Weining Wu
University of Liverpool
15 Papers
9 Citations
Weining Wu is an academic researcher from University of Liverpool. The author has contributed to research in topics: Proteomics & Virus. The author has an hindex of 12, co-authored 14 publications. Previous affiliations of Weining Wu include University of Leeds.
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Papers
Quantitative proteomic analysis of A549 cells infected with human respiratory syncytial virus.
Diane C. Munday,Edward Emmott,Rebecca Surtees,Charles-Hugues Lardeau,Weining Wu,W. Paul Duprex,Brian K. Dove,John N. Barr,Julian A. Hiscox +8 more
TL;DR: The study served to validate and expand upon known HRSV-host cell interactions, including those associated with the antiviral response and alterations in subnuclear structures such as the nucleolus and ND10 (promyelocytic leukemia bodies).
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Elucidation of the Ebola virus VP24 cellular interactome and disruption of virus biology through targeted inhibition of host-cell protein function.
Isabel García-Dorival,Weining Wu,Stuart D. Dowall,Stuart D. Armstrong,Stuart D. Armstrong,Olivier Touzelet,Jonathan M. Wastling,Jonathan M. Wastling,John N. Barr,David A. Matthews,Miles W. Carroll,Roger Hewson,Julian A. Hiscox,Julian A. Hiscox +13 more
TL;DR: To better understand the potential functions of VP24, label-free quantitative proteomics was used to identify cellular proteins that had a high probability of forming the VP24 cellular interactome and disrupted the activity of ATP1A1 in Ebola-virus-infected cells with a small molecule inhibitor resulted in a decrease in progeny virus.
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Nucleocapsid protein structures from orthobunyaviruses reveal insight into ribonucleoprotein architecture and RNA polymerization
Antonio Ariza,Sian J. Tanner,Cheryl T. Walter,Kyle C. Dent,Dale A. Shepherd,Weining Wu,Susan V. Matthews,Julian A. Hiscox,Todd Green,Ming Luo,Richard M. Elliott,Anthony R. Fooks,Alison E. Ashcroft,Nicola J. Stonehouse,Neil A. Ranson,John N. Barr,Thomas A. Edwards +16 more
TL;DR: Comparison between these crystal structures and electron microscopy images of both soluble tetramers and authentic RNPs suggests the N protein does not bind RNA as a repeating monomer; thus, it represents a newly described architecture for bunyavirus RNP assembly, with implications for many other segmented negative-strand RNA viruses.
Crystal structure of the essential transcription antiterminator M2-1 protein of human respiratory syncytial virus and implications of its phosphorylation
Sian J. Tanner,Antonio Ariza,Charles-Adrien Richard,Hannah F. Kyle,Rachel L. Dods,Marie-Lise Blondot,Weining Wu,José Trincão,Chi H. Trinh,Julian A. Hiscox,Miles W. Carroll,Nigel Silman,Jean-François Eléouët,Thomas A. Edwards,John N. Barr +14 more
TL;DR: This structure reveals how M2-1 forms an extremely stable tetramer and has allowed us to pinpoint the location of critical regions that regulate M1-1 activity, providing insight into its function and identifies surfaces critical for M 2-1 function that may be targeted by antiviral compounds.
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Elucidation of the Cellular Interactome of Ebola Virus Nucleoprotein and Identification of Therapeutic Targets
Isabel García-Dorival,Isabel García-Dorival,Weining Wu,Stuart D. Armstrong,Stuart D. Armstrong,John N. Barr,Miles W. Carroll,Roger Hewson,Julian A. Hiscox,Julian A. Hiscox +9 more
TL;DR: This work focused on defining the interactome of the EBOV nucleoprotein and identified that cellular chaperones, including HSP70, associate with this protein to promote stability and demonstrate that disrupting the stability of NP had an adverse effect on viral RNA synthesis.