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".

Input: Consider Input: Paragraph: The phosphoprotein (P) gene of most Paramyxovirinae encodes several proteins in overlapping frames: P and V, which share a common N-terminus (PNT), and C, which overlaps PNT. Overlapping genes are of particular interest because they encode proteins originated de novo, some of which have unknown structural folds, challenging the notion that nature utilizes only a limited, well-mapped area of fold space. The C proteins cluster in three groups, comprising measles, Nipah, and Sendai virus. We predicted that all C proteins have a similar organization: a variable, disordered N-terminus and a conserved, a-helical Cterminus. We confirmed this predicted organization by biophysically characterizing recombinant C proteins from Tupaia paramyxovirus (measles group) and human parainfluenza virus 1 (Sendai group). We also found that the C of the measles and Nipah groups have statistically significant sequence similarity, indicating a common origin. Although the C of the Sendai group lack sequence similarity with them, we speculate that they also have a common origin, given their similar genomic location and structural organization. Since C is dispensable for viral replication, unlike PNT, we hypothesize that C may have originated de novo by overprinting PNT in the ancestor of Paramyxovirinae. Intriguingly, in measles virus and Nipah virus, PNT encodes STAT1-binding sites that overlap different regions of the C-terminus of C, indicating they have probably originated independently. This arrangement, in which the same genetic region encodes simultaneously a crucial functional motif (a STAT1-binding site) and a highly constrained region (the C-terminus of C), seems paradoxical, since it should severely reduce the ability of the virus to adapt. The fact that it originated twice suggests that it must be balanced by an evolutionary advantage, perhaps from reducing the size of the genetic region vulnerable to mutations. Citation: Lo MK, Søgaard TM, Karlin DG (2014) Evolution and Structural Organization of the C Proteins of Paramyxovirinae. PLoS ONE 9(2): e90003. 
 Title: Evolution and Structural Organization of the C Proteins of Paramyxovirinae

Output: False


Input: Consider Input: Paragraph: Research on respiratory protection against biologic agents is important to address major concerns such as occupational safety and terrorist attack. This review describes the literature on respiratory protection against bioaerosols and identifies research gaps. Respiratory protection is a complex field involving a number of factors, such as the efficiency of respirator filter material; facepiece fitting; and maintenance, storage, and reuse of respirators. Several studies used nonpathogenic microorganisms having physical characteristics similar to that of Mycobacterium tuberculosis to analyze microbial penetration through respirators. Some studies showed that high-efficiency particulate air (HEPA) and N95 filters provided a higher level of protection than dust/mist (DM) and dust/mist/fume (DMF) filters. Flow rate and relative humidity appear to alter the level of penetration of microorganisms through respirator filters. The relationship between microbial penetration through respirator filters and the aerodynamic diameter, length, or other physical characteristics of microorganisms remains controversial. Whether reaerosolization of bioaerosol particles should be a concern is unclear, given the fact that one study has demonstrated significant reaerosolization of 1-to 5-mm particles loaded onto respirator filters. Respirator maintenance, storage, and decontamination are important factors to be considered when reusing respirators. The respiratory protection against biologic warfare agents such as anthrax in military and civilian situations is described. (Am J Infect Control 2004;32:345-54.)  
 Title: Respiratory protection against bioaerosols: Literature review and research needs

Output: False


Input: Consider Input: Paragraph: SJG), and John.Skehel@crick.ac.uk (JJS) SUPPLEMENTAL EXPERIMENTAL PROCEDURES: Monoclonal antibody isolation was perfomed as previously described (Pappas et al., 2014; Traggiai et al., 2004) . In brief, peripheral blood mononuclear cell (PBMC) samples were obtained from a single healthy donor after vaccination following written consent. Memory B cells were isolated from cryopreserved or fresh PBMCs using CD22 microbeads or anti-FITC (fluorescein isothiocyanate) microbeads (Miltenyi Biotec) after staining of PBMCs with CD22-FITC, and were immortalized with Epstein-Barr virus (EBV) and CpG in multiple wells. Supernatants of immortalized B cell clones containing monoclonal antibodies were screened for binding to HA proteins representing two different HA subtypes. Using this methodology, we identified a monoclonal from primary screening in ELISA assay that showed crossreactive binding to recombinant HA proteins of A/Vietnam/2005 H5N1 and A/ Netherlands/2003 H7N7. Variable gene sequences were isolated from this cross-reactive clone by RT-PCR, cloned and expressed as a full-length IgG transiently in 293 T cells. The lead FY1 antibody was further modified to revert the non-germline framework amino acid changes and affinity optimize the CDRs. For the affinity optimization, full-length IgG constructs containing the different variants created by CDR based parsimonious mutagenesis were expressed transiently in 293 T cells and supernatants were screened by ELISA to select clones that resulted in increased binding activity to H3 while maintaining or increasing the binding activity to H1 HA proteins. Coating concentrations of 0.15 µg/ml of rabbit anti-human IgG were used to capture and normalize variant IgG constructs from supernatants, and binding was probed using 0.5 µg/ml of biotinylated HA proteins A/Perth/2009 H3N2 and A/California/7/2009 H1N1 followed by the addition of streptavidin-HRP (1:5000). Beneficial single mutations were combined and cloned into a combinatorial library, which were expressed and screened by ELISA as described above, leading to the generation of MEDI8852. The DNA Maximum Likelihood program (Dnaml) of the PHYLIP package, version 3.69, was used to estimate immunoglobulin phylogenies from nucleotide sequences that were first aligned using ClustalW2, as previously described12. IgHCDR3 regions were defined with their Kabat numbering using the software available on the Abnum website (http://www.bioinf.org.uk/abs/abnum/). The V, D and J genes of the IgH DNA sequences were identified using the IMGT database as a reference (Brochet et al., 2008; Ye et al., 2013) . The UCA sequences were inferred with Antigen Receptor Probabilistic Parser (ARPP) UA Inference software (Kepler, 2013) , and produced by gene synthesis (Genscript). Branchpoint antibodies were determined by the antibody phylogenetic tree derived by dnaml, and produced by gene synthesis (Genscript). Recombinant HA proteins were expressed and purified as previously described (Benjamin et al., 2014) ELISA binding assays were performed using 384 well plates (Maxisorp, Nunc) with 0.5 µg/ml of purified HA protein as described in Table S2 . ELISA plates were washed, blocked 1% (w/v) casein (Thermo Scientific), and serially diluted antibodies were incubated for 1 hr at room temperature. Bound antibodies were detected using a peroxidase-conjugated mouse anti-human IgG antibody (KPL 1:10,000), followed by development with TMB solution (KPL). The absorbance at 450nm was measured, and EC 50 values were calculated using a non-linear regression of log (inhibitor) vs response in Graph Pad Prism. Cell surface expressed protein binding assays were conducted using flow cytometry to detect binding of antibodies to HA transfected cells. HEK 293 cells were transiently transfected with full-length wild type HA expressing plasmids. Forty-eight hours after transfection, cells were detached with trypsin, and incubated with 5 µg/ml of FY1 or MEDI8852 on ice for 1 hour. Antibody remaining bound to surface expressed HA protein after washing was then stained with a goat anti-human IgG Daylight 649 (Jackson ImmunoResearch), and detected by flow cytometry. 
 Title: Supplemental Information Structure and Function Analysis of an Antibody Recognizing All Influenza A Subtypes


Output: True