Publications

Found 19 results
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2015
X. Y. Li, Luo, B. L., Wang, L. J., Zhang, W. D., and Liu, Z. G., 15-Deoxy-prostaglandin J2 anti-inflammation in a rat model of chronic obstructive pulmonary disease and human bronchial epithelial cells via Nrf2 activation, vol. 14, pp. 14037-14042, 2015.
B. Yuan, Li, X. Y., Zhu, T., Yuan, L., Hu, J. P., Chen, J., Gao, W., and Ren, W. Z., Antibody study in canine distemper virus nucleocapsid protein gene-immunized mice, vol. 14, pp. 3098-3105, 2015.
X. Y. Li, Ye, J. Z., Ding, X. P., Zhang, X. H., Ma, T. J., Zhong, R., and Ren, H. Y., Association between methionine synthase reductase A66G polymorphism and primary infertility in Chinese males, vol. 14, pp. 3491-3500, 2015.
X. Y. Li, Yang, G. W., Zheng, D. S., Guo, W. S., and Hung, W. N. N., An efficient algorithm for computing fixed length attractors based on bounded model checking in synchronous Boolean networks with biochemical applications, vol. 14, pp. 4238-4244, 2015.
H. Y. Yu, Li, X. Y., Cai, Z. F., Li, L., Shi, X. Z., Song, H. X., and Liu, X. J., Eosinophil cationic protein mRNA expression in children with bronchial asthma, vol. 14, pp. 14279-14285, 2015.
X. Y. Li, Liu, F., Hu, Y. F., Xia, M., Cheng, B. J., Zhu, S. W., and Ma, Q., Overexpression of an endo-1,4-β-glucanase V gene (EGV) from Trichoderma reesei leads to the accumulation of cellulase activity in transgenic rice, vol. 14, pp. 17519-17528, 2015.
Z. Y. Gao, Li, X. Y., Bhandari, V., Li, L. D., and Lan, D., Pre-B-cell colony-enhancing factor is markedly elevated in childhood hemophagocytic lymphohistiocytosis, vol. 14, pp. 5287-5295, 2015.
W. C. Zhao, Gao, X., Dong, J., Zhao, Z. J., Chen, Q. G., Chen, L. G., Shi, Y. G., and Li, X. Y., Stripe rust resistance and dough quality of new wheat - Dasypyrum villosum translocation lines, vol. 14, pp. 8077-8083, 2015.
L. Jiang, Jing, G. X., Li, X. Y., Wang, X. Q., Xing, Z., Deng, P. K., and Zhao, R. G., Tissue culture characteristics of maize (Zea mays L.) haploid coleoptile sections, vol. 14, pp. 16265-16275, 2015.
X. L. Shi, Li, C. W., Liang, B. C., He, K. H., and Li, X. Y., Weak cation magnetic separation technology and MALDI-TOF-MS in screening serum protein markers in primary type I osteoporosis, vol. 14, pp. 15285-15294, 2015.
2012
Y. J. Li, Li, X. Y., Guo, X. R., Li, Y., Shen, B. F., Shi, Y. C., and Zhang, J. Y., Absence of SH2B3 mutation in nonobese diabetic mice, vol. 11, pp. 1266-1271, 2012.
Cui J, Zhu N, Wang Q, Yu M, et al. (2009). p38 MAPK contributes to CD54 expression and the enhancement of phagocytic activity during macrophage development. Cell Immunol. 256: 6-11. http://dx.doi.org/10.1016/j.cellimm.2008.12.003 PMid:19185295   D'Alise AM, Auyeung V, Feuerer M, Nishio J, et al. (2008). The defect in T-cell regulation in NOD mice is an effect on the T-cell effectors. Proc. Natl. Acad. Sci. U. S. A. 105: 19857-19862. http://dx.doi.org/10.1073/pnas.0810713105 PMid:19073938 PMCid:2604930   Delovitch TL and Singh B (1997). The nonobese diabetic mouse as a model of autoimmune diabetes: immune dysregulation gets the NOD. Immunity 7: 727-738. http://dx.doi.org/10.1016/S1074-7613(00)80392-1   Hung JT, Liao JH, Lin YC, Chang HY, et al. (2005). Immunopathogenic role of TH1 cells in autoimmune diabetes: evidence from a T1 and T2 doubly transgenic non-obese diabetic mouse model. J. Autoimmun. 25: 181-192. http://dx.doi.org/10.1016/j.jaut.2005.08.010 PMid:16263243   Hunt KA, Zhernakova A, Turner G, Heap GA, et al. (2008). Newly identified genetic risk variants for celiac disease related to the immune response. Nat. Genet. 