Related Articles from Rockefeller University Press
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This study identifies patients with autoinflammation and mutations affecting the mitochondrial/ER protein chaperone TRAP1, either alone or digenic, with MEFV mutation possibly synergizing to produce severe disease. TRAP1 mutations lead to increased mitochondrial reactive oxygen species and may contribute to autoinflammation.
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An expanded hydrophobic cavity within the structurally constrained receptor-binding site of the Cedar virus attachment glycoprotein facilitates idiosyncratic utilization of ephrin-B1.
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Irgb6 has a role in the cell-autonomous response against T. gondii and involves ubiquitination and breakdown of vacuoles via binding of a specific phospholipid on the parasitophorous vacuole membrane.