Activation of the NACHT, leucine‐rich repeat, and pyrin domains‐containing protein 3 (collectively known as NLRP3) inflammasome plays a key role in host immune response, which is the first line of defense against cellular stresses and pathogen infections. However, excessive inflammasome activation damages host cells, and therefore it must be precisely controlled. Here, we discover that Cullin1 (CUL1), a key component of the Skp1‐Cullin1‐F‐box E3 ligase, plays a critical role in controlling the NLRP3 inflammasome. CUL1 represses inflammasome assembly in cultured cells, suppresses NLRP3 function in human monocytic cell line macrophages, and attenuates inflammatory responses in mouse model. Detailed studies demonstrate that CUL1 interacts with NLRP3 and promotes NLRP3 ubiquitination, but not protein degradation, to repress the NLRP3 inflammasome activation. Moreover, upon inflammatory stimuli, including ATP and nigericin treatments, CUL1 disassociates from NLRP3 to release the repression of the NLRP3 inflammasome. Thus, this study reveals a distinct and unique mechanism underlying the control of systematic activation of the NLRP3 inflammasome.—Wan, P., Zhang, Q., Liu, W., Jia, Y., Ai, S., Wang, T., Wang, W., Pan, P., Yang, G., Xiang, Q., Huang, S., Yang, Q., Zhang, W., Liu, F., Tan, Q., Zhang, W., Wu, K., Liu, Y., Wu, J. Cullin1 binds and promotes NLRP3 ubiquitination to repress systematic inflammasome activation. FASEB J. 33, 5793–5807 (2019). http://www.fasebj.org

Index Terms-High-speed integrated circuits, inductance measurement, integrated circuit interconnections, integrated circuit modeling, scattering parameters measurement, skin effect.

Enterovirus 71 (EV71) infection causes hand, foot, and mouth disease (HFMD), and even fatal neurological complications. However, the mechanisms underlying EV71 neurological pathogeneses are largely unknown. This study reveals a distinct mechanism by which EV71 induces apoptosis and autophagy in neural cells. EV71 non-structure protein 3D (also known as RNA-dependent RNA polymerase, RdRp) interacts with the peroxisomal protein acyl-CoA oxidase 1 (ACOX1), and contributes to ACOX1 downregulation. Further studies demonstrate that EV71 reduces peroxisome numbers. Additionally, knockdown of ACOX1 or peroxin 19 (PEX19) induces apoptosis and autophagy in neural cells including human neuroblastoma (SK-N-SH) cells and human astrocytoma (U251) cells, and EV71 infection induces neural cell death through attenuating ACOX1 production. Moreover, EV71 infection and ACOX1 knockdown facilitate reactive oxygen species (ROS) production and attenuate the cytoprotective protein deglycase (DJ-1)/Nuclear factor erythroid 2-related factor 2 (NRF2)/Heme oxygenase 1 (HO-1) pathway (DJ-1/NRF2/HO-1), which collectively result in ROS accumulation in neural cells. In conclusion, EV71 downregulates ACOX1 protein expression, reduces peroxisome numbers, enhances ROS generation, and attenuates the DJ-1/NRF2/HO-1 pathway, thereby inducing apoptosis and autophagy in neural cells. These findings provide new insights into the mechanism underlying EV71-induced neural pathogenesis, and suggest potential treatments for EV71-associated diseases.

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Electrochemical and chemical oxidation methods are the two common methods used for the preparation of poly(pyrrole). The two methods have been acknowledged greatly and extensively studied because of their feasibility in manipulating the properties of poly(pyrrole) according to the desired application. However, chemical oxidation method is considered the best method for the preparation of poly(pyrrole) in larger quantities. There are other methods through which poly(pyrrole) can be synthesized such as plasma polymerization and photopolymerization, which have so far received less attention in the literature. For this paper, chemical oxidation was used to prepare poly(pyrrole) by oxidizing pyrrole with CuCl 2 under different emulsifying conditions. The surfactants used were sodium dodecyl sulfate and/or p-toluenesulfonic acid. Additionally, photopolymerization was also exploited to prepare poly(pyrrole) under similar emulsifying conditions. In this method, poly(pyrrole) was synthesized with the oxidizing ability of AgNO 3 under UV radiation. All samples were investigated by Fourier Transform-Infrared Spectroscopy (FT-IR), X-ray Photoelectron Spectroscopy (XPS), and Powder X-ray Diffraction (XRD). Scanning electron microscope was used to compare the morphological differences, which occurred due to different experimental conditions. The thermal stability was studied using thermogravimetric analysis (TGA).