In this task, you're given a paragraph from the research paper and your task is to generate a suitable title for the research paper based on the given paper. Under 100 words is a good title length.

Example Input: SARS-CoV-2, a member of the coronavirus family, is responsible for the current COVID-19 pandemic. Based on our analysis of hepatitis C virus and coronavirus replication, and the molecular structures and activities of viral inhibitors, we previously demonstrated that three nucleotide analogues inhibit the SARS-CoV RNA-dependent RNA polymerase (RdRp). Here, using polymerase extension experiments, we have demonstrated that the active triphosphate form of Sofosbuvir (a key component of the FDA approved hepatitis C drug EPCLUSA), is incorporated by SARS-CoV-2 RdRp, and blocks further incorporation. Using the same molecular insight, we selected the active triphosphate forms of three other anti-viral agents, Alovudine, AZT (an FDA approved HIV/AIDS drug) and Tenofovir alafenamide (TAF, an FDA approved drug for HIV and hepatitis B) for evaluation as inhibitors of SARS-CoV-2 RdRp. We demonstrated the ability of these three viral polymerase inhibitors, 3'-fluoro-3'-deoxythymidine triphosphate, 3'-azido-3'deoxythymidine triphosphate and Tenofovir diphosphate (the active triphosphate forms of Alovudine, AZT and TAF, respectively) to be incorporated by SARS-CoV-2 RdRp, where they also terminate further polymerase extension. These results offer a strong molecular basis for these nucleotide analogues to be evaluated as potential therapeutics for COVID-19.
Example Output: Nucleotide Analogues as Inhibitors of SARS-CoV-2 Polymerase

Example Input: IFITM3 restricts cellular infection by multiple important viral pathogens, and is particularly critical for the innate immune response against influenza virus. Expression of IFITM3 expands acidic endolysosomal compartments and prevents fusion of endocytosed viruses, leading to their degradation. This small, 133 amino acid, antiviral protein is controlled by at least four distinct post-translational modifications. Positive regulation of IFITM3 antiviral activity is provided by Spalmitoylation, while negative regulatory mechanisms include lysine ubiquitination, lysine methylation and tyrosine phosphorylation. Herein, we describe specific insights into IFITM3 trafficking and activity that were provided by studies of IFITM3 post-translational modifications, and discuss evidence suggesting that IFITM3 adopts multiple membrane topologies involving at least one intramembrane domain in its antivirally active conformation.
Example Output: Regulation of the trafficking and antiviral activity of IFITM3 by post-translational modifications

Example Input: Two fractions of herpes simplex virus glycoprotein gC were isolated and characterized by means of immunosorbent-purification with monoelonal antibodies against gC and Helix pomatia leetin (HPA) affinity chromatography. About 25 per cent of the glyeoprotein gC population demonstrated affinity for the lectin, compatible with presence of N-acetylgalactosamine as terminal sugar of the oligosaccharide. The HPA-binding populations of gC appeared as two electrophoretic bands with lower molecular weights than the non-binding gC. The gC subfraction without affinity for the HPA was subjected to treatments aiming to desialylize the carbohydrate moiety. Only 5 per cent of the initially non-reactive fraction of gC became reactive to HPA after the treatments, suggesting that masking of penultimate N-acetylgalactosamine by sialic acid was not a main reason for lack of HPA affinity. Results of treatment with alkaline Na BH4 demonstrated presence of oligosaccharide-peptidc linkages sensitive to ~-elimination suggesting O-glycosidic type of linkage. The subfraetion of gC demonstrating affinity for HPA as well as gC devoid of HPA binding capacity both revealed affinity for Con A, Therefore N-glycosidically as well as O-glycosidically linked oligosaceharides seemed to be present on the one and same glycoprotein. On the basis of the results presented we assume that the glycosylation of HSV glyeoprotein gC may lead to, at least, two populations of the gtyeoprotein gC, one with terminal N-acetylgalactosamine residues of oligosaccharides 0-glycosidically tinked to the polypeptide and the other without affinity-for HPA. However, both populations of gC contain similar proportions of oligosaccharides of the high 0304-8608/83/0076/0025/$ 02.80 S. OLOFSSO~ et al. : mannose or complex types with N-glycosidic carbohydrate-peptide linkages as indicated by their affinity for Con A.
Example Output:
Archives of Virology Populations of Herpes Simplex Virus Glyeoprotein tiC with and without Mfinity for the N-Aeetyl-Galaetosamine Specific Leetin ot Helix pomatia