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.
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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


Question: Paul, P.S., 1990. Applications of nucleic acid probes in veterinary infectious diseases. Vet. Microbiol., 24:409-417. Nucleic acid probe technology is increasingly being used in basic research in veterinary microbiology and in diagnosis of infectious diseases of veterinary importance. This review presents an overview of nucleic acid probe methodology and its applications in veterinary infectious diseases. The major applications of nucleic acid probes include detection of pathogens in clinical samples, especially those organisms which are fastidious and difficult to cultivate, differentiation of virulent from avirulent organisms and vaccine strains from wild type isolates, typing of microorganisms, mapping genes, screening libraries of cloned DNA for specific genes, detection of latently infected or carrier animals, study of mechanisms of pathogenesis, epidemiological studies and food safety. 0378-1135/90/$03.50

Answer: Applications of nucleic acid probes in veterinary infectious diseases


Question: Porcine reproductive and respiratory syndrome virus (PRRSV) is an enveloped, positive-sense singlestranded RNA virus belonging to the Arteriviridae family. Arteriviruses and coronaviruses are grouped together in the order Nidovirales, based on similarities in genome organization and expression strategy. Over the past decade, crystal structures of several viral proteins, electron microscopic studies of the virion, as well as biochemical and in vivo studies on protein-protein interactions have led to a greatly increased understanding of PRRSV structural biology. At this point, crystal structures are available for the viral proteases NSP1␣, NSP1␤ and NSP4 and the nucleocapsid protein, N. The NSP1␣ and NSP1␤ structures have revealed additional non-protease domains that may be involved in modulation of host functions. The N protein forms a dimer with a novel fold so far only seen in PRRSV and other nidoviruses. Cryo-electron tomographic studies have shown the three-dimensional organization of the PRRSV virion and suggest that the viral nucleocapsid has an asymmetric, linear arrangement, rather than the isometric core previously described. Together, these studies have revealed a closer structural relationship between arteri-and coronaviruses than previously anticipated.

Answer:
The structural biology of PRRSV