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Migrating cells are restricted by their ability to squeeze their nuclei through pores in the extracellular matrix.

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Briggs studies the organization of viral and cellular coat proteins using cryo-electron microscopy.

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Plant virus movement proteins compartmentalize replication complexes at plasmodesmata for localized RNA synthesis and directional trafficking of the virus between cells.

A genome-wide screen of phosphatases that control mitosis identified CDKN3, which acts through the CDC2 signaling axis.

The spindle checkpoint, APC/C-Cdc20, and APC/C-Cdh1 act successively to connect disappearance of geminin and cyclin B1 to a peak of Cdt1 and Cdc6.

Engineered Golgi-resident constructs that can be polymerized at will to prevent their recycling via Golgi carriers provide evidence for the cisternal maturation mechanism of secretory protein transport through the Golgi.

The splice isoform Drp1-x01 promotes mitochondrial fission and is regulated by Cdk phosphorylation-dependent changes in microtubule association.

Crystals soaked with RGD peptides reveal six intermediate conformational states between the closed and higher affinity, fully open state of the integrin αIIbβ3 headpiece.

The physical limits of cell migration in dense porous environments are dependent upon the available space and the deformability of the nucleus and are modulated by matrix metalloproteinases, integrins and actomyosin function.

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