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- 저자 : Xiaoyang Yuan (검색결과 2 건)
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Quantum Coherent Dissociation in a Hybrid Atom-light System with Photon Loss
Xiaoyang Yuan,Jialu Yin,Jiahao Xu,Yixiao Huan,Zhengda Hu 한국광학회 2024 Current Optics and Photonics Vol.8 No.1
We investigate the effect of photon loss on pair production in a hybrid atom-light system. The loss of light field not only affects the generation of photons, but also prevents the generation of atomic collective excitation, although the atoms are not influenced directly. We propose an unbalanced homodyne detection of the number of atomic collective excitation that overcomes the challenge caused by counting uncertainty in practical measurement. In discussion, we show that the intermode correlations and the number correlation is closely related to the initial input state, while the quadrature correlations are independent of the initial state and always exhibit opposite intermode correlations even in the presence of loss.
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Weishi Yu,Yuequn Wang,Yongqing Li,Yun Deng,Zequn Wang,Wuzhou Yuan,Dali Li,Chuanbing Zhu,Xueying Zhao,Xiaoyang Mo,Wen Huang,Na Luo,Yan Yan,Karen Ocorr,Rolf Bodmer,Xiushan Wu 한국분자세포생물학회 2008 Molecules and cells Vol.26 No.5
The Bric-a-brac, Tramtrack, Broad-complex (BTB) domain is a protein-protein interaction domain that is found in many zinc finger transcription factors. BTB containing proteins play important roles in a variety of cellular functions including regulation of transcription, regulation of the cytoskeleton, protein ubiquitination, angiogenesis, and apoptosis. Here, we report the cloning and characterization of a novel human gene, KLHL31, from a human embryonic heart cDNA library. The cDNA of KLHL31 is 5743 bp long, encoding a protein product of 634 amino acids containing a BTB domain. The protein is highly conserved across different species. Western blot analysis indicates that the KLHL31 protein is abundantly expressed in both embryonic skeletal and heart tissue. In COS-7 cells, KLHL31 proteins are localized to both the nucleus and the cytoplasm. In primary cultures of nascent mouse cardiomyocytes, the majority of endogenous KLHL31 proteins are localized to the cytoplasm. KLHL31 acts as a transcription repressor when fused to GAL4 DNA-binding domain and deletion analysis indicates that the BTB domain is the main region responsible for this repression. Overexpression of KLHL31 in COS-7 cells inhibits the transcriptional activities of both the TPA-response element (TRE) and serum response element (SRE). KLHL31 also significantly reduces JNK activation leading to decreased phosphorylation and protein levels of the JNK target c-Jun in both COS-7 and Hela cells. These results suggest that KLHL31 protein may act as a new transcriptional repressor in MAPK/JNK signaling pathway to regulate cellular functions.
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