Purpose To compare the benefits and harms of radiofrequency ablation (RFA) and hepatic resection (HR) and to test the consistency of currently available evidence. Materials and Methods PubMed, Embase, and the Cochrane Library were systematically searched for randomized controlled trials (RCTs) that compared the effects of HR and RFA for Barcelona Clinic Liver Cancer very early or early stage hepatocellular carcinoma (HCC). The primary outcome was overall survival, and secondary outcomes were recurrence rate, complication rate, and hospitalization duration. A random- or fixed-effects model according to the level of heterogeneity was applied. The meta-analysis was performed by using software, and trial sequential analysis (TSA) was performed. Results Five trials examining 742 patients were included in this study (sizes of trials: 161, 230, 168, 120, and 63 patients). The meta-analysis showed that RFA and HR had similar overall survival at 1 year (relative risk [RR], 1.39; 95% confidence interval [CI]: 0.36, 5.33; P = .63) and 3 years (RR, 1.40; 95% CI: 0.75, 2.62; P = .29), whereas RFA resulted in decreased overall survival compared with HR at 5 years (RR: 1.91; 95% CI: 1.32, 2.79; P = .001). The TSA showed that more trials were needed to control random errors. The incidence of overall recurrence was markedly higher and the hospitalization duration was significantly shorter in the RFA group than in the HR group, which was confirmed by TSA. Complications may have been less frequent in the RFA group, but TSA showed that additional trials were necessary to confirm this conclusion. Conclusion The indication for RFA as a primary treatment for patients who are eligible for HR with early stage HCC is unclear, and additional well-designed RCTs are needed. RSNA, 2017 Online supplemental material is available for this article.

Chemotherapy before enucleation of group E eyes with advanced retinoblastoma downstaged pathologic evidence of extraocular extension, and increased the risk of metastatic death from reduced surveillance and inappropriate management of high-risk disease, if enucleation was performed longer than 3 months after diagnosis.

Lamina cribrosa thickness and peripapillary sclera thickness decreased significantly with axial length, in addition to a glaucoma-related thinning of the lamina cribrosa. In non-axially elongated eyes, the peripapillary sclera thickness did not vary significantly between glaucomatous eyes and normal eyes.

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The nucleocapsid (N) protein of hantaviruses encapsidates both viral genomic and antigenomic RNAs, although only the genomic viral RNA (vRNA) is packaged into virions. To define the domain within the Hantaan virus (HTNV) N protein that mediates these interactions, 14 N-and C-terminal deletion constructs were cloned into a bacterial expression vector, expressed, and purified to homogeneity. Each protein was examined for its ability to bind the HTNV S segment vRNA with filter binding and gel electrophoretic mobility shift assays. These studies mapped a minimal region within the HTNV N protein (amino acids 175 to 217) that bound vRNA. Sequence alignments made from several hantavirus N protein sequences showed that the region identified has a 58% identity and an 86% similarity among these amino acid sequences. Two peptides corresponding to amino acids 175 to 196 (N1) and 197 to 218 (N2) were synthesized. The RNA binding of each peptide was measured by filter binding and competition analysis. Three oligoribonucleotides were used to measure binding affinity and assess specificity. The N2 peptide contained the major RNA binding determinants, while the N1 peptide, when mixed with N2, contributed to the specificity of vRNA recognition.

The nucleocapsid (N) protein encapsidates both viral genomic RNA (vRNA) and the antigenomic RNA (cRNA), but not viral mRNA. Previous work has shown that the N protein has preference for vRNA, and this suggested the possibility of a cis-acting signal that could be used to initiate encapsidation for the S segment. To map the cis-acting determinants, several deletion RNA derivatives and synthetic oligoribonucleotides were constructed from the S segment of the Hantaan virus (HTNV) vRNA. N protein-RNA interactions were examined by UV cross-linking studies, filter-binding assays, and gel electrophoresis mobility shift assays to define the ability of each to bind HTNV N protein. The 5 end of the S-segment vRNA was observed to be necessary and sufficient for the binding reaction. Modeling of the 5 end of the vRNA revealed a possible stem-loop structure (SL) with a large single-stranded loop. We suggest that a specific interaction occurs between the N protein and sequences within this region to initiate encapsidation of the vRNAs.Hantaviruses are tripartite, negative-stranded viruses harbored by a variety of rodents in the Muridae family, which are distributed throughout the world. Transmission of these viruses to humans occurs through inhalation of rodent excreta and can result in one of two illnesses depending on the virus, hantavirus pulmonary syndrome (HPS) or hemorrhagic fever with renal syndrome (HFRS) (10). Because of the geographical distribution of the rodent reservoirs of these viruses, HPS has emerged as a significant illness throughout the Americas, while HFRS is limited to the Old World. One of the more severe HFRS illnesses is caused by Hantaan virus (HTNV), which causes death in 5 to 15% of the cases (5, 6).The hantavirus genome encodes an RNA-dependent RNA polymerase (RdRp) (L segment), a nucleocapsid (N) protein (S segment), and two glycoproteins, G1 and G2 (M segment) (11,12). Minimally, the components of replication include the RdRp, the N protein, and the virus genomic and antigenomic RNA templates. Following entry of the virion into the cytoplasm, the RdRp initiates viral cRNA synthesis from the L, M, and S viral genomic RNAs (vRNAs). Additional vRNA is synthesized from the cRNA. Both vRNA and cRNA are complexed with the N protein throughout transcription and replication, but mRNA is not (3). The cis-acting viral sequences which promote the specific interaction of N with vRNA and cRNA during viral replication are unknown. It is likely that sequences or structures present in the 5Ј ends of the RNA molecules would provide a point of nucleation for subsequent encapsidation of the entire genomic or antigenomic segment (8).Interaction of the HTNV N protein with its vRNA shows little ionic strength dependence (13). However, increase in the ionic strength of the binding reaction greatly reduced the HTNV N protein's affinity for nonviral RNA. In the same study, filter-binding assays demonstrated a moderate binding preference of the HTNV N for the S-segment vRNA compared to an RNA comprising only the open rea...