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".

Paragraph: Human rhinovirus 3C protease (HRV 3C pro ) is known to be a promising target for development of therapeutic agents against the common cold because of the importance of the protease in viral replication as well as its expression in a large number of serotypes. To explore non-peptidic inhibitors of HRV 3C pro , a series of novel heteroaromatic esters was synthesized and evaluated for inhibitory activity against HRV 3C pro , to determine the structure-activity relationships. The most potent inhibitor, 7, with a 5-bromopyridinyl group, had an IC 50 value of 80 nM. In addition, the binding mode of a novel analog, 19, with the 4hydroxyquinolinone moiety, was explored by molecular docking, suggesting a new interaction in the S1 pocket. Ó 2009 Elsevier Ltd. All rights reserved. Picornaviruses include important human pathogens such as human rhinovirus (HRV), enterovirus (EV), coxsackievirus (CV), poliovirus (PV), and hepatitis A virus (HAV). HRVs are the single major cause of the common cold in populations of all ages. 1,2 Although rhinovirus infection is self-limiting, complications still occur in patients with asthma, congestive heart failure, bronchiectasis, and cystic fibrosis. 1 To date, no agent has been approved by the FDA for treatment of rhinovirus infection. In addition, the large number (>100) of known HRV serotypes makes vaccine development difficult. 3 Clinical treatments are directed toward relief of the most prominent symptoms of each clinical syndrome. Previous work on anti-rhinoviral therapeutic agents focused principally on capsid-binding anti-picornaviral compounds 4 and HRV 3C protease (3C pro ) inhibitors. 5, 6 HRV 3C pro is essential for virus replication, specifically catalyzing the cleavage of glutamine-glycine peptide bonds in a 230 kDa viral polyprotein produced by cellular translation of the viral RNA genome. HRV 3C pro belongs to the cysteine protease family, showing structural similarity to trypsin proteases, but sharing minimal homology with common mammalian enzymes. 7,8 Because of the importance of the enzyme in viral replication, and the high conservation of enzyme active site components in all known HRV serotypes, potent and selective HRV 3C pro inhibitors could be potential broad-spectrum anti-rhinoviral therapeutic agents. [9] [10] [11] As part of an effort to develop HRV 3C pro inhibitors, peptidomimetic approaches have been widely employed based on active site structure and cleavage specificity. To date, one peptidomimetic analog, rupintrivir (AG7088) (1), shown in Figure 1 , is the only HRV 3C Pro inhibitor that has advanced to the stage of human clinical trials. Phase II clinical trials of rupintrivir showed that intranasal delivery reduced the mean total daily symptom score by 33%. 12 Recently, several efforts to develop orally bioavailable anti-rhinoviral agents have been reported; these include a rupintrivir analog, 2, 13 with an improved pharmacokinetic profile, and the non-peptidic inhibitors 3 and 4. 14-16 The crystal structure of severe acute respiratory syndrome (SARS) coronavirus 3C-like protease (3CL pro ) 17 revealed a high similarity of active site architecture to that of HRV 3C pro , suggesting that picornavirus 3C pro and SARS 3CL pro inhibitors should cross-react. In fact, SARS 3CL pro inhibitors were developed by modifying rupintrivir 18 and common inhibitors with IC 50 values in the micromolar range were recently identified for both picornavirus 3C pro and coronavirus 3CL pro using high-throughput screening. 19,20 The pyridinyl thiophene ester 5 was discovered by screening a small molecule library (50,000 molecules) and has significant inhibitory activity against both HAV 3C pro and SARS 3CL pro (IC 50 = 0.5 lM). 19, 21 Further work on a series of heteroaromatic esters resulted in the discovery of the most potent ester 6, inhibiting SARS 3CL pro with an IC 50 of 30 nM and an antiviral activity (EC 50 value) of 6.9 lM. 22 Another analog, 7, also showed potent inhibition of HAV 3C pro with an IC 50 of 53 nM. 23 Studies on the inhibitory and molecular docking mechanisms of heteroaromatic esters have shown that the 5-halopyridine moiety is crucial in binding to the S1 pocket, because both 3C pro and 3CL pro show high specificity for Gln as the P1 residue. 23 0960-894X/$ -see front matter Ó 
 Title: Structure-activity relationships of heteroaromatic esters as human rhinovirus 3C protease inhibitors
True

Paragraph: The yeast two-hybrid (Y2H) system is a powerful method to identify and analyze binary protein interactions. In the fi eld of virology, the Y2H system has signifi cantly increased our knowledge of structure and function of viral proteins by systematically assessing intraviral protein interactions. Several comprehensive approaches to determine virus-host interactions have provided insight into viral strategies to manipulate the host for effi cient replication and to escape host-derived countermeasures. To expand our knowledge of intraviral and virus-host protein interactions, we here present a Y2H protocol that is well suited for high-throughput screening. Yeast mating followed by liquid handling in a 96-well format as well as fl uorescent readout of the reporter system provides a highly standardized and fully automated screening situation. The protocol can either be applied to screen complex host cDNA libraries or protein pairs arrayed for cross-testing. The ease of use, the cost-effectiveness as well as the robotic handling allows for extensive and multiple rounds of screening providing high coverage of protein-protein interactions. Thus, this protocol represents an improved "deep" screening method for high-throughput Y2H assays. 
 Title: Chapter 1 A High-Throughput Yeast Two-Hybrid Protocol to Determine Virus-Host Protein Interactions
True

Paragraph: Twenty TGEV isolates were compared by sequencing a 393±414 nucleotide stretch near the 5 H end of the S gene, after ampli®cation by RT-PCR. This part of the S gene is known to show considerable variation between porcine, canine and feline coronaviruses and is completely deleted from porcine respiratory coronaviruses. The discrimination achieved by nucleotide sequence analysis was compared with that obtained by monoclonal antibody typing. The viruses could be split into several clusters, and recent isolates of TGEV from England, The Netherlands and Belgium showed the greatest differences compared to earlier reference types. However, not all viruses with unique isolation histories were distinct, suggesting either genetic stability over many years, laboratory cross-contaminations or repeated introductions of similar viruses into the ®eld. Firm conclusions on evolutionary trends cannot be drawn without obtaining a larger number of isolates, preferably from outbreaks with known epidemiological links. The sequences of some ®eld isolates from the 1980s contained both nucleotide deletions and insertions. The latter included a short sequence of fourteen nucleotides with identity to a region of the TGEV polymerase gene. Transmissible gastroenteritis (TGE) is a highly contagious pig disease that may cause serious losses, especially in unweaned piglets [17] . The causative virus, TGEV, is a member of the Coronaviridae, and has a large, single-stranded, positive sense RNA genome. The virion is enveloped, and covered in projections caused by a glycosylated spike protein (S), of approximately 200 kDa. The S protein is a major target for antibodies, and monoclonal antibodies (mAbs) have helped to de®ne four principal antigenic sites, one of which 
 Title: Discrimination between transmissible gastroenteritis virus isolates Brief Report

False