instruction:
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.
question:
Viroporins are small, hydrophobic trans-membrane viral proteins that oligomerize to form hydrophilic pores in the host cell membranes. These proteins are crucial for the pathogenicity and replication of viruses as they aid in various stages of the viral life cycle, from genome uncoating to viral release. In addition, the ion channel activity of viroporin causes disruption in the cellular ion homeostasis, in particular the calcium ion. Fluctuation in the calcium level triggers the activation of the host defensive programmed cell death pathways as well as the inflammasome, which in turn are being subverted for the viruses' replication benefits. This review article summarizes recent developments in the functional investigation of viroporins from various viruses and their contributions to viral replication and virulence. Recent categorization places viroporins into two major classes based on the number of TMD that are then further classified into A or B subclasses based on their membrane topology [2] . Single TMD viroporins in subclass A have their N terminus facing the ER lumen while those in subclass B have their C-terminal tails in the ER lumen. For Class IIA and IIB viroporins, both N-and C-terminus are inside the ER lumen or the cytoplasmic matrix, respectively (Figure 1 ). An additional third class of viroporins may be necessary as viroporins with three-pass TMD have been proposed, such as the non-structural protein 4 (NSP4) of rotavirus [49] and 3a of severe acute respiratory syndrome SARS-CoV [31]. Due to their high structural variability under different conditions, solving the architecture of viroporins under physiological environment has been difficult. However, recent advancement in technology such as the ability to characterize protein structure at the atomic resolution using nuclear magnetic resonance (NMR)
answer:
Viral Membrane Channels: Role and Function in the Virus Life Cycle


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Purpose: To provide recommendations and standard operating procedures (SOPs) for intensive care unit (ICU) and hospital preparations for an influenza pandemic or mass disaster with a specific focus on protection of patients and staff. Methods: Based on a literature review and expert opinion, a Delphi process was used to define the essential topics including protection of patients and staff. Results: Key recommendations include: (1) prepare infection control and occupational health policies for clinical risks relating to potential disease transmission; (2) decrease clinical risks and provide adequate facilities through advanced planning to maximise capacity by increasing essential equipment, drugs, supplies and encouraging staff availability; (3) create robust systems to maintain staff confidence and safety by minimising non-clinical risks and maintaining or escalating essential services; (4) prepare formal reassurance plans for legal protection; (5) provide assistance to staff working outside their normal domains. Conclusions: Judicious planning and adoption of protocols for protection of patients and staff are necessary to optimise outcomes during a pandemic.
answer:
Chapter 6. Protection of patients and staff during a pandemic


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a b s t r a c t 5-Arylcarbamoyl-2-methylisoxazolidin-3-yl-3-phosphonates have been synthesised from N-methyl-Cdiethoxyphosphorylnitrone and N-arylacrylamides in good yields. cis-and trans-isoxazolidine phosphonates obtained herein were evaluated for activity against a broad range of DNA and RNA viruses. None of the compounds were endowed with antiviral activity at subtoxic concentrations. Isoxazolidines having phenyl substituted with halogen (Ar = 2-F-C 6 H 4 ; 3-Br-C 6 H 4 ; and 4-Br-C 6 H 4 ) have been found to inhibit proliferation of L1210, CEM as well as HeLa cells with IC 50 in the 100-170 lM range.
answer:

Design, synthesis, antiviral and cytostatic evaluation of novel isoxazolidine nucleotide analogues with a carbamoyl linker