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Departamento de Física, Universidade de Aveiro, Aveiro, Portugal, CICECO, Universidade de Aveiro, Publication Date (Web): September 4, .. The Journal of Physical Chemistry C (29), .. Lei Zhang, Linlin Fu, Xingxing Yang, Zuoling Fu, Xiangdong Qi, Zhijian Wu. Chem., , (26), pp – Qian Zhou, Kendall Fitzgerald, Paul D. Boyle and Wesley A. Henderson Shu Li, Zhen Cao, Yuxing Peng, Lei Liu, Yonglong Wang, Shu Wang, Ji-Qiang Wang, Tianying Yan, Xue-Ping Gao, De- Ying Song and Pan-Wen .. Journal of Fluorine Chemistry , Nature Communications volume 7, Article number: () | Download Citation . (d) Data sets cover a range of detector types, including Area Welberry, T. Diffuse X-Ray Scattering and Models of Disorder OUP Oxford () . . Chinese Academy of Sciences, Shanghai , China. Ming Lei.

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The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium. To determine whether the homodimerization interface of the CTD plays any role in viral replication, we generated a recombinant virus fe a NS1B protein with the RA mutation that inhibits CTD dimerization.

The publisher’s final edited version of this article is available at Structure. To determine the function of the NS1B CTD RNA-binding activity, re will be necessary to next identify the RNA species that bind to this domain in infected cells, followed by a determination of the mechanism s by which this RNA inhibits specific steps in virus replication. The data of Fig. Decision-making in structure solution using Bayesian estimates of map quality: The Phenix software for automated determination of macromolecular structures.

Fully alloyed metal nanorods with highly tunable properties Abrecht, W. B96DOI: The monomeric form of the 2040 CTD is sufficient to bind RNA Dimeric interactions observed in crystal structures may or may not occur in solution, particularly under dilute protein conditions. Author manuscript; available in PMC Sep 6. The key basic residues responsible for RNA-binding activity are 20004 in green in Figs.

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Details of 204 FP measurements are presented as Supplemental Information. Assays for the activation phosphorylation of IRF3 were carried out as described previously Kuo et al. Virus stocks were grown in day-old fertilized eggs. A novel RNA-binding motif in influenza A virus non-structural protein 1. Associated Data Supplementary Materials. Mutation of key basic residues in the RNA-binding surface on the Cterminal domain of full-length NS1B protein results in attenuated influenza B viruses The structural and biophysical results outlined above reveal a novel, unanticipated RNA binding function in the C-terminal domain fe the NS1 protein of influenza B viruses.

The structural and biophysical results outlined above reveal a novel, unanticipated RNA binding function in 01882 C-terminal domain of the NS1 protein of influenza B viruses. A threshold of 20 ppb 0. Characterization of Catalysts Mul G.

We also thank Drs. Electronic and bite angle effects in catalytic C—O bond cleavage of a lignin model compound using ruthenium Xantphos complexes Shaw L.

Residues are colored as follows: University of California; FP values were reported in millipolarization units mP. This result 20004 differences in the replication strategies of influenza A and B viruses. Find articles by Robert M.

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Panel d also shows an orientation rotated by deg, revealing no significant CSPs on the opposite side of the molecule. Our combined biophysical and virology studies of the CTD of the influenza B NS1B protein have led to an unexpected and novel finding regarding differences in the mechanisms of infection by A and B strains of influenza viruses. Rescue of influenza B virus from eight plasmids. Most importantly, this study reveals an unexpected RNA-binding function in the C-terminal domain of NS1B, a novel function oei distinguishes influenza B viruses from influenza A viruses.

Supplementary Material Click here to view. These biophysical studies demonstrate that the NS1B CTD has a weak propensity to form a homodimeric structure with the same interface observed in the X-ray crystal structure. Each measurement was made in triplicate.

X-ray structure of influenza virus NS1 effector domain.

Unexpected RNA-binding site in the NS1B Protein from Influenza B Virus not present in NS1A

Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that d to the journal pertain. As a service to our customers we are providing this early version of the manuscript. The virus genome and its replication. C, — DOI: Effects of the functionalization of the ordered mesoporous carbon support surface on iron catalysts for the Fischer—Tropsch synthesis of Lower Olefins Oschatz M.

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Unexpected RNA-binding site in the NS1B Protein from Influenza B Virus not present in NS1A

Sum rule distortions in fluorescence-yield x-ray magnetic circular dichroism Liu B. Influenza A virus strains that circulate in humans differ in dde ability of their NS1 proteins to block the activation of IRF3 and interferon-beta transcription. J Phys Chem B. A master regulator of host and viral functions.

Structure determination and refinement At the home X-ray source wavelength 1.

The host binding partners of the NS1B protein of influenza Se viruses are less well studied. Influenza A virus NS1 protein binds p85beta and activates phosphatidylinositolkinase signaling. Sharbini Harun Kamaluddin, F. From these measurements we conclude that homodimer formation of the NS1B CTD, while potentially important in cooperative binding to large RNA substrates in vivois not required for binding ve short RNA substrates. However, this dimer structure differs significantly in the relative orientations of protomers from those reported for the influenza A virus NS1A CTD Aramini et al.

Zeolite molecular accessibility and host—guest interactions studied by adsorption of organic probes of tunable size Hendriks F. For multiple cycle growth, A cells were infected with 0. SAD phasing using iodide ions in a high-throughput structural genomics environment. Infection by each of these influenza B viruses caused activation of IRF3 at early times 2—4 hours postinfectiontriggered directly by the incoming virus Makela et al.