Developing a peptide to disrupt cohesin head domain interactions.

Cohesin mediates the 3-D structure of chromatin and is involved in maintaining genome stability and function. The cohesin core comprises Smc1 and Smc3, elongated-shaped proteins that dimerize through globular domains at their edges, called head and hinge. ATP binding to the Smc heads induces their dimerization and the formation of two active sites, while ATP hydrolysis results in head disengagement.

Suprapatellar Tibial Nailing: Future or Fad?

Over the last hundred years, there have been significant advancements in the way the Orthopaedic community treats tibial fractures. More recently, the focus of Orthopaedic trauma surgeons has been comparing the different techniques of insertion for tibial nails, specifically suprapatellar (SPTN) versus infrapatellar. The existing literature is convincing that there does not appear to be any clinically significant differences between suprapatellar and infrapatellar tibial nailing, with some apparent benefits of SPTN.

It's all in the numbers: Cohesin stoichiometry.

Cohesin, a structural maintenance of chromosome (SMC) complex, organizes chromatin into three-dimensional structures by threading chromatin into loops and stabilizing long-range chromatin interactions. Four subunits in a 1:1:1:1 ratio compose the cohesin core, which is regulated by auxiliary factors that interact with or modify the core subunits. An ongoing debate about cohesin's mechanism of action regards its stoichiometry.

Fold-change of chromatin condensation in yeast is a conserved property.

During mitosis, chromatin is condensed and organized into mitotic chromosomes. Condensation is critical for genome stability and dynamics, yet the degree of condensation is significantly different between multicellular and single-cell eukaryotes. What is less clear is whether there is a minimum degree of chromosome condensation in unicellular eukaryotes.