Evidence map›Paper›PMID 37155737›Full record

ArticleJournal of the American Society for Mass Spectrometry2023

The Edge Effect in High-Throughput Proteomics: A Cautionary Tale.

Colleen B Maxwell, Jatinderpal K Sandhu, Thong H Cao, Gerry P McCann, Leong L Ng, Donald J L Jones

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. MR-SPJournal of proteome research · 2026
    Article
  5. Article
  6. Article
  7. Proteomic Analysis of COVID-19 Infection.Advances in experimental medicine and biology · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
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

6 authors.

Colleen B MaxwellThe Leicester van Geest MultiOmics Facility, Hodgkin Building, University of Leicester, Leicester LE1 9HN, United Kingdom.ORCID 0000-0003-4463-3566
Jatinderpal K SandhuThe Leicester van Geest MultiOmics Facility, Hodgkin Building, University of Leicester, Leicester LE1 9HN, United Kingdom.
Thong H CaoThe Leicester van Geest MultiOmics Facility, Hodgkin Building, University of Leicester, Leicester LE1 9HN, United Kingdom.
Gerry P McCannDepartment of Cardiovascular Sciences and NIHR Leicester Biomedical Research Centre, Glenfield Hospital, Leicester LE3 9QP, United Kingdom.
Leong L NgThe Leicester van Geest MultiOmics Facility, Hodgkin Building, University of Leicester, Leicester LE1 9HN, United Kingdom.
Donald J L JonesThe Leicester van Geest MultiOmics Facility, Hodgkin Building, University of Leicester, Leicester LE1 9HN, United Kingdom.ORCID 0000-0001-6583-870X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In order for mass spectrometry to continue to grow as a platform for high-throughput clinical and translational research, careful consideration must be given to quality control by ensuring that the assay performs reproducibly and accurately and precisely. In particular, the throughput required for large cohort clinical validation in biomarker discovery and diagnostic screening has driven the growth of multiplexed targeted liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) assays paired with sample preparation and analysis in multiwell plates. However, large scale MS-based proteomics studies are often plagued by batch effects: sources of technical variation in the data, which can arise from a diverse array of sources such as sample preparation batches, different reagent lots, or indeed MS signal drift. These batch effects can confound the detection of true signal differences, resulting in incorrect conclusions being drawn about significant biological effects or lack thereof. Here, we present an intraplate batch effect termed the edge effect arising from temperature gradients in multiwell plates, commonly reported in preclinical cell culture studies but not yet reported in a clinical proteomics setting. We present methods herein to ameliorate the phenomenon including proper assessment of heating techniques for multiwell plates and incorporation of surrogate standards, which can normalize for intraplate variation.

Indexed as

ProteomicsTandem Mass SpectrometryChromatography, LiquidHumansQuality ControlReference Standards

Identifiers

PMID37155737
PMCPMC10251511

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.