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We report experimental and theoretical results on the extremely large Lamb shift in a multimode circuit quantum electrodynamics (QED) system in the deep-strong coupling (DSC) regime, where the qubit-resonator coupling strength is comparable to or larger than the qubit and resonator frequencies. The system comprises a superconducting flux qubit (FQ) and a quarter-wavelength coplanar waveguide resonator ([Formula: see text] CPWR) that are coupled inductively through a shared edge that contains a Josephson junction to achieve the DSC regime. Spectroscopy is performed around the frequency of the fundamental mode of the CPWR, and the spectrum is fitted by the single-mode quantum Rabi Hamiltonian to obtain the system parameters. Since the qubit is also coupled to a large number of higher modes in the resonator, the single-mode fitting does not provide the bare qubit energy but a value that incorporates the renormalization from all the other modes. We derive theoretical formulas for the Lamb shift in the multimode resonator system. As shown in previous studies, there is a cut-off frequency [Formula: see text] for the coupling between the FQ and the modes in the CPWR, where the coupling grows as [Formula: see text] for [Formula: see text] and decreases as [Formula: see text] for [Formula: see text]. Here [Formula: see text] is the frequency of the nth mode. The cut-off effect occurs because the qubit acts as an obstacle for the current in the resonator, which suppresses the current of the modes above [Formula: see text] at the location of the qubit and results in a reduced coupling strength. Using our observed spectrum and theoretical formulas, we estimate that the Lamb shift from the fundamental mode is 82.3% and the total Lamb shift from all the modes is 96.5%. This result illustrates that the coupling to the large number of modes in a CPWR yields an extremely large Lamb shift but does not suppress the qubit energy to zero, which would happen in the absence of a high-frequency cut-off., (© 2023. The Author(s).)

The functional role of thyroid hormone (TH) in the cortex and hippocampus of mouse during neuronal development was investigated in this study. TH insufficiency showed a decrease in the expression of parvalbumin (PV) in the cortex and hippocampus of pups at postnatal day (PD) 14, while treatment with thyroxine from PD 0 to PD 14 ameliorated the PV loss. On the other hand, treatment with antithyroid agents in adulthood did not result in a decrease in the expression of PV in these areas. These results indicate the existence of a critical period of TH action during the early postnatal period. A decrease in MeCP2-positive neuronal nuclei was also observed in the cortical layers II-IV of the cerebral cortex. The brains were then stained with CUX1, a marker for cortical layers II-IV. In comparison with normal mice, CUX1 signals were decreased in the somatosensory cortex of the hypothyroid mice, and the total thickness of cortical layers II-IV of the mice was lower than that of normal mice. These results suggest that TH insufficiency during the perinatal period strongly and broadly affects neuronal development.

Prion diseases are fatal neurodegenerative disorders characterized by the accumulation of prion protein (PrP(C)). To date, there is no effective treatment for the disease. The accumulated PrP, termed PrP(Sc), forms amyloid fibrils and could be infectious. It has been suggested that PrP(Sc) is abnormally folded and resistant to proteolytic degradation, and also inhibits proteasomal functions in infected cells, thereby inducing neuronal death. Recent work indicates that the ubiquitin-proteasome system is involved in quality control of PrP(C). To reveal the significance of prion protein ubiqitination, we focused on ubiquitin-specific protease 14 (USP14), a deubiqutinating enzyme that catalyzes trimming of polyubiquitin chains and plays a role in regulation of proteasomal processes. Results from the present study showed that treatment with a selective inhibitor of USP14 reduced PrP(C), as well as PrP(Sc), levels in prion-infected neuronal cells. Overexpression of the dominant negative mutant form of USP14 reduced PrP(Sc), whereas wildtype USP14 increased PrP(Sc) in prion-infected cells. These results suggest that USP14 prevents degradation of both normal and abnormal PrP. Collectively, a better understanding about the regulation of PrP(Sc) clearance caused by USP14 might contribute greatly to the development of therapeutic strategies for prion diseases.

As a prompt response against invasion of various viruses, interferon regulatory factor-3 (IRF-3) is initially phosphorylated to become activated and upregulates mainly Type I Interferons (IFN-I) in most cell types. We previously reported that IRF-3-dependent host innate immune responses partially interfere in infection of prions. Here, we found that stable infection of prion suppressed IRF-3 gene-expression. The decreased promoter activity of IRF-3 was significantly restored along with treatment of anti-prion drugs in the prion-infected cells, suggesting that infection of prion directly influence the regulation of IRF-3 transcription. We further investigated promoter activity of 5'- flanking region of murine IRF-3 using a luciferase reporter system and found that the nucleotides -119 to -1 were indispensable for the promoter activity. Within this region, mutations in the Oct-1 binding site significantly reduced the promoter activity and chromatin immunoprecipitation (ChIP) assay revealed that Oct-1 indeed binds to the region. In addition, overexpression of Oct-1 increased the promoter activity of IRF-3. Intriguingly, Oct-1 protein was significantly reduced in prion-infected cells and mice brains compared with uninfected groups. Taken together, we concluded that prion infection could interfere in the function of Oct-1, resulting in the down-regulation of IRF-3.