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Static light scattering analysis of purified wild-type NP and variants.

<p>Horizontal lines on top of the curves illustrate the calculated molecular weights.</p

The viral RNP activity of wild-type BNP and variants.

<p>Viral RNP activity of wild-type and BNP N-terminal deletion variants. For each mutants triplicate wells were set and recorded. Experiments are repeated twice. P values are calculated by T-test algorithm. *, <i>P</i> < 0.01; <i>**</i>, <i>P</i> < 0.001.</p

The oligomeric states of wild-type BNP, BNP-Δ38 and BNP-Δ66 examined by election microscopy.

<p>Electron microscopy pictures of NP and its variants. <i>a)</i> wild-type BNP (<i>a1</i>), BNP-Δ38 (<i>a2)</i> and BNP-Δ66 (<i>a3</i>) in 100 mM sodium phosphate, 100 mM NaCl, pH6.8. b) Wild-type BNP (<i>b1</i>), BNP-Δ38 (<i>b2)</i> and BNP-Δ66 (<i>b3</i>) in PBS when RNA was added at 0h. c) Wild-type BNP (<i>c1</i>), BNP-Δ38 (<i>c2)</i> and BNP-Δ66 (<i>c3</i>) in PBS 16hr after RNA was added. The red arrow in the <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0137802#pone.0137802.g003" target="_blank">Fig 3B</a>-c1 indicates the RNA-BNP complexes that displays a double layered structure.</p

Wild-type BNP and BNP-Δ66 have comparable RNA binding activities.

<p>Indicated amount of purified BNP and BNP-Δ66 were incubated with 10 μM of 24 nt 2-O-methylated RNA and analyzed by agarose gel electrophoresis. Band intensities were calculated by ImageJ (National Institutes of Health)[<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0137802#pone.0137802.ref019" target="_blank">19</a>], using the RNA without the protein as a control (100%).</p

The construction and growth curves of influenza B virus with BNP variants.

<p>(A) Construction of influenza B NP mutants by systematically deleting the N-terminal coding region of NP. (B) Growth curves of influenza B wild-type and NP N-terminal deletion mutants after virus rescue. The growth curves are averages from three independent replicates.</p

Additional file 2: of Sheng Jiang San, a traditional multi-herb formulation, exerts anti-influenza effects in vitro and in vivo via neuraminidase inhibition and immune regulation

Figure S1. HPLC analysis of SJS (a) HPLC profile of SJS (b) Some constituents were denoted by standard compounds. (PPTX 128 kb

Additional file 1: of Sheng Jiang San, a traditional multi-herb formulation, exerts anti-influenza effects in vitro and in vivo via neuraminidase inhibition and immune regulation

Method of High-performance liquid chromatography (HPLC) analysis of SJS. HPLC method was used to analyze the chemical profile of SJS. The HPLC condition is described in this additional file and the profile is shown in Additional file 2: Figure S1. By comparing with reference compounds, rhein, chrysophanol, emodin, aloe emodin and curcumin were found. (DOCX 13 kb

Lys158–Lys161 on MOD are responsible for the interaction between maize RIP and P2.

<p><b>A) MOD does not bind to P2 when Lys158–Lys161 are mutated to alanine.</b> SDS-PAGE of the last wash (W) and elution (E) obtained from the pull-down assay of maize RIP and P2. Input indicates the purified proteins loaded to the column. <b>B) Sensorgram showing MOD but not pro-RIP and MOD [K158A-K161A] interact with sensor chip-immobilized P2.</b> 500 nM of maize RIP variants or running buffer were injected to the sensor chip for three minutes for association, followed by a dissociation using running buffer. Response unit (RU) was monitored in a real-time manner.</p

Interaction between RIPs and P2.

<p><b>A) Interaction of MOD, TCS and StxA with P2 at different ionic strengths.</b> Pull-down assay was conducted on RIPs under various ionic strengths to compare their strength of interaction with P2. Input indicates the same amount of purified RIPs was loaded to the P2-sepharose column and proteins were eluted using buffer with 1M NaCl. <b>B) Interactions between RIPs and C-terminal truncated P2.</b> C-terminal truncated P2 variants were subject to pull down assay with RIPs. The C-terminal amino acid sequences of P2, P2 [ΔC5] and P2 [ΔC10] are: AEEKKDEKKEESEE<b>SDDDMGFGLFD</b>, AEEKKDEKKEESEE<b>SDDDMG</b> and AEEKKDEKKEESEE<b>S</b> respectively. The bold letters refer to the conserved residues in P-proteins.</p