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.

[EX Q]: Redirecting the splicing machinery through the hybridization of high affinity, RNase H-incompetent oligonucleotide analogs such as phosphoramidate morpholino oligonucleotides (PMO) might lead to important clinical applications. Chemical conjugation of PMO to arginine-rich cell penetrating peptides (CPP) such as (R-Ahx-R) 4 (with Ahx standing for 6-aminohexanoic acid) leads to sequencespecific splicing correction in the absence of endosomolytic agents in cell culture at variance with most conventional CPPs. Importantly, (R-Ahx-R) 4 -PMO conjugates are effective in mouse models of various viral infections and Duchenne muscular dystrophy. Unfortunately, active doses in some applications might be close to cytotoxic ones thus presenting challenge for systemic administration of the conjugates in those clinical settings. Structureactivity relationship studies have thus been undertaken to unravel CPP structural features important for the efficient nuclear delivery of the conjugated PMO and limiting steps in their internalization pathway. Affinity for heparin (taken as a model heparan sulfate), hydrophobicity, cellular uptake, intracellular distribution and splicing correction have been monitored. Spacing between the charges, hydrophobicity of the linker between the Arg-groups and Arg-stereochemistry influence splicing correction efficiency. A significant correlation between splicing correction efficiency, affinity for heparin and ability to destabilize model synthetic vesicles has been observed but no correlation with cellular uptake has been found. Efforts will have to focus on endosomal escape since it appears to remain the limiting factor for the delivery of these splice-redirecting ON analogs.
[EX A]: Delivery of steric block morpholino oligomers by (R-X-R) 4 peptides: structure-activity studies

[EX Q]: An oligonucleotide array (microarray) incorporating 13,000 elements representing selected strains of hepatitis A virus (HAV), human coxsackieviruses A and B (CVA and CVB), genogroups I and II of Norovirus (NV), and human rotavirus (RV) gene segments 3,4,10, and 11 was designed based on the principle of tiling. Each oligonucleotide was 29 bases long, starting at every 5 th base of every sequence, resulting in an overlap of 24 bases in two consecutive oligonucleotides. The applicability of the array for virus identification was examined using PCR amplified products from multiple HAV and CV strains. PCR products labeled with biotin were hybridized to the array, and the biotin was detected using a brief reaction with Cy3-labeled streptavidin, the array subjected to laser scanning, and the hybridization data plotted as fluorescence intensity against each oligonucleotide in the array. The combined signal intensities of all probes representing a particular strain of virus were calculated and plotted against all virus strains identified on a linear representation of the array. The profile of the total signal intensity identified the strain that is most likely represented in the amplified cDNA target. The results obtained with HAV and CV indicated that the hybridization profile thus generated can be used to identify closely related viral strains. This represents a significant improvement over current methods for virus identification using PCR amplification and amplicon sequencing.
[EX A]: A Microarray Based Approach for the Identification of Common Foodborne Viruses

[EX Q]: When it was noticed that 5D-8.1 may cross-react with human proteins, doubt was casted on the significance of the above histopathologic findings. To address this issue, properties of EV antibodies 5D-8.1 and 9D5 have been investigated using peptide microarrays, peptide substitution scanning, immunofluorescence of EV-infected cells, EV neutralization assays, bioinformatics analysis. Evidence indicates that the two antibodies bind to distinct non-neutralizing linear epitopes in VP1 and are specific for a vast spectrum of EV types (not for other human viruses). However, their epitopes may align with a few human proteins at low expected values. When tested by immunofluorescence, high concentrations of 5D-8. Several recent reports point to enterovirus (EV) infections as key environmental triggers of type 1 diabetes (T1D) 1-7 . Conclusions are based on multiple proofs that include the histopathologic detection of EV antigens/ genome in the islets of Langerhans of diabetics at different stages of the disease 8-12 . Recent findings suggest that EVs are causing chronic low-level infection in the islet cells of newly diagnosed T1D patients 12 . EVs are small, non-enveloped, single-strand positive-sense RNA viruses belonging to the family Picornaviridae. The EV capsid is composed of four structural proteins named VP1, VP2, VP3, and VP4. The main structural differences among VP1, VP2, and VP3 lie in the loops that connect the beta-strands with the N-and C-terminal sequences extending from the beta-barrel domain 13 . These amino acid (AA) sequences give each EV its distinct morphology and antigenicity. The VP4 component lies on the inner surface of the shell and is essential for virion stability. Evolution has resulted in a large number of antigenically distinguishable members that have been categorized as EV "serotypes" 13 . Not considering human rhinoviruses, the EV genus contains human agents of the A, B, C, D, and unnamed species that, together, comprise 109 different types. Each of the serotypes correlates with a specific immune response of the host and protection from disease. The serotype-specific protective immune response is directed to the capsid proteins VP1, VP2, and VP3, as the VP4 has no role in the interaction with neutralizing antibodies (i.e., those directed to variable regions of surface capsid proteins). Non-neutralizing antibodies recognizing VP regions that are conserved among different EV types are also produced. The significance of the non-neutralizing antibody response is currently under investigation 14 . Immunization with different EV types allowed to produce a variety of monoclonal antibodies (MAbs) that are either type-specific (i.e., responsible of virus neutralization) or directed to conserved regions of capsid proteins 15-18 . Reactivity of the latter antibodies may be limited to sets of different EV types or may be directed to a wider range of EV types. Though molecular methods are held to be more informative than classical serologic methods for virus identification 19 , "pan-EV antibodies" capable of reacting with all or with the majority of EV types remain desirable reagents for detecting these agents both in the diagnosis of infectious diseases 20-23 and in immunohistochemistry 24 .
[EX A]:
Properties of Two Enterovirus Antibodies that are Utilized in Diabetes Research OPEN