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7. CEOs’ Green Innovation Awareness in Manufacturing Companies: Enhancing Environmental Performance through Supply Chain Integration

Author

Liu, Suyang, Appolloni, Andrea, Series Editor, Caracciolo, Francesco, Series Editor, Ding, Zhuoqi, Series Editor, Gogas, Periklis, Series Editor, Huang, Gordon, Series Editor, Nartea, Gilbert, Series Editor, Ngo, Thanh, Series Editor, Striełkowski, Wadim, Series Editor, Liao, Junfeng, editor, Li, Hongbo, editor, and Ng, Edward H. K., editor

Published
2024
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17. High-Precision Digital Clock Steering Method Based on Discrete Σ-Δ Modulation for GNSS.

Author

Liu, Mingkai, Meng, Zhijun, Yan, Enqi, Liu, Suyang, Lv, Yinhong, Guo, Xiye, and Yang, Jun

Subjects
GLOBAL Positioning System
Abstract

A high-precision time reference is fundamental to the positioning, navigation, and timing (PNT) of global navigation satellite systems (GNSS). The precision of clock steering determines the accuracy of practical applications that rely on the time–frequency reference. With the invention of direct digital synthesizer (DDS) technology, digital clock steering (DCS) has gradually become a mainstream technology. However, the key factor limiting DCS accuracy is the system quantization noise, which leads to a low frequency and phase adjustment accuracy. Here we propose a DCS method based on Σ - Δ modulation to address the issue of low resolution of DAC through shaping the quantization noise. A simulated GNSS time–frequency reference system experimental platform is constructed to validate the effectiveness of the proposed method. The experimental results demonstrate that this method achieves a phase adjustment accuracy of 0.48 ps and a frequency adjustment accuracy better than 0.48 pHz, which is two orders of magnitude higher than that of existing GNSS time–frequency reference systems. Thus, the proposed method offers a significant improvement in time–frequency reference systems, leading to better performance, reliability, and accuracy in a wide range of practical applications. [ABSTRACT FROM AUTHOR]

Published
2024
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24. Functional Genomics Reveals Linkers Critical for Influenza Virus Polymerase

Author

Wang, Lulan, Wu, Aiping, Wang, Yao E, Quanquin, Natalie, Li, Chunfeng, Wang, Jingfeng, Chen, Hsiang-Wen, Liu, Suyang, Liu, Ping, Zhang, Hong, Qin, F Xiao-Feng, Jiang, Taijiao, and Cheng, Genhong

Subjects
Vaccine Related, Prevention, Biodefense, Genetics, Infectious Diseases, Pneumonia & Influenza, Influenza, Emerging Infectious Diseases, Aetiology, 1.1 Normal biological development and functioning, 2.2 Factors relating to the physical environment, Underpinning research, Infection, Animals, Cell Line, DNA Mutational Analysis, Humans, Influenza A virus, RNA Stability, RNA, Messenger, RNA, Viral, RNA-Dependent RNA Polymerase, Viral Proteins, RNA Replicase, Biological Sciences, Agricultural and Veterinary Sciences, Medical and Health Sciences, Virology
Abstract

UnlabelledInfluenza virus mRNA synthesis by the RNA-dependent RNA polymerase involves binding and cleavage of capped cellular mRNA by the PB2 and PA subunits, respectively, and extension of viral mRNA by PB1. However, the mechanism for such a dynamic process is unclear. Using high-throughput mutagenesis and sequencing analysis, we have not only generated a comprehensive functional map for the microdomains of individual subunits but also have revealed the PA linker to be critical for polymerase activity. This PA linker binds to PB1 and also forms ionic interactions with the PA C-terminal channel. Nearly all mutants with five-amino-acid insertions in the linker were nonviable. Our model further suggests that the PA linker plays an important role in the conformational changes that occur between stages that favor capped mRNA binding and cleavage and those associated with viral mRNA synthesis.ImportanceThe RNA-dependent RNA polymerase of influenza virus consists of the PB1, PB2, and PA subunits. By combining genome-wide mutagenesis analysis with the recently discovered crystal structure of the influenza polymerase heterotrimer, we generated a comprehensive functional map of the entire influenza polymerase complex. We identified the microdomains of individual subunits, including the catalytic domains, the interaction interfaces between subunits, and nine linkers interconnecting different domains. Interestingly, we found that mutants with five-amino-acid insertions in individual linkers were nonviable, suggesting the critical roles these linkers play in coordinating spatial relationships between the subunits. We further identified an extended PA linker that binds to PB1 and also forms ionic interactions with the PA C-terminal channel.

Published
2016

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