Ultimately, the story is not just about friendship it is also about one woman, a single swallow, who changes the lives of three men forever. Like the men’s posthumously binding friendship, their connection with Swallow leaves such a deep impact on them, and they remember her with fondness and guilt. At one point, all three of these men show her kindness, and their lives are forever altered. Themes of gender, memory, and trauma are woven throughout the narrative. Swallow shows great promise and intelligence, but the villagers, especially the men, see her as soiled from the attack by the Japanese and disregard her. Her life was devastated when she experienced the violence of Japanese troops firsthand, and the priest, who is serving as the village doctor, shows her compassion and takes her in. Yan means “swallow,” and like a bird she flies into each man’s life and changes them forever. They each refer to her by one of these names, claiming ownership over their version of her. Stella, Wende, A Yan: the three men know her by three different names. Their past slowly begins to unfold throughout the narrative via another common aspect of their lives: meeting a young girl. This friendship even continues beyond death, as the ghost of the priest still travels to the village each year waiting for his friends. Their collective trauma brings them together, and they agree that even after the war, they will all meet again annually in the village on a set day. One is a priest, the other two soldiers, and they must navigate the violent and tense climate of wartime China. She is affiliated with Pomona Valley Hospital Medical Center. She graduated from Xinjiang Med Coll in 1983. THE STORY OF A Single Swallow follows the lives of three men, two westerners and one Chinese, who became friends during World War II in a Chinese village. Xiao-Ling Zhang, MD is an internal medicine specialist in El Monte, CA and has over 39 years of experience in the medical field. Read more about how to correctly acknowledge RSC content.Seattle. Permission is not required) please go to the Copyright If you want to reproduce the wholeĪrticle in a third-party commercial publication (excluding your thesis/dissertation for which If you are the author of this article, you do not need to request permission to reproduce figuresĪnd diagrams provided correct acknowledgement is given. Xiao-Ling Zhangs 165 research works with 2,117 citations and 5,258 reads, including: Two-photon excited red-green 'discoloration' bioprobes for monitoring lipid droplets and lipid droplet. Provided correct acknowledgement is given. If you are an author contributing to an RSC publication, you do not need to request permission Please go to the Copyright Clearance Center request page. To request permission to reproduce material from this article in a commercial publication, Zirui Huang, Min Li, Mengmeng Jin, Yan Li, Hui Zhang, Suhong Sun. Provided that the correct acknowledgement is given and it is not used for commercial purposes. Chunming Wang, Zhijun Cheng, Ling Jiang, Jiawu Zhou, Huishan Guo. This article in other publications, without requesting further permission from the RSC, Ge,Ĭreative Commons Attribution-NonCommercial 3.0 Unported Licence. This work reveals the huge potential of NRPS-like biosynthetic gene clusters in the discovery of novel natural products.ĭiscovery and biosynthesis of guanipiperazine from a NRPS-like pathway Further intermolecular oxidative coupling forming the C–C or C–O bond is catalyzed by another P450 enzyme. The subsequent enzymatic reduction affords piperazine, which can be morphed by a P450 monooxygenase into a highly strained compound through C–O bond formation. The NRPS-like enzyme activates two L-tyrosine molecules, reduces them to the corresponding amino aldehydes, and forms an unstable imine product. Heterologous expression of the gup cluster led to the production of two unprecedented alkaloids, guanipiperazines A and B. Here, we report the discovery of a gene cluster ( gup) encoding a NRPS-like megasynthetase through genome mining. Unlike these canonical multi-modular NRPSs, single-module NRPS-like enzymes, which lack the key condensation (C) domain, are rare in bacteria, and have been largely unexplored to date. Nonribosomal peptide synthetases (NRPSs) are modular enzymes that use a thiotemplate mechanism to assemble the peptide backbones of structurally diverse and biologically active natural products in bacteria and fungi.
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