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".

[EX Q]: 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
[EX A]: True

[EX Q]: Paragraph: Background: Infrared thermography (IRT) is used to screen febrile passengers at international airports, but it suffers from low sensitivity. This study explored the application of a combined visible and thermal image processing approach that uses a CMOS camera equipped with IRT to remotely sense multiple vital signs and screen patients with suspected infectious diseases. Methods: An IRT system that produced visible and thermal images was used for image acquisition. The subjects' respiration rates were measured by monitoring temperature changes around the nasal areas on thermal images; facial skin temperatures were measured simultaneously. Facial blood circulation causes tiny color changes in visible facial images that enable the determination of the heart rate. A logistic regression discriminant function predicted the likelihood of infection within 10 s, based on the measured vital signs. Sixteen patients with an influenza-like illness and 22 control subjects participated in a clinical test at a clinic in Fukushima, Japan. Results: The vital-sign-based IRT screening system had a sensitivity of 87.5% and a negative predictive value of 91.7%; these values are higher than those of conventional fever-based screening approaches. Conclusions: Multiple vital-sign-based screening efficiently detected patients with suspected infectious diseases. It offers a promising alternative to conventional fever-based screening. 
 Title: Remote sensing of multiple vital signs using a CMOS camera-equipped infrared thermography system and its clinical application in rapidly screening patients with suspected infectious diseases
[EX A]: True

[EX Q]: Paragraph: A new coronavirus (CoV) identified as COVID-19 virus is the etiological agent responsible 31 for the 2019-2020 viral pneumonia outbreak that commenced in Wuhan 1-4 . Currently there 32 is no targeted therapeutics and effective treatment options remain very limited. In order to 33 rapidly discover lead compounds for clinical use, we initiated a program of combined 34 structure-assisted drug design, virtual drug screening and high-throughput screening to 35 identify new drug leads that target the COVID-19 virus main protease (M pro ). M pro is a key 36 CoV enzyme, which plays a pivotal role in mediating viral replication and transcription, 37 making it an attractive drug target for this virus 5,6 . Here, we identified a mechanism-based 38 inhibitor, N3, by computer-aided drug design and subsequently determined the crystal 39 structure of COVID-19 virus M pro in complex with this compound. Next, through a 40 combination of structure-based virtual and high-throughput screening, we assayed over 41 10,000 compounds including approved drugs, drug candidates in clinical trials, and other 42 pharmacologically active compounds as inhibitors of M pro . Six of these inhibit M pro with 43 IC50 values ranging from 0.67 to 21.4 μM. Ebselen also exhibited promising antiviral 44 activity in cell-based assays. Our results demonstrate the efficacy of this screening strategy, 45 which can lead to the rapid discovery of drug leads with clinical potential in response to 46 new infectious diseases where no specific drugs or vaccines are available. 47 48 author/funder. All rights reserved. No reuse allowed without permission. : bioRxiv preprint CoVs infect humans and other animal species, causing a variety of highly prevalent and 49 severe diseases, including Severe Acute Respiratory Syndrome (SARS) and Middle East 50 Respiratory Syndrome (MERS) 7 . The COVID-19 virus genome is comprised of ~30,000 51 nucleotides; its replicase gene encodes two overlapping polyproteins, pp1a and pp1ab, 52 required for viral replication and transcription 3,4 . The functional polypeptides are released 53 from the polyproteins by extensive proteolytic processing, predominantly by a 33.8-kDa 54 main protease (M pro ), also referred to as the 3C-like protease. M pro digests the polyprotein 55 at no less than 11 conserved sites, starting with the autolytic cleavage of this enzyme itself 56 from pp1a and pp1ab 8 . The functional importance of M pro in the viral life cycle, together 57 with the absence of closely related homologues in humans, identify the M pro as an attractive 58 target for antiviral drug design 9 . 59 To facilitate the rapid discovery of antiviral compounds with clinical potential, we 60 developed a strategy combining structure-assisted drug design, virtual drug screening and 61 high-throughput screening to repurpose existing drugs to target COVID-19 virus M pro . 62 Establishing a high-throughput activity assay 63 Recombinant COVID-19 virus M pro with native N and C termini was expressed in 64 Escherichia coli and subsequently purified (Extended Data Fig. 1a, b). The molecular 65 weight of COVID-19 virus M pro as determined by mass spectroscopy is 33797.0 Da, 66 consistent with its theoretical molecular weight 33796.8 Da. In order to characterize its 67 enzymatic activity and to carry out high-throughput screening of inhibitors, we developed 68 a fluorescence resonance energy transfer (FRET) assay. To do this, a fluorescently labeled 69 substrate, MCA-AVLQ↓SGFR-Lys(Dnp)-Lys-NH2, derived from the N-terminal auto-70 cleavage sequence of the viral protease was designed and synthesized for time-dependent 
 Title: Structure of M pro from COVID-19 virus and discovery of its inhibitors
[EX A]:
True