The N-terminal domain of the Schaaf–Yang syndrome protein MAGEL2 likely has a role in RNA metabolism
Author:
Funder
Foundation for Prader-Willi Research
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference134 articles.
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4. MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases;Doyle;Mol. Cell,2010
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1. Truncated variants of MAGEL2 are involved in the etiologies of the Schaaf-Yang and Prader-Willi syndromes;The American Journal of Human Genetics;2024-07
2. Weighted gene coexpression network analysis and machine learning for the determination of tfh cell and B cell infiltrating biomarkers in thymoma-associated myasthenia gravis;Heliyon;2024-07
3. MAGEL2 (patho‐)physiology and Schaaf–Yang syndrome;Developmental Medicine & Child Neurology;2024-07
4. YTHDF2 protein stabilization by the deubiquitinase OTUB1 promotes prostate cancer cell proliferation via PRSS8 mRNA degradation;Journal of Biological Chemistry;2024-04
5. Subcellular localisation of truncated MAGEL2 proteins: insight into the molecular pathology of Schaaf-Yang syndrome;Journal of Medical Genetics;2024-03-28
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