Evidence map›Paper›PMID 27121989›Full record

ArticleScientific reports2016

Consequences of point mutations in melanoma-associated antigen 4 (MAGE-A4) protein: Insights from structural and biophysical studies.

Yoshio Hagiwara, Lina Sieverling, Farina Hanif, Jensy Anton, Eleanor R Dickinson, Tam T T Bui, Antonina Andreeva, Perdita E Barran, Ernesto Cota, Penka V Nikolova

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

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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

10 authors.

Yoshio HagiwaraKing's College London, Faculty of Life Sciences &Medicine, Institute of Pharmaceutical Science, Franklin-Wilkins Building, 150 Stamford St, London, SE1 9NH, UK.
Lina SieverlingKing's College London, Faculty of Life Sciences &Medicine, Institute of Pharmaceutical Science, Franklin-Wilkins Building, 150 Stamford St, London, SE1 9NH, UK.
Farina HanifKing's College London, Faculty of Life Sciences &Medicine, Institute of Pharmaceutical Science, Franklin-Wilkins Building, 150 Stamford St, London, SE1 9NH, UK.
Jensy AntonKing's College London, Faculty of Life Sciences &Medicine, Institute of Pharmaceutical Science, Franklin-Wilkins Building, 150 Stamford St, London, SE1 9NH, UK.
Eleanor R DickinsonMichael Barber Centre for Collaborative Mass Spectrometry, Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Tam T T BuiBiomolecular Spectroscopy Centre, King's College London, The Wolfson Wing, Hodgkin Building, London SE1 1UL.
Antonina AndreevaMRC-LMB, Francis Crick Avenue, Cambridge, CB2 0QH.
Perdita E BarranMichael Barber Centre for Collaborative Mass Spectrometry, Manchester Institute of Biotechnology, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
Ernesto CotaImperial College London, Faculty of Natural Sciences, London, SW7 2AZ.
Penka V NikolovaKing's College London, Faculty of Life Sciences &Medicine, Institute of Pharmaceutical Science, Franklin-Wilkins Building, 150 Stamford St, London, SE1 9NH, UK.

Funding

Medical Research Council G0100305Medical Research Council MC_U105192716
6 · The paper itself

Abstract

The Melanoma-Associated Antigen A4 (MAGE-A4) protein is a target for cancer therapy. The function of this protein is not well understood. We report the first comprehensive study on key cancer-associated MAGE-A4 mutations and provide analysis on the consequences of these mutations on the structure, folding and stability of the protein. Based on Nuclear Magnetic Resonance and Circular Dichroism, these mutations had no significant effects on the structure and the folding of the protein. Some mutations affected the thermal stability of the protein remarkably. Native mass spectrometry of wild-type MAGE-A4 showed a broad charge state distribution suggestive of a structurally dynamic protein. Significant intensity was found in relatively low charge states, indicative of a predominantly globular form and some population in more extended states. The latter is supported by Ion Mobility measurements. The MAGE-A4 mutants exhibited similar features. These novel molecular insights shed further light on better understanding of these proteins, which are implicated in a wide range of human cancers.

Indexed as

Point MutationAntigens, NeoplasmCircular DichroismHumansMagnetic Resonance SpectroscopyMass SpectrometryNeoplasm ProteinsNeoplasmsProtein ConformationProtein FoldingProtein StabilityAntigens, NeoplasmMAGEA4 protein, humanNeoplasm Proteins

Identifiers

PMID27121989
PMCPMC4848555

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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.