DMA-tudor interaction modules control the specificity of in vivo condensatesThe SMN tudor domain is sufficient for condensation by binding to dimethylarginine (DMA) modified protein ligands. Asymmetric versus symmetric DMA determines whether gems and Cajal bodies were separate or “docked” to one another.The SMN tudor domain is sufficient for condensation by binding to dimethylarginine (DMA) modified protein ligands. Asymmetric versus symmetric DMA determines whether gems and Cajal bodies were separate or “docked” to one another.Edward M. Courchaine, Andrew E.S. Barentine, Korinna Straube, Dong-Ryoung Lee, Joerg Bewersdorf, Karla M. Neugebauerhttps://secure.jbs.elsevierhealth.com/action/getSharedSiteSession?redirect=https%3A%2F%2Fwww.cell.com%2Fcell%2Ffulltext%2FS0092-8674%2821%2900625-5%3Frss%3Dyes&rc=0http://www.cell.com/cell/inpress.rssCellCell RSS feed.Wireless News CampaignJune 11, 2021

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