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| 1 | Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics on the design of substrate analogs or site- directed mutagenesis 显示文摘 | LIU Qun HUANG Qingqiu LEI Xingen | 2004 | Structure2004，12，9： | 1 |
| 2 | Sperm cryopreservation in guppies and black mollies—A generalized freezing protocol for livebearers in Poeciliidae显示文摘 | Changjiang Huang Chunli Sun Xinyou Su Xingen Zhao Miao Miao Yueqin Liu Qiaoxiang Dong | 2009 | Cryobiology2009，，3： | 1 |
| 3 | Selenium deficiency-induced multiple tissue damage with dysregulation of immune and redox homeostasis in broiler chicks under heat stress显示文摘Broiler chicks are fast-growing and susceptible to dietary selenium(Se) deficiency. This study sought to reveal the underlying mechanisms of how Se deficiency induces key organ dysfunctions in broilers. Day-old male chicks(n=6 cages/diet, 6 chicks/cage) were fed with a Se-deficient diet(Se-Def, 0.047 mg Se/kg) or the Se-Def+0.3 mg Se/kg(Control, 0.345 mg Se/kg) for 6weeks. The serum, liver, pancreas, spleen, heart, and pectoral muscle of the broilers were collected at week 6 to assay for Se concentration, histopathology, serum metabolome, and tissue transcriptome. Compared with the Control group, Se deficiency induced growth retardation and histopathological lesions and reduced Se concentration in the five organs. Integrated transcriptomics and metabolomics analysis revealed that dysregulation of immune and redox homeostasis related biological processes and pathways contributed to Se deficiency-induced multiple tissue damage in the broilers. Meanwhile, four metabolites in the serum, daidzein, epinephrine, L-aspartic acid and 5-hydroxyindoleacetic acid, interacted with differentially expressed genes with antioxidative effects and immunity among all the five organs, which contributed to the metabolic diseases induced by Se deficiency. Overall, this study systematically elucidated the underlying molecular mechanisms in the pathogenesis of Se deficiency-related diseases, which provides a better understanding of the significance of Se-mediated heath in animals. | Ling Zhao Meng Liu Hua Sun Jia-Cheng Yang Yu-Xuan Huang Jia-Qiang Huang Xingen Lei Lv-Hui Sun | 2023 | Science China(Life Sciences)2023，66，9： | 1 |
| 4 | Chlorogenic acid protects MSCs against oxidative stress by altering FOXO family genes and activating intrinsic pathway显示文摘 | Shiyong Li Hetao Bian Zhe Liu Ye Wang Jianghua Dai Wenfeng He Xingen Liao Rongrong Liu Jun Luo | 2011 | European Journal of Pharmacology2011，，2： | 1 |
| 5 | Enhanced lu- minescence of CaaB206 = Dy^3+ phosphors hy Na+-codoping for LED applications显示文摘 | Sun Xinyuan Zhang Juncheng Liu Xingen | 2011 | Physica B: Condensed Matter2011，406，21： | 1 |
| 6 | Enhanced lu- minescence of novel Ca3 B2 O6 : Dy^3+ phosphors by Li^+-codoping for LED applications 显示文摘 | Sun Xinyuan Zhang Juncheng Liu Xingen | 2012 | Ceramics International2012，38，2： | 1 |
| 7 | Cloning,expression,and characterization of a porcine pancreatic α-amylase in Pichia pastoris显示文摘Pancreatic α-amylase(α-1, 4-glucan-4-glucanohydrolase, EC.3.2.1.1) plays a primary role in the intestinal digestion of feed starch and is often deficient in weanling pigs.The objective of this study was to clone,express, and characterize porcine pancreatic α-amylase(PPA).The full-length c DNA encoding the PPA was isolated from pig pancreas by RT-PCR and cloned into the pPICZαA vector.After the resultant pPICZαА-PPA plasmid was transferred into Pichia pastoris, Ni Sepharose affinity column was used to purify the over-expressed extracellular recombinant PPA protein(re PPA) that contains a His-tag to the C terminus and was characterized against the natural enzyme(α-amylase from porcine pancreas).The re PPA exhibited a molecular mass of approximately 58 kDa and showed optimal temperature(50℃),optimal pH(7.5), K_m(47.8 mg/mL), and V_(max)(2,783 U/mg) similar to those of the natural enzyme.The recombinant enzyme was stable at 40℃ but lost 60% to 90%(P < 0.05) after exposure to heating at≥50℃ for 30 min.The enzyme activity was little affected by Cu^(2+)or Fe^(3+), but might be inhibited(40% to 50%) by Zn^(2+)at concentrations in pig digesta.However, Ca^(2+)exhibited a dose-dependent stimulation of the enzyme activity.In conclusion, the present study successfully cloned the porcine pancreatic aamylase gene and over-expressed the gene in P.pastoris as an extracellular, functional enzyme.The biochemical characterization of the over-produced enzyme depicts its potential and future improvement as an animal feed additive. | Lv-hui Sun Tao Qin Yan Liu Hua Zhao Xinjie Xia Xingen Lei | 2018 | Animal Nutrition2018，，2： | 0 |
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