分类： 天文学 >> 天文学 提交时间： 2024-05-10 合作期刊: 《Research in Astronomy and Astrophysics》
摘要： Rotating Radio Transients (RRATs) are a relatively new subclass of pulsars that emit detectable radio bursts sporadically. We analyzed 10 RRATs observed using the Parkes telescope, with eight of these observed via the ultra-wide-bandwidth low-frequency (UWL) receiver. We measured the burst rate and produced integrated profiles spanning multiple frequency bands for three RRATs. We also conducted a spectral analysis on both integrated pulses and individual pulses of three RRATs. All of their integrated pulses follow a simple power law, consistent with the known range of pulsar spectral indices. Their average spectral indices of single pulses are −0.9, −1.2, and −1.0 respectively, which are within the known range of pulsar spectral indices. Additionally, we find that the spreads of single-pulse spectral indices for these RRATs (ranging from −3.5 to +0.5) are narrower compared to what has been observed in other RRATs. Notably, the average spectral index and scatter of single pulses are both relatively small. For the remaining five RRATs observed at the UWL receiver, we also provide the upper limits on fluence and flux density. In addition, we obtain the timing solution of PSR J1709-43. Our analysis shows that PSRs J1919+1745, J1709-43, and J1649-4653 are potentially nulling pulsars or weak pulsars with sparse strong pulses.
分类： 生物学 >> 生物物理学 提交时间： 2016-05-05
Guo, Yu
Ma, Chao
Wang, Xu
Wang, Xin
Liu, Pi
Lin, Jianping
Guo, Yu
Ma, Chao
Wang, Xu
Wang, Xin
Liu, Pi
Lin, Jianping
Lou, Zhiyong
Lou, Zhiyong
Sun, Yuna
Lou, Zhiyong
Shen, Shu
Deng, Fei
Wang, Hualin
Wang, Wenming
摘要： Hantaviruses, which belong to the genus Hantavirus in the family Bunyaviridae, infect mammals, including humans, causing either hemorrhagic fever with renal syndrome (HFRS) or hantavirus cardiopulmonary syndrome (HCPS) in humans with high mortality. Hantavirus encodes a nucleocapsid protein (NP) to encapsidate the genome and form a ribonucleoprotein complex (RNP) together with viral polymerase. Here, we report the crystal structure of the core domains of NP (NPcore) encoded by Sin Nombre virus (SNV) and Andes virus (ANDV), which are two representative members that cause HCPS in the New World. The constructs of SNV and ANDV NPcore exclude the N- and C-terminal portions of full polypeptide to obtain stable proteins for crystallographic study. The structure features an N lobe and a C lobe to clamp RNA-binding crevice and exhibits two protruding extensions in both lobes. The positively charged residues located in the RNA-binding crevice play a key role in RNA binding and virus replication. We further demonstrated that the C-terminal helix and the linker region connecting the N-terminal coiled-coil domain and NPcore are essential for hantavirus NP oligomerization through contacts made with two adjacent protomers. Moreover, electron microscopy (EM) visualization of native RNPs extracted from the virions revealed that a monomer-sized NP-RNA complex is the building block of viral RNP. This work provides insight into the formation of hantavirus RNP and provides an understanding of the evolutionary connections that exist among bunyaviruses. IMPORTANCE Hantaviruses are distributed across a wide and increasing range of host reservoirs throughout the world. In particular, hantaviruses can be transmitted via aerosols of rodent excreta to humans or from human to human and cause HFRS and HCPS, with mortalities of 15% and 50%, respectively. Hantavirus is therefore listed as a category C pathogen. Hantavirus encodes an NP that plays essential roles both in RNP formation and in multiple biological functions. NP is also the exclusiv
点击量
通过
点击量
下载量
评论
待评议
