Evidence map›Paper›PMID 28448532›Full record

ArticlePloS one2017

A selected reaction monitoring mass spectrometric assessment of biomarker candidates diagnosing large-cell neuroendocrine lung carcinoma by the scaling method using endogenous references.

Tetsuya Fukuda, Masaharu Nomura, Yasufumi Kato, Hiromasa Tojo, Kiyonaga Fujii, Toshitaka Nagao, Yasuhiko Bando, Thomas E Fehniger, György Marko-Varga, Haruhiko Nakamura and 2 more

Abstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

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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

7 citing papers in PubMed.

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4 · The record

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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.

Tetsuya FukudaBiosys Technologies, Inc., Tokyo, Japan.
Masaharu NomuraDepartment of Thoracic and Thyroid Surgery, Tokyo Medical University, Tokyo, Japan.
Yasufumi KatoDepartment of Thoracic Surgery, Tokyo Medical University Ibaraki Medical Center, Ibaraki, Japan.
Hiromasa TojoDepartment of Biophysics and Biochemistry, Osaka University Graduate School of Medicine, Osaka, Japan.
Kiyonaga FujiiDepartment of Translational Medicine Informatics, St. Mariana University School of Medicine, Kawasaki, Japan.
Toshitaka NagaoDepartment of Clinical Pathology, Tokyo Medical University, Tokyo, Japan.
Yasuhiko BandoBiosys Technologies, Inc., Tokyo, Japan.
Thomas E FehnigerCenter of Excellence in Biological and Medical Mass Spectrometry, Lund University, Lund, Sweden.
György Marko-VargaCenter of Excellence in Biological and Medical Mass Spectrometry, Lund University, Lund, Sweden.
Haruhiko NakamuraDepartment of Translational Medicine Informatics, St. Mariana University School of Medicine, Kawasaki, Japan.
Harubumi KatoDepartment of Thoracic and Thyroid Surgery, Tokyo Medical University, Tokyo, Japan.
Toshihide NishimuraDepartment of Translational Medicine Informatics, St. Mariana University School of Medicine, Kawasaki, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Selected reaction monitoring mass spectrometry (SRM-MS) -based semi-quantitation was performed to assess the validity of 46 selected candidate proteins for specifically diagnosing large-cell neuroendocrine lung carcinoma (LCNEC) and differentiating it from other lung cancer subtypes. The scaling method was applied in this study using specific SRM peak areas (AUCs) derived from the endogenous reference protein that normalizes all SRM AUCs obtained for the candidate proteins. In a screening verification study, we found that seven out of the 46 candidate proteins were statistically significant for the LCNEC phenotype, including 4F2hc cell surface antigen heavy chain (4F2hc/CD98) (p-ANOVA ≤ 0.0012), retinal dehydrogenase 1 (p-ANOVA ≤ 0.0029), apolipoprotein A-I (p-ANOVA ≤ 0.0004), β-enolase (p-ANOVA ≤ 0.0043), creatine kinase B-type (p-ANOVA ≤ 0.0070), and galectin-3-binding protein (p-ANOVA = 0.0080), and phosphatidylethanolamine-binding protein 1 (p-ANOVA ≤ 0.0012). In addition, we also identified candidate proteins specific to the small-cell lung carcinoma (SCLC) subtype. These candidates include brain acid soluble protein 1 (p-ANOVA < 0.0001) and γ-enolase (p-ANOVA ≤ 0.0013). This new relative quantitation-based approach utilizing the scaling method can be applied to assess hundreds of protein candidates obtained from discovery proteomic studies as a first step of the verification phase in biomarker development processes.

Indexed as

Biomarkers, TumorCarcinoma, Large CellCarcinoma, NeuroendocrineHumansLung NeoplasmsMass SpectrometryProteomicsReference StandardsBiomarkers, Tumor

Identifiers

PMID28448532
PMCPMC5407814

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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.