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A 2.4-GHz fully integrated frequency synthesizer is presented in this paper for Low-IF ZigBee (IEEE802.15.4) transceiver applications. The frequency synthesizer meets the system requirement of 2.4-2.4835GHz frequency range with a frequency resolution of 5 MHz. The automaticamplitude control (AAC) technique is employed for the voltage-controlled oscillator (VCO) which helps to optimize the output amplitude of the VCO over voltage, process and temperature variations. The chip has been fabricated in a 0.18 µm complementary metal oxide semiconductor (CMOS) process using a single poly layer, four metal layers and metal-insulator-metal (MIM) capacitors. The synthesized has a current dissipation of 4.7mA from a 1.8V power supply and occupies an area of 1mm² × 0:85mm². Measurement results show that the phase noise are 82 dBc/Hz-100 kHz offset and -109 dBc/Hz-1MHz offset respectively. [ABSTRACT FROM AUTHOR]

Rabies, as the oldest known infectious disease, remains a serious threat to public health worldwide. The eukaryotic cytosolic chaperonin TRiC/CCT complex facilitates the folding of proteins through ATP hydrolysis. Here, we investigated the expression, cellular localization, and function of neuronal CCT? during neurotropic rabies virus (RABV) infection using mouse N2a cells as a model. Following RABV infection, 24 altered proteins were identified by using two-dimensional electrophoresis and mass spec-trometry, including 20 upregulated proteins and 4 downregulated proteins. In mouse N2a cells infected with RABV or cotrans-fected with RABV genes encoding nucleoprotein (N) and phosphoprotein (P), confocal microscopy demonstrated that upregu-lated cellular CCT? was colocalized with viral proteins N and P, which formed a hollow cricoid inclusion within the region around the nucleus. These inclusions, which correspond to Negri bodies (NBs), did not form in mouse N2a cells only expressing the viral protein N or P. Knockdown of CCT? by lentivirus-mediated RNA interference led to significant inhibition of RABV replication. These results demonstrate that the complex consisting of viral proteins N and P recruits CCT? to NBs and identify the chaperonin CCT? as a host factor that facilitates intracellular RABV replication. This work illustrates how viruses can utilize cellular chaperonins and compartmentalization for their own benefit. [ABSTRACT FROM AUTHOR]

Abstract  Strain AM105 was separated from mangrove sediment in the South China Sea in this research. The morphological and genomic data showed that the strain merits description as a novel species, proposed as Micromonospora rifamycinica. From the acetate ethyl extract of its fermentation broth, two antibiotics against Gram-positive bacteria (including MRSA), rifamycin S and its geometric isomer were isolated. Their structures were elucidated on the basis of spectroscopic analyzes. 1H and 13C NMR data of the isomer of rifamycin S were first described in this paper. [ABSTRACT FROM AUTHOR]

Interferon-stimulated genes (ISGs) create multiple lines of defense against viral infection. Here, we show that interferon-induced protein 35 (IFI35) inhibits swine (H3N2) influenza virus replication by directly interacting with the viral protein NS1. IFI35 binds more preferentially to the effector domain of NS1 (amino acids 128 to 207 [128-207aa]) than to the viral RNA sensor RIG-I. This promotes mutual antagonism between IFI35 and NS1 and frees RIG-I from IFI35-mediated K48-linked ubiquitination and degradation. However, IFI35 does not interact with the NS1 encoded by avian (H7N9) influenza virus, resulting in IFI35 playing an opposite virus-enabling role during highly pathogenic H7N9 virus infection. Notably, replacing the 128-207aa region of H7N9 NS1 with the corresponding region of H3N2 NS1 results in the chimeric NS1 acquiring the ability to bind to and mutually antagonize IFI35. IFI35-deficient mice accordingly exhibit more resistance to lethal H7N9 infection than exhibited by their wild-type control. Our data uncover a novel mechanism by which IFI35 regulates RIG-I-mediated antiviral immunity through mutual antagonism with influenza virus protein NS1. [ABSTRACT FROM AUTHOR]