Selective APC/C-mediated proteolysis of cyclin B drives progression through the metaphase-anaphase transition whilst wide-spread waves of dephosphorylation co-ordinate the subsequent events of mitotic exit.

In contrast to other transcription factors, CTCF and Esrrb rapidly regain binding after replication and remain bound to their targets during mitosis, preserving local nucleosome organization throughout the cell cycle.

High-resolution single-cell mass accumulation and protein synthesis rate measurements are used to quantify the extent, dynamics and consequences of animal cell growth in mitosis and cytokinesis.

Extensive cytological and biochemical analyses show that the conserved Sf3A2 and Prp31 splicing factors bind microtubules and the Ndc80 complex, playing direct mitotic functions in both Drosophila and human mitosis.

Ribosomal profiling reveals that translational repression is an important mechanism for cell cycle control and can complement protein degradation.

Direct live-cell imaging of human cells, combined with RNA-seq, qPCR and in vitro reconstitution essays, reveal that mitotic progression, arrest, exit or death is independent of de novo transcription.

A detailed analysis of protein abundance and phosphorylation changes across mitotic subphases and interphase in asynchronously growing human cells has been enabled by combining FACS with quantitative MS-based proteomics.

Biochemical analysis on hetero-mutated c₁₀ subunits ring and molecular dynamics simulations demonstrate the cooperation among c-subunits of F_oF₁-ATP synthase in rotation-coupled proton translocation.

A combination of in vivo and in vitro approaches using Xenopus eggs and embryos reveals how dimensions of mitotic chromosomes scale with decreasing cell size and increasing nuclear-cytoplasmic ratio during early embryogenesis.

Nuclei and spatial system dimensions control local concentrations of cell cycle regulators, determining the spatial origin of waves that coordinate​ DNA replication and, subsequently, cell division.