In this task, you're given a paragraph and title from the research paper. Your task is to classify whether the given title is suitable or not for the research paper based on the given paragraph. Return "True" if title is proper according to paragraph else "False".

[Q]: Paragraph: Infectious bronchitis (IB) is a highly contagious upper respiratory tract disease of chickens caused by infectious bronchitis virus (IBV), which has various serotypes that do not cross-protect. Vaccine control strategies for this virus are only effective when designed around the currently circulating serotypes. It is essential to not only rapidly detect IBV but also to identify the type of virus causing disease. Six TaqMan™️-based quantitative realtime RT-PCR assays (Universal, Ark, Mass, DE/GA98, GA07, GA08) were developed and examined the sensitivity and specificity for each assay. Assays were developed targeting the hypervariable region in the S1 gene subunit. The analytical sensitivity of TaqMan™️-based quantitative real-time RT-PCR assays (qRT-PCR) assays was evaluated using synthetic DNA standards that were identical with the target sequence and specificity was further validated using clinical and biological specimens. All developed assays performed equivalently when using synthetic DNA templates as standard material, as it achieved linearity over a 5 log 10 dynamic range with a reproducible limit of detection of 10 target copies per reaction, with high calculated amplification efficiencies ranging between 90%-115%. Further validation of specificity using clinical and biological specimens was also successful.
Title: Validation of specific quantitative real-time RT-PCR assay panel for Infectious Bronchitis using synthetic DNA standards and clinical specimens
[A]: True

[Q]: Paragraph: Norovirus infection constitutes the primary cause of acute viral gastroenteritis. There are currently no vaccines or norovirus-specific antiviral therapeutics available for the management of norovirus infection. Norovirus 3C-like protease is essential for viral replication, consequently, inhibition of this enzyme is a fruitful avenue of investigation that may lead to the emergence of anti-norovirus therapeutics. We describe herein the optimization of dipeptidyl inhibitors of norovirus 3C-like protease using iterative SAR, X-ray crystallographic, and enzyme and cell-based studies. We also demonstrate herein in vivo efficacy of an inhibitor using the murine model of norovirus infection. . Accession Codes. The coordinates and structure factors for norovirus 3CL protease in complex with inhibitors have been deposited to the Protein Databank with the accession codes NVpro:17 (4XBB), NVPro:44-h (4XBC) and NVPro:44-o (4XBD). We initially focused on the design of peptidyl transition state inhibitors of NV 3CLpro that incorporate in their structure a recognition element (a peptidyl fragment) that is congruent with the known substrate specificity of the enzyme (vide supra) and a warhead (aldehyde or -ketoamide), latent warhead (bisulfite adduct) or transition state mimic (- Kankanamalage et al. The synthesized compounds were evaluated for their inhibitory activity against NV 3CLpro, as well as their anti-norovirus activity in a cell-based replicon system, as previously Kankanamalage et al. In order to evaluate the specific interactions between the enzyme and the hydroxyphosphonate inhibitors, inhibitor 17 was incubated with NV 3CLpro in Tris buffer, pH 8.0. Surprisingly, the enzyme-inhibitor complex formed corresponded to the complex formed between aldehyde 16 and 3CL protease. The formation of this complex indicates initial non-enzymatic (buffer)-or enzyme-catalyzed conversion of -hydroxyphosphonate 17 to the corresponding aldehyde 16, followed by the formation of a tetrahedral adduct with the active site cysteine (Cys139). Studies aimed at ascertaining the validity of this hypothesis are in progress. The ensemble of hydrogen bonding and hydrophobic interactions Kankanamalage et al.
Title: Structure-Guided Design and Optimization of Dipeptidyl Inhibitors of Norovirus 3CL Protease. Structure-Activity Relationships and Biochemical, X-ray Crystallographic, Cell- Based, and In Vivo Studies
[A]: False

[Q]: Paragraph: Avipoxviruses are divided into three clades: canarypox-like viruses, fowlpox-like viruses, and psittacinepox-like viruses. Several molecular clock and demographic models available in the BEAST package were compared on three avipoxvirus genes (P4b, cnpv186 and DNA polymerase genes), which enabled to determine that avipoxviruses evolved at a rate of 2-8 A 10 A5 substitution/site/year, in the range of poxviruses previously reported evolution rates. In addition, the date of mean time of divergence of avipoxviruses from a common ancestor was extrapolated to be about 10,000-30,000 years ago, at the same period as modern poxvirus species. Our findings will facilitate epidemiological investigations on avipoxviruses' spread, origin and circulation.
Title: Time scale evolution of avipoxviruses-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/)
[A]:
True