Advancement in the pressureless sintering of CP titanium using high-frequency induction heating

High-frequency induction heating is applied as an alternative heating source for pressureless sintering of commercially pure Ti powders, aiming to intensify the sintering process. The effects of the process parameters on the properties of the sintered material are systematically studied. The initial powder compact density is the most influential parameter permitting sintered structures with highly porous to almost fully dense appearance. Short heating time combined with sintering to temperatures just above the β-transus resulted in a strong diffusion bonding between the Ti powder particles, and grain growth is observed at the former boundaries of the neighboring powder particles. The dimpled appearance of the fracture surface at those regions confirmed the strong metallic interparticle bonding. Tensile properties comparable to those of Ti-Grade 3 and Ti-Grade 4 are achieved, which also demonstrates the efficiency of the induction sintering process. A mechanism explaining the fast and efficient sintering is proposed. The process has the added advantage of minimizing the oxygen pickup

Protein Phosphatases at the Nuclear Envelope

© 2018 The Author(s). The Nuclear Envelope (NE) is a unique topological structure formed by lipid membranes (Inner and Outer Membrane- IM and OM) interrupted by open channels (Nuclear Pore complexes). Besides its well established structural role in providing a physical separation between the genome and the cytoplasm and regulating the exchanges between the two cellular compartments, it has become quite evident in recent years that the NE also represents a hub for localised signal transduction. Mechanical, stress or mitogen signals reach the nucleus and trigger the activation of several pathways, many effectors of which are processed at the NE. Therefore, the concept of the NE acting just as a barrier needs to be expanded to embrace all the dynamic processes that are indeed associated with it. In this context, dynamic protein association and turnover coupled to reversible post-translational modifications of NE components can provide important clues on how this integrated cellular machinery functions as a whole. Reversible protein phosphorylation is the most used mechanism to control protein dynamics and association in cells. Keys to the reversibility of the system are protein phosphatases and the regulation of their activity in space and time. As the NE is clearly becoming an interesting compartment for the control and transduction of several signalling pathways, in this review we will focus on the role of Protein Phosphatases at the NE since the significance of this class of proteins in this context has been little explored.BBSRC grant BB/K017632/1, Wellcome Trust Investigator Award in Science 210742/Z/18/Z, Brunel IDEA AWARD, Isambard PhD studentship, Cluster of Excellence Cellular Networks (Heidelberg, Germany