40: 395-402. http://dx.doi.org/10.1038/ng.102 PMid:18311140 PMCid:2673512   Li Y, He X, Schembri-King J, Jakes S, et al. (2000). Cloning and characterization of human Lnk, an adaptor protein with pleckstrin homology and Src homology 2 domains that can inhibit T cell activation. J. Immunol. 164: 5199-5206. PMid:10799879   Marleau AM, Summers KL and Singh B (2008). Differential contributions of APC subsets to T cell activation in nonobese diabetic mice. J. Immunol. 180: 5235-5249. PMid:18390704   Todd JA, Walker NM, Cooper JD, Smyth DJ, et al. (2007). Robust associations of four new chromosome regions from genome-wide analyses of type 1 diabetes. Nat. Genet. 39: 857-864. http://dx.doi.org/10.1038/ng2068 PMid:17554260 PMCid:2492393   Velazquez L, Cheng AM, Fleming HE, Furlonger C, et al. (2002). Cytokine signaling and hematopoietic homeostasis are disrupted in Lnk-deficient mice. J. Exp. Med. 195: 1599-1611. http://dx.doi.org/10.1084/jem.20011883 PMid:12070287 PMCid:2193556   Zhang J, Zhu N, Wang Q, Wang J, et al. (2010). MEKK3 overexpression contributes to the hyperresponsiveness of IL-12- overproducing cells and CD4+ T conventional cells in nonobese diabetic mice. J. Immunol. 185: 3554-3563. http://dx.doi.org/10.4049/jimmunol.1000431 PMid:20720201
2011
X. Y. Li, Zhang, J. L., and Zhu, S. W., Improved thermostable α-amylase activity of Bacillus amyloliquefaciens by low-energy ion implantation, vol. 10, pp. 2181-2189, 2011.
Asghari SM,Khajeh K,Ranjbar B,Sajedi RH,et al. (2004). Comparative studies on trifluoroethanol (TFE) state of a thermophilic alpha-amylase and its mesophilic counterpart: limited proteolysis, conformational analysis, aggregation and reactivation of the enzymes. Int. J. Biol. Macromol. 34: 173-179. http://dx.doi.org/10.1016/j.ijbiomac.2004.03.006 PMid:15225989 Azad MA, Bae JH, Kim JS, Lim JK, et al. (2009). Isolation and characterization of a novel thermostable alpha-amylase from Korean pine seeds. N. Biotechnol. 26: 143-149. http://dx.doi.org/10.1016/j.nbt.2009.09.006 PMid:19772955 Declerck N, Machius M, Wiegand G, Huber R, et al. (2000). Probing structural determinants specifying high thermostability in Bacillus licheniformis alpha-amylase. J. Mol. Biol. 301: 1041-1057. http://dx.doi.org/10.1006/jmbi.2000.4025 PMid:10966804 Dong Y,Liu Y,Chen Y,Niu D,et al. (2008). Purification and characterization of thermostable amylases from two bacterial species. Wei Sheng Wu Xue Bao 48: 169-175. PMid:18437997 Du BB, Hao S, Li YM, Yue LL, et al. (2006). Expression of a thermostable a-amylase mutant into Escherichia coli and Pichia pastoris. Wei Sheng Wu Xue Bao 46: 827-830. PMid:17172038 Fielden MR, Matthews JB, Fertuck KC, Halgren RG, et al. (2002). In silico approaches to mechanistic and predictive toxicology: an introduction to bioinformatics for toxicologists. Crit. Rev. Toxicol. 32: 67-112. http://dx.doi.org/10.1080/20024091064183 PMid:11951993 Fondy BR, Geiger DR and Servaites JC (1989). Photosynthesis, carbohydrate metabolism, and export in Beta vulgaris L. and Phaseolus vulgaris L. during square and sinusoidal light regimes. Plant Physiol. 89: 396-402. http://dx.doi.org/10.1104/pp.89.2.396 PMid:16666555    PMCid:1055853 Hoj PB,Hartman DJ,Morrice NA,Doan DN,et al. (1989). Purification of (1→3)-beta-glucan endohydrolase isoenzyme II from germinated barley and determination of its primary structure from a cDNA clone. Plant Mol. Biol. 13: 31-42. http://dx.doi.org/10.1007/BF00027333 Igarashi K, Hatada Y, Hagihara H, Saeki K, et al. (1998). Enzymatic properties of a novel liquefying alpha-amylase from an alkaliphilic Bacillus isolate and entire nucleotide and amino acid sequences. Appl. Environ. Microbiol. 64: 3282- 3289. PMid:9726872    PMCid:106722 Khemakhem B, Ali MB, Aghajari N, Juy M, et al. (2009). Engineering of the alpha-amylase from Geobacillus stearothermophilus US100 for detergent incorporