The water-gas shift (WGS) reaction is a well-known step for upgrading carbon monoxide to hydrogen in the production of synthesis gas. For more than 90 years after its first industrial application, many issues in respect of the catalyst, process configuration, reactor design, reaction mechanisms and kinetics have been investigated. More recently, a renewed interest in the WGS reaction carried out in hydrogen perm-selective membrane reactors (MRs) has been observed because of the growing use of polymeric electrolyte membrane (PEM) fuel cells that operate using high-purity hydrogen. Moreover, MRs are viewed as an interesting technology in order to overcome the equilibrium conversion limitations in traditional reactors.This article reviews the most relevant topics of WGS MR technology -catalysis and membrane science. The most used catalysts and relevant progress achieved so far are described and critically reviewed. The effects of the most important parameters affecting the WGS in MRs are detailed. In addition, an overview on the most used membranes in MRs is also presented and discussed. 

In innate immune responses, induction of type-I interferons (IFNs) prevents virus spreading while viral replication is delayed by protein synthesis inhibition. We asked how cells perform these apparently contradictory activities. Using single fibroblast monitoring by flow cytometry and mathematical modeling, we demonstrate that type-I IFN production is linked to cell's ability to enter dsRNA-activated PKR-dependent translational arrest and then overcome this inhibition by decreasing eIF2a phosphorylation through phosphatase 1c cofactor GADD34 (Ppp1r15a) expression. GADD34 expression, shown here to be dependent on the IRF3 transcription factor, is responsible for a biochemical cycle permitting pulse of IFN synthesis to occur in cells undergoing protein synthesis inhibition. Translation arrest is further demonstrated to be key for anti-viral response by acting synergistically with MAVS activation to amplify TBK1 signaling and IFN-b mRNA transcription, while GADD34-dependent protein synthesis recovery contributes to the heterogeneous expression of IFN observed in dsRNA-activated cells.

Protein ubiquitination, a major post-translational modification in eukaryotes, requires an adequate pool of free ubiquitin. Cells maintain this pool by two pathways, both involving deubiquitinases (DUBs): recycling of ubiquitin from ubiquitin conjugates and processing of ubiquitin precursors synthesized de novo. Although many advances have been made in recent years regarding ubiquitin recycling, our knowledge on ubiquitin precursor processing is still limited, and questions such as when are these precursors processed and which DUBs are involved remain largely unanswered. Here we provide data suggesting that two of the four mammalian ubiquitin precursors, UBA52 and UBA80, are processed mostly post-translationally whereas the other two, UBB and UBC, probably undergo a combination of co- and post-translational processing. Using an unbiased biochemical approach we found that UCHL3, USP9X, USP7, USP5 and Otulin/Gumby/FAM105b are by far the most active DUBs acting on these precursors. The identification of these DUBs together with their properties suggests that each ubiquitin precursor can be processed in at least two different manners, explaining the robustness of the ubiquitin de novo synthesis pathway.