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: Although Middle East respiratory syndrome coronavirus (MERS-CoV) has a recorded 5 years of circulation in 27 countries worldwide, there is no international study to assess whether there is variation in mortality by region. Neither has there been a comprehensive study detailing how the disease characteristics of MERS-CoV influence mortality in patients presenting symptoms. This study aimed to assess how region, patient and disease characteristics influence 14-and 45-day mortality in MERS patients. The author utilised publically available data on MERS-CoV. The study included 883 MERS patients reported between 5 January 2015 and 10 March 2017. Data on patient and disease characteristics were collected. The mean age at MERS-CoV diagnosis was 54.3 years: 69.1% were male, and 86.7% of the cases were reported from Saudi Arabia. About 40% of MERS patients studied were over the age of 60. The study estimated 14-and 45-day survival rates after initial onset of symptoms: 83.67% and 65.9%, respectively. Saudi Arabian MERS patients exhibited 4.1 and 5.0 times higher 14-day (adjusted hazard risk (aHR) = 4.1; 95% confidence interval (CI) 1.012-16.921) and 45-day (aHR = 5.0; 95% CI 1.856-13.581) mortality risk compared with MERS patients in the Republic of Korea or other countries. Similarly, Middle Eastern MERS patients showed 5.3 and 4.1 times higher 14-day (aHR = 5.3; 95% CI 1.070-25.902) and 45-day (aHR = 4.1; 95% CI 1.288-113.076) mortality risk compared with MERS patients in the Republic of Korea or other countries. The results demonstrated a link between mortality and geography, disease and patient factors such as regions, symptoms, source of infections, underlying medical conditions, modes of transmission, non-healthcare workers and those of older age. Educational programmes, access to healthcare and early diagnosis could be implemented as modifiable factors to reduce the higher mortality rates in MERS patients. 
 Title: Epidemiology and Infection Estimating survival rates in MERS-CoV patients 14 and 45 days after experiencing symptoms and determining the differences in survival rates by demographic data, disease characteristics and regions: a worldwide study
[EX A]: False

[EX Q]: Paragraph: This study contributes to the fields of hospitality and tourism by examining interactions between business conditions and financial performance of tourism firms in both China and Taiwan. We investigate whether the improvement of business conditions enhances financial performance of tourism firms and whether financial success of tourism firms matters to business development. In general, cointegration test results support a long-run equilibrium relationship between the two variables, business conditions and financial performance of tourism firms, and Granger causality test results show that these two factors reinforce each other in both China and Taiwan. This study therefore documents significant contributions of financial success of tourism firms to business development and strengthening of financial performance of tourism firms by business conditions. Some managerial implications are also discussed. r 
 Title: Interactions between business conditions and financial performance of tourism firms: Evidence from China and Taiwan
[EX A]: False

[EX Q]: Paragraph: Chikungunya virus (CHIKV), genus Alphavirus, family Togaviridae, has a positive-stand RNA genome approximately 12 kb in length. In infected cells, the genome is translated into non-structural polyprotein P1234, an inactive precursor of the viral replicase, which is activated by cleavages carried out by the non-structural protease, nsP2. We have characterized CHIKV nsP2 using both cell-free and cell-based assays. First, we show that Cys478 residue in the active site of CHIKV nsP2 is indispensable for P1234 processing. Second, the substrate requirements of CHIKV nsP2 are quite similar to those of nsP2 of related Semliki Forest virus (SFV). Third, substitution of Ser482 residue, recently reported to contribute to the protease activity of nsP2, with Ala has almost no negative effect on the protease activity of CHIKV nsP2. Fourth, Cys478 to Ala as well as Trp479 to Ala mutations in nsP2 completely abolished RNA replication in CHIKV and SFV trans-replication systems. In contrast, trans-replicases with Ser482 to Ala mutation were similar to wild type counterparts. Fifth, Cys478 to Ala as well as Trp479 to Ala mutations in nsP2 abolished the rescue of infectious virus from CHIKV RNA transcripts while Ser482 to Ala mutation had no effect. Thus, CHIKV nsP2 is a cysteine protease. Chikungunya virus (CHIKV) belongs to genus Alphavirus (family Togaviridae). It is transmitted by Aedes mosquitoes and has caused several massive outbreaks since 2004 1 . CHIKV has a positive-strand RNA genome approximately 12 kb in length. A large 5′ open reading frame (ORF), which covers 2/3 of the viral genome, is translated directly from the viral genomic RNA and encodes for a non-structural (ns) polyprotein designated as P1234. The second ORF encodes for the precursors of viral structural proteins and is translated from a specific subgenomic RNA synthesized in virus-infected cells 2 . All virus-specific enzymatic activities, required for viral RNA synthesis, are present in P1234 and its cleavage products 3 . Allthough uncleaved P1234 possesses several enzymatic activities 4 , it is incapable of performing viral RNA replication at detectable levels 5 . To become active, P1234 must first be processed into the early replicase (P123 polyprotein + nsP4). This complex can, in principle, perform all the essential steps of viral RNA synthesis 6 . However, during alphavirus infection the early replicase is converted into the mature (nsP1 + nsP2 + nsP3 + nsP4) form 7 . All these cleavages are performed by a protease located at the C-terminus of nsP2 8-10 and the processing of P1234 is regulated at multiple levels [11] [12] [13] [14] . The protease part of nsP2 can be easily purified as an active recombinant protein 10,15 . In addition, the protease activity of nsP2 can be studied using in vitro translation and cell culture models 9,16 . Early studies showed that alphavirus nsP2 is similar to papaine-like proteases. The catalytic dyad of Sindbis virus (SINV) nsP2 is represented by Cys481 and His558 residues 8,17,18 ; these correspond to Cys478 and His548 in CHIKV and Semliki Forest virus (SFV) nsP2. Mutation of these residues results in the complete loss of protease activity 19 and abolishes the infectivity of SINV genomes 18 . Different cleavage sites in P1234 are recognized in different ways. Specifically, SFV nsP2 cannot cleave short substrates representing the cleavage site between nsP2 and nsP3 (2/3 site). This cleavage requires both the native N-terminus of nsP2 and a long substrate comprising a few P-side residues followed by approximately 165 N-terminal residues of nsP3 12,15 . The 3D structures of the proteases from Venezuelan equine encephalitis virus (VEEV) 20 , SINV 21 and CHIKV (Protein Data Bank code 3TRK) reveal that nsP2 protease is a member of MEROPS Clan CN and contains a papain-like protease linked to a C-terminal domain resembling FtsJ-like methyltransferases (MTL domain) 20 . Subsequent molecular modelling revealed the features of the catalytic site and the S1′ -S4 subsites 22 . A peptidomimetic inhibitor of nsP2 protease binds at the interface of the protease and MTL domains resulting in conformational change that most probably assists in leaving group departure of either the amine or Cys thiolate during the catalytic cycle 23 ; the binding mode of natural substrates is most likely similar. In addition to the catalytic Cys, Asn475 and Lys480 residues (correspond to residues 476 and 481 of CHIKV nsP2) have been shown to be important for the protease activity of VEEV nsP2 23 . Known 3D structure coupled with the functional importance of nsP2 have made this protein an attractive target for the development of inhibitors of alphavirus infection [23] [24] [25] [26] [27] [28] . CHIKV nsP2 possesses all the enzymatic activities known for nsP2 derived from other alphaviruses 29,30 . However, data concerning the protease activity of CHIKV nsP2 is conflicting. On one hand, studies performed using the purified protease part of nsP2 31 or full length nsP2 with a native N-terminus 16 have demonstrated that CHIKV nsP2 is functionally similar to SFV nsP2. On the other hand, Saisawang and co-authors observed that CHIKV nsP2, derived from East/Central/South African (ECSA) isolate from Thailand, differs from other alphavirus nsP2 proteases in the recognition of small peptide substrates 32 . Recently the same team also reported that the catalytic dyad Cys478 of CHIKV nsP2 could be interchangeable with a proximal Ser482 residue that also contributes to the protease activity of nsP2 33 . Thus, CHIKV nsP2 was reported to have properties very different from those revealed for the ns proteases of other alphaviruses. Indeed, functions of the same ns protein originating from different alphaviruses can be substantially different 34, 35 . However, in this case the data was obtained using only a single short peptide substrate based assay and the conclusion was not directly confirmed by comparing the enzymes from different alphaviruses in the same experiment. Furthermore, this finding has not been verified using cell-based experiments. As unusual properties of CHIKV nsP2 would have implications for the molecular biology of this virus as well as for the development of inhibitors of CHIKV infection, we evaluated the properties of CHIKV nsP2 using multiple verified cell-free and cell-based assays. This analysis revealed that Cys478 residue is indispensable for CHIKV ns polyprotein processing, RNA replication and viral infectivity. Substitution of Ser482 residue did not affect any of these crucial functions. Thus, it must be asserted that CHIKV nsP2 is a classical alphavirus ns protease with properties very similar to those previously revealed for SFV nsP2. 
 Title: Chikungunya virus infectivity, RNA replication and non-structural polyprotein processing depend on the nsP2 protease's active site cysteine residue OPEN
[EX A]:
False