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".
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Question: Paragraph: To extend the frontier of genome editing and enable the radical redesign of mammalian genomes, we developed a set of dead-Cas9 base editor (dBE) variants that allow editing at tens of thousands of loci per cell by overcoming the cell death associated with DNA double-strand breaks (DSBs) and single-strand breaks (SSBs). We used a set of gRNAs targeting repetitive elementsranging in target copy number from about 31 to 124,000 per cell. dBEs enabled survival after 5 large-scale base editing, allowing targeted mutations at up to ~13,200 and ~2610 loci in 293T and human induced pluripotent stem cells (hiPSCs), respectively, three orders of magnitude greater than previously recorded. These dBEs can overcome current on-target mutation and toxicity barriers that prevent cell survival after large-scale genome engineering. One Sentence Summary: Base editing with reduced DNA nicking allows for the simultaneous 10
Title: Enabling large-scale genome editing by reducing DNA nicking

Answer: True

Question: Paragraph: Since the refinement of tissue culture techniques for virus isolation and propagation from the mid 1960s onwards, veterinary virology has received much academic and industrial interest, and has now become a major global industry largely centred on vaccine development against economically important virus diseases of food animals. Bio-tech approaches have been widely used for improved vaccines development. While many viral diseases are controlled through vaccination, many still lack safe and efficacious vaccines. Additional challenges faced by academia, industry and governments are likely to come from viruses jumping species and also from the emergence of virulent variants of established viruses due to natural mutations. Also viral ecology is changing as the respective vectors adapt to new habitats as has been shown in the recent incursion by bluetongue virus into Europe. In this paper the current vaccines for livestock, horses and birds are described in a species by species order. The new promising bio-tech approaches using reverse genetics, non-replicating viral vectors, alpha virus vectors and genetic vaccines in conjunction with better adjuvants and better ways of vaccine delivery are discussed as well.
Title: Immunoprophylaxis against important virus diseases of horses, farm animals and birds

Answer: False

Question: Paragraph: We have previously reported that the 3C-like proteinase of the coronavirus infectious bronchitis virus (IBV) is responsible for processing of the 1a and 1a/1b polyproteins to three mature products of 24, 10, and 100 kDa (Liu et al., 1994 (Liu et al., , 1997 Ng and Liu, 1998) . The C-terminal cleavage site of the 100-kDa protein was defined to be the Q 891(1b) -S 892(1b) dipeptide bond encoded by nucleotides 15, 129 to 15, 134 (Liu and Brown, 1995). In this report, other cleavage sites of the 3C-like proteinase in the polyprotein encoded by the ORF 1b region were mapped by coexpression, deletion, and site-directed mutagenesis studies. Using two ORF 1b-specific antisera, V58 and V17, three more Q-S(G) dipeptide bonds, encoded by nucleotides 16,929 to 16,934, 18,492 to 18,497, and 19,506 to 19,511, respectively, were demonstrated to be the cleavage sites of the 3C-like proteinase. Cleavage at these four positions would result in the release of four mature products with molecular masses of approximately 68, 58, 39, and 35 kDa. Among them, the 39-and 35-kDa proteins were specifically identified in IBV-infected cells. Taken together with the 100-kDa protein previously identified, these results suggest that the ORF 1b region of IBV mRNA1 may be able to encode five mature products.
Title: Proteolytic Mapping of the Coronavirus Infectious Bronchitis Virus 1b Polyprotein: Evidence for the Presence of Four Cleavage Sites of the 3C-like Proteinase and Identification of Two Novel Cleavage Products

Answer:
False