scholarly journals Identification of a Pharmacological Biomarker for the Bioassay-Based Quality Control of a Thirteen-Component TCM Formula (Lianhua Qingwen) Used in Treating Influenza A Virus (H1N1) Infection

2020 ◽  
Vol 11 ◽  
Author(s):  
Dan Gao ◽  
Ming Niu ◽  
Shi-zhang Wei ◽  
Cong-en Zhang ◽  
Yong-feng Zhou ◽  
...  
2011 ◽  
Vol 7 (11) ◽  
pp. e1002341 ◽  
Author(s):  
Toshihiro Ito ◽  
Ronald M. Allen ◽  
William F. Carson ◽  
Matthew Schaller ◽  
Karen A. Cavassani ◽  
...  

Virology ◽  
2016 ◽  
Vol 496 ◽  
pp. 131-137 ◽  
Author(s):  
Liqian Zhu ◽  
Chen Yuan ◽  
Xiuyan Ding ◽  
Shuai Xu ◽  
Jiayun Yang ◽  
...  

The Analyst ◽  
2015 ◽  
Vol 140 (13) ◽  
pp. 4566-4575 ◽  
Author(s):  
Jacky F. C. Loo ◽  
S. S. Wang ◽  
F. Peng ◽  
J. A. He ◽  
L. He ◽  
...  

A new non-PCR assay platform using RNase H to detect MicroRNA 29a-3p from patients’ throat swabs with influenza A virus H1N1 infection.


PLoS ONE ◽  
2011 ◽  
Vol 6 (12) ◽  
pp. e28102 ◽  
Author(s):  
Chen-Yen Kuo ◽  
Yhu-Chering Huang ◽  
Chung-Guei Huang ◽  
Kuo-Chien Tsao ◽  
Tzou-Yien Lin

2021 ◽  
Author(s):  
Lehao Ren ◽  
Wanju Zhang ◽  
Jing Zhang ◽  
Jiaxiang Zhang ◽  
Huiying Zhang ◽  
...  

AbstractViruses depend on host cellular metabolism to provide the energy and biosynthetic building blocks required for their replication. In this study, we observed that influenza A virus (H1N1), a single-stranded, negative-sense RNA virus with an eight-segmented genome, enhanced glycolysis both in mouse lung tissues and in human lung epithelial (A549) cells. In detail, the expression of hexokinase 2 (HK2), the first enzyme in glycolysis, was upregulated in H1N1-infected A549 cells, and the expression of pyruvate kinase M2 (PKM2) and pyruvate dehydrogenase kinase 3 (PDK3) was upregulated in H1N1-infected mouse lung tissues. Pharmacologically inhibiting the glycolytic pathway or targeting hypoxia-inducible factor 1 (HIF-1), the central transcriptional factor critical for glycolysis, significantly reduced H1N1 replication, revealing a requirement for glycolysis during H1N1 infection. In addition, pharmacologically enhancing the glycolytic pathway further promoted H1N1 replication. Furthermore, the change of H1N1 replication upon glycolysis inhibition or enhancement was independent of interferon signaling. Taken together, these findings suggest that influenza A virus induces the glycolytic pathway and thus facilitates efficient viral replication. This study raises the possibility that metabolic inhibitors, such as those that target glycolysis, could be used to treat influenza A virus infection in the future.


1980 ◽  
Vol 141 (5) ◽  
pp. 548-554 ◽  
Author(s):  
C. B. Smith ◽  
R. P. Charette ◽  
J. P. Fox ◽  
M. K. Cooney ◽  
C. E. Hall

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