ArticlePloS one2016
Structures of Two Melanoma-Associated Antigens Suggest Allosteric Regulation of Effector Binding.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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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.
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Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
- Mechanisms of Polymer-Antigen Binding and Hydrolysis Inhibition: Molecular Dynamics Simulations and Experimental Measurements.Polymers · 2026Article
- Development of Next Generation Cell-Permeable Peptide Inhibitors for the Oncological Target MAGE-A4.Journal of medicinal chemistry · 2025Article
- Identification of new tissue markers for the monitoring and standardization of penile cancer according to the degree of differentiation.Histology and histopathology · 2025Article
- Melanoma-associated antigen A4: A cancer/testis antigen as a target for adoptive T-cell receptor T-cell therapy.Cancer treatment reviews · 2025Review
- Structural basis for RAD18 regulation by MAGEA4 and its implications for RING ubiquitin ligase binding by MAGE family proteins.The EMBO journal · 2024Article
- Melanoma Antigen Family A (MAGE A) as Promising Biomarkers and Therapeutic Targets in Bladder Cancer.Cancers · 2024Review
- Identification of Covalent Cyclic Peptide Inhibitors in mRNA Display.Journal of the American Chemical Society · 2023Article
- Article
- Discovery and Structural Basis of the Selectivity of Potent Cyclic Peptide Inhibitors of MAGE-A4.Journal of medicinal chemistry · 2022Article
- Cancer-Testis Antigens in Triple-Negative Breast Cancer: Role and Potential Utility in Clinical Practice.Cancers · 2021Review
- T-cell receptor-based therapy: an innovative therapeutic approach for solid tumors.Journal of hematology & oncology · 2021Review
- Structure Basis for Shaping the Nse4 Protein by the Nse1 and Nse3 Dimer within the Smc5/6 Complex.Journal of molecular biology · 2021Article
- The Smc5/6 Core Complex Is a Structure-Specific DNA Binding and Compacting Machine.Molecular cell · 2020Article
- Vesicular Stomatitis Virus Encoding a Destabilized Tumor Antigen Improves Activation of Anti-tumor T Cell Responses.Molecular therapy : the journal of the American Society of Gene Therapy · 2020Article
- The necdin interactome: evaluating the effects of amino acid substitutions and cell stress using proximity-dependent biotinylation (BioID) and mass spectrometry.Human genetics · 2020Article
- Emerging roles of the MAGE protein family in stress response pathways.The Journal of biological chemistry · 2020Review
- Structural basis for substrate recognition and chemical inhibition of oncogenic MAGE ubiquitin ligases.Nature communications · 2020Article
- Regulation of MAGE-A3/6 by the CRL4-DCAF12 ubiquitin ligase and nutrient availability.EMBO reports · 2019Article
- Cellular and disease functions of the Prader-Willi Syndrome geneThe Biochemical journal · 2017Review
- Institutional profile: the national Swedish academic drug discovery & development platform at SciLifeLab.Future science OA · 2017Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
The MAGE (melanoma associated antigen) protein family are tumour-associated proteins normally present only in reproductive tissues such as germ cells of the testis. The human genome encodes over 60 MAGE genes of which one class (containing MAGE-A3 and MAGE-A4) are exclusively expressed in tumours, making them an attractive target for the development of targeted and immunotherapeutic cancer treatments. Some MAGE proteins are thought to play an active role in driving cancer, modulating the activity of E3 ubiquitin ligases on targets related to apoptosis. Here we determined the crystal structures of MAGE-A3 and MAGE-A4. Both proteins crystallized with a terminal peptide bound in a deep cleft between two tandem-arranged winged helix domains. MAGE-A3 (but not MAGE-A4), is predominantly dimeric in solution. Comparison of MAGE-A3 and MAGE-A3 with a structure of an effector-bound MAGE-G1 suggests that a major conformational rearrangement is required for binding, and that this conformational plasticity may be targeted by allosteric binders.
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Registered trials
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.