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Defective proteins in the endoplasmic reticulum (ER) are tagged as terminally aberrant by the composition of their N-linked glycans. The ER carbohydrate-binding protein EDEM selectively recognizes such tags and sorts the defective proteins for degradation via the ERAD pathway.
Structural characterization of the DCX domains from doublecortin reveals novel mechanisms for microtubule binding in a protein essential for brain development.
Cryo-electron microscopy has been used to study the stepwise maturation of herpes simplex virus capsids. This approach should be useful for exploring other dynamic processes in biology.
The structure of Plasmodium falciparum dihydrofolate reductase–thymidylate synthase, a target of clinically established antimalarial drugs, reveals the nature of inhibitor binding, drug resistance and autologous gene repression, all of which influence species-specific drug sensitivity.