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Lin Bai,Qiaoyu Li,Wei Bai,Jinho Choi IET 2014 IET COMMUNICATIONS Vol.8 No.5
<P>For iterative detection and decoding (IDD) in multiple-input-multiple-output (MIMO) systems, although the maximum a posteriori (MAP) detector can achieve an optimal performance, because of its prohibitively high computational complexity, various low-complexity approximate MAP detectors are studied. Among the existing MIMO detectors for the non-IDD receivers, lattice reduction (LR)-aided detectors can provide a near maximum-likelihood (ML) detector's performance with reasonably low complexity, and they could be modified to be used in the IDD receivers. In this study, the authors propose a bit-level LR-aided MIMO detector whose performance can approach that of the MAP detector, where a priori information is taken into account for soft-decisions. Furthermore, the proposed method can be extended to large dimensional MIMO systems by channel matrix decomposition and successive interference cancellation, by which a significant complexity reduction can be achieved. Through simulations and complexity analysis, it is shown that a near-optimal performance is obtained by the authors proposed low-complexity bit-level LR-aided detector for the IDD in the MIMO systems.</P>
Fang, Xiaonan,Ye, Linbai,Timani, Khalid Amine,Li, Shanshan,Zen, Yingchun,Zhao, Meng,Zheng, Hong,Wu, Zhenghui Korean Society for Biochemistry and Molecular Biol 2005 Journal of biochemistry and molecular biology Vol.38 No.4
Severe acute respiratory syndrome (SARS) is an emerging infectious disease associated with a novel coronavirus (CoV) that was identified and molecularly characterized in 2003. Previous studies on various coronaviruses indicate that protein-protein interactions amongst various coronavirus proteins are critical for viral assembly and morphogenesis. It is necessary to elucidate the molecular mechanism of SARS-CoV replication and rationalize the anti-SARS therapeutic intervention. In this study, we employed an in vitro GST pull-down assay to investigate the interaction between the membrane (M) and the nucleocapsid (N) proteins. Our results show that the interaction between the M and N proteins does take place in vitro. Moreover, we provide an evidence that 12 amino acids domain (194-205) in the M protein is responsible for binding to N protein. Our work will help shed light on the molecular mechanism of the virus assembly and provide valuable information pertaining to rationalization of future anti-viral strategies.
Hepatitis C Virus Non-structural Protein NS4B Can Modulate an Unfolded Protein Response
Yi Zheng,Bo Gao,Li Ye,Lingbao Kong,Wei Jing,Xiaojun Yang,Zhenghui Wu,Linbai Ye 한국미생물학회 2005 The journal of microbiology Vol.43 No.6
Viral infection causes stress to the endoplasmic reticulum (ER). The response to endoplasmic reticulum stress, known as the unfolded protein response (UPR), is designed to eliminate misfolded proteins and allow the cell to recover. The role of hepatitis C virus (HCV) non-structural protein NS4B, a component of the HCV replicons that induce UPR, is incompletely understood. We demonstrate that HCV NS4B could induce activating transcription factor (ATF6) and inositol-requiring enzyme 1 (IRE1), to favor the HCV subreplicon and HCV viral replication. HCV NS4B activated the IRE1 pathway, as indicated by splicing of X box-binding protein (Xbp-1) mRNA. However, transcriptional activation of the XBP-1 target gene, EDEM (ER degradation-enhancing α-mannosidase-like protein, a protein degradation factor), was inhibited. These results imply that NS4B might induce UPR through ATF6 and IRE1- XBP1 pathways, but might also modify the outcome to benefit HCV or HCV subreplicon replication.
Hepatitis C Virus Non-structural Protein NS4B Can Modulate an Unfolded Protein Response
Zheng Yi,Gao Bo,Ye Li,Kong Lingbao,Jing Wei,Yang Xiaojun,Wu Zhenghui,Ye Linbai The Microbiological Society of Korea 2005 The journal of microbiology Vol.43 No.6
Viral infection causes stress to the endoplasmic reticulum (ER). The response to endoplasmic reticulum stress, known as the unfolded protein response (UPR), is designed to eliminate misfolded proteins and allow the cell to recover. The role of hepatitis C virus (HCV) non-structural protein NS4B, a component of the HCV replicons that induce UPR, is incompletely understood. We demonstrate that HCV NS4B could induce activating transcription factor (ATF6) and inositol-requiring enzyme 1 (IRE1), to favor the HCV subreplicon and HCV viral replication. HCV NS4B activated the IRE1 pathway, as indicated by splicing of X box-binding protein (Xbp-1) mRNA. However, transcriptional activation of the XBP-1 target gene, EDEM (ER degradation-enhancing $\alpha-mannosidase-like$ protein, a protein degradation factor), was inhibited. These results imply that NS4B might induce UPR through ATF6 and IRE1-XBP1 pathways, but might also modify the outcome to benefit HCV or HCV subreplicon replication.