Beyond every binary is a more complex reality. And so it is with driver and passenger mutations. The separation of tumor mutations into drivers and passengers underpins much progress in the development of targeted therapies.

Everything’s good for something. Including, it turns out, 5’ untranslated trinucleotide repeats. In the Feb. 17, 2020, issue of Nature Neuroscience, researchers have demonstrated a role for such repeats in controlling protein levels of fragile X mental retardation protein (FMRP).

BioWorld looks at translational medicine, including: Noncoding RNA protects blood vessel walls; PD-1 blockade interferes with opioid analgesia; T-cell population is biomarker for beta cell function; Glutaminase 1 is NASH target; Oligodendrocyte-neural connections not just about myelin; Sharper look yields new potential kinase target in ovarian cancer; Structural insights could enable specific activation of GPCRs; Autophagy activation may prevent metastasis; AI finds structurally unique antibiotics.

Beyond every binary is a more complex reality. And so it is with driver and passenger mutations. The separation of tumor mutations into drivers and passengers underpins much progress in the development of targeted therapies. By looking at passenger mutations more carefully, though, researchers at Yale University have shown that passenger mutations, too, played a role in how tumors progressed.

Parkinson’s disease (PD) is a neurodegenerative disorder. But not just. And it may not start that way. There is increasing evidence that a-synuclein, the protein whose aggregates eventually destroy midbrain dopaminergic neurons in PD (and that are the cause of other diseases collectively known as the synucleinopathies), first aggregates “in enteric neurons, the neurons that control gastrointestinal function,” Collin Challis told BioWorld.