPEED) method, which uses strong acid for denaturation. We compared the quantitative performance of each method using label-free mass spectrometry in both sheep kidney cortical tissue and plasma. In kidney tissue, SPEED quantified the most unique proteins (SPEED 1250; S-Trap 1202; SDC 1197). In plasma, S-Trap produced the most unique protein quantifications (S-Trap 150; SDC 148; SPEED 137). Protein quantifications were reproducible across biological replicates in both tissue (R

Indexed as

DetergentsTandem Mass SpectrometryAnimalsProteinsProteomicsReproducibility of ResultsSheepDetergentsProteinskidneymass spectrometryplasmaproteomicsquantitative proteomicsrenalsample preparation techniquesSPEEDsuspension trapSWATH-MS

Identifiers

PMID37047281
PMCPMC10094439
OpenAlexW4361224551

What OpenQuestion holds

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LicenceCC BY
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.