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 Input:
Here we describe a novel endonuclease IV (Endo IV) based assay utilizing a substrate that mimics the abasic lesions that normally occur in doublestranded DNA. The three component substrate is characterized by single-stranded DNA target, an oligonucleotide probe, separated from a helper oligonucleotide by a one base gap. The oligonucleotide probe contains a non-fluorescent quencher at the 5 0 end and fluorophore attached to the 3 0 end through a special rigid linker. Fluorescence of the oligonucleotide probe is efficiently quenched by the interaction of terminal dye and quencher when not hybridized. Upon hybridization of the oligonucleotide probe and helper probe to their complementary target, the phosphodiester linkage between the rigid linker and the 3 0 end of the probe is efficiently cleaved, generating a fluorescent signal. In this study, the use of the Endo IV assay as a post-PCR amplification detection system is demonstrated. High sensitivity and specificity are illustrated using single nucleotide polymorphism detection.

Ex Output:
A novel endonuclease IV post-PCR genotyping system


Ex Input:
Toxoplasma gondii is a worldwide spread protozoan and is able to infect almost all warm-blood animals. No effective drugs are available clinically on toxoplasmosis. Chinese traditional herbal medicines have provided remedies for many health problems. There exists a possibility that Chinese herbs may provide protection against T. gondii. This work aims to assess the protective efficacy of combined Chinese herbs against T. gondii. We screened five herbal medicines that have different pharmacological effects and combined them into a prescription according to the traditional Chinese medicine compatibility principle. The drug potential and protective efficacy were evaluated through a mouse model by determining the survival time, the parasite load in blood and tissues, the change of cell proportions in blood and histological detection. The results showed that the survival time of mice in the 500 mg Chinese herbs group and sulfadiazine group was significantly longer than that of the PBS control group. Also the parasite load in blood and tissues of 500 mg Chinese herbs and sulfadiazine groups was significantly lower than that of PBS group at 7 days post infection (dpi), which was in accordance with the result of histological detection. Monocyte and neutrophil of infected mice were remarkably increased while lymphocyte was dramatically decreased compared to that of blank group at 7 dpi. The results demonstrated that the 500 mg dosage of our Chinese herbs could slow down the replication of T. gondii and prolong the survival time of mice and could be considered as possible candidate drug against toxoplasmosis.

Ex Output:
Evaluation of potential anti-toxoplasmosis efficiency of combined traditional herbs in a mouse model *


Ex Input:
The Sabin I poliovirus live, attenuated vaccine strain encodes for four amino acid changes (i.e., D53N, Y73H, K250E, and T362I) in the RNA-dependent RNA polymerase (RdRp). We have previously shown that the T362I substitution leads to a lower fidelity RdRp, and viruses encoding this variant are attenuated in a mouse model of poliovirus. Given these results, it was surprising that the nucleotide incorporation rate and nucleobase fidelity of the Sabin I RdRp is similar to that of wild-type enzyme, although the Sabin I RdRp is less selective against nucleotides with modified sugar groups. We suggest that the other Sabin amino acid changes (i.e., D53N, Y73H, K250E) help to re-establish nucleotide incorporation rates and nucleotide discrimination near wild-type levels, which may be a requirement for the propagation of the virus and its efficacy as a vaccine strain. These results also suggest that the nucleobase fidelity of the Sabin I RdRp likely does not contribute to viral attenuation. Viruses 2015, 7, 5571-5586 viral virulence, likely because the T362I RdRp is a more error-prone polymerase than the "wild-type" (WT) enzyme [22] . These results are intriguing, and might suggest that the Sabin I RdRp also contributes to viral attenuation. Such findings would be intriguing in light of the suggestion that viruses encoding RdRp enzymes with altered fidelity might serve as live, attenuated vaccine candidates [23] . PV RdRp has a highly-conserved canonical cupped right-hand structure with palm, thumb, and finger subdomains (Figure 1) [24]. There are seven conserved structural motifs, five of which (A to E) are located in the palm subdomain [25, 26] . The T362I amino acid change occurs on structural motif D, which we have proposed is important in phosphodiester bond formation and nucleotide discrimination [27, 28] . More specifically, motif D contains a highly-conserved lysine residue (Lys359 in PV RdRp), which we have proposed acts as a general acid to protonate the β-phosphate of the incoming nucleotide to facilitate bond breakage between the αand β-phosphates and create a better pyrophosphate leaving group [28, 29] . We have suggested that the active-site loop containing Lys359 fluctuates between "closed" and "open" conformations in which Lys359 is positioned and out-of-position for catalysis, respectively. Our previous nuclear magnetic resonance (NMR) studies are consistent with this proposal [22, 29, 30] . We have shown that the Sabin-derived T362I amino acid substitution alters the motions of motif D, allowing the enzyme to fluctuate more readily into a closed conformation even in the presence of incorrect nucleotide, leading to a less faithful polymerase [22] . Other amino acid substitutions in the Sabin I RdRp may also change RdRp function. The Y73H substitution has been shown to interfere with the initiation of RNA synthesis [19] , which might help to explain why PV encoding the Y73H substitution is attenuated [17, 20] . The D53N, Y73H, and T362I substitutions also contribute to the temperature sensitivity of the Sabin I vaccine [15] [16] [17] 31] . The Sabin substitutions may also affect each other. Our previous molecular dynamics (MD) simulations suggest that the T362I amino acid substitution induces different nanosecond timescale motions in distant parts of the enzyme, including around Asp53 [22] . We have also previously noted anti-correlated motions between motif D and the α-helix containing Tyr73 [32] . It is also noted that the helices containing Tyr73 and Lys250 are packed closely together (Figure 1 ). Altogether, these results suggest that there are structural and dynamic connections between the various Sabin sites, which may contribute to the function of the Sabin I RdRp.

Ex Output:

Nucleobase but not Sugar Fidelity is Maintained in the Sabin I RNA-Dependent RNA Polymerase