Porous organic polymers (POPs), a class of highly crosslinked amorphous polymers possessing nano-pores, have recently emerged as a versatile platform for the deployment of catalysts. The bottom-up approach for porous organic polymer synthesis provides the opportunity for the design of polymer frameworks with various functionalities, for their use as catalysts or ligands. This tutorial review focuses on the framework structures and functionalities of catalytic POPs. Their structural design, functional framework synthesis and catalytic reactions are discussed along with some of the challenges.

Activate and reduce: Carbon dioxide was reduced with silane using a stable N-heterocyclic carbene organocatalyst to provide methanol under very mild conditions. Dry air can serve as the feedstock, and the organocatalyst is much more efficient than transition-metal catalysts for this reaction. This approach offers a very promising protocol for chemical CO(2) activation and fixation.

5-Hydroxymethylfurfural (HMF) has been known as a product from hexose dehydration for over 100 years and is considered to be one of the most promising platform molecules that can be converted into a variety of interesting chemicals. HMF, together with furfural and 2,5-furandicarboxylic acid (FDCA) are derivatives of furan compounds, which were listed as the top 10 value-added bio-based chemicals by the US Department of Energy. The great and increasing interest in the production of furan derivatives from biomass resources is due to the great potential of furan derivatives as feedstock for bulk chemicals and fuels. HMF can be synthesized by dehydration of all types of C6 carbohydrates, including monomeric and polymeric carbohydrates, such as fructose, glucose, sucrose, starch, inulin, cellulose, and raw biomass.Numerous improvements and milestones have been made in the dehydration process during the past 130 years. The big challenge for the process of HMF production is its suitability for industrial scale yet being cost efficient. This perspective article will review the HMF development timeline, focusing on the important events, landmark contributions, engineering and practical challenges of HMF production.

Alpha/beta interferon (IFN-␣/␤) produces antiviral effects through upregulation of many interferon-stimulated genes (ISGs) whose protein products are effectors of the antiviral state. Previous data from our laboratory have shown that IFN-␣/␤ can limit Sindbis virus (SB) replication through protein kinase R (PKR)-dependent and PKR-independent mechanisms and that one PKR-independent mechanism inhibits translation of the infecting virus genome (K. D. Ryman et al., J. Virol. 79:1487-1499, 2005). Further, using Affymetrix microarray technology, we identified 44 genes as candidates for PKR/RNase L-independent IFN-induced antiviral activities. In the current studies, we have begun analyzing these gene products for antialphavirus activity using three techniques: (i) overexpression of the protein from SB vectors and assessment of virulence attenuation in mice; (ii) overexpression of the proteins in a stable tetracycline-inducible murine fibroblast culture system and assessment of effects upon SB replication; and (iii) small interfering RNA-mediated knockdown of gene mRNA in fibroblast cultures followed by SB replication assessment as above. Tested proteins included those we hypothesized had potential to affect virus genome translation and included murine ISG20, ISG15, the zinc finger antiviral protein (ZAP), viperin, p56, p54, and p49. Interestingly, the pattern of antiviral activity for some gene products was different between in vitro and in vivo assays. Viperin and ZAP attenuated virulence most profoundly in mice. However, ISG20 and ZAP potently inhibited SB replication in vitro, whereas and viperin, p56, and ISG15 exhibited modest replication inhibition in vitro. In contrast, p54 and p49 had little to no effect in any assay.

SUMMARY Virus infection is sensed in the cytoplasm by retinoic acid-inducible gene I (RIG-I, also known as DDX58), which requires RNA and polyubiquitin binding to induce type I interferon (IFN), and activate cellular innate immunity. We show that the human IFN-inducible oligoadenylate synthetases-like (OASL) protein had antiviral activity and mediated RIG-I activation by mimicking polyubiquitin. Loss of OASL expression reduced RIG-I signaling and enhanced virus replication in human cells. Conversely, OASL expression suppressed replication of a number of viruses in a RIG-I-dependent manner and enhanced RIG-I-mediated IFN induction. OASL interacted and colocalized with RIG-I, and through its C-terminal ubiquitin-like domain specifically enhanced RIG-I signaling. Bone marrow derived macrophages from mice deficient for Oasl2 showed that among the two mouse orthologs of human OASL; Oasl2 is functionally similar to human OASL. Our findings show a mechanism by which human OASL contributes to host antiviral responses by enhancing RIG-I activation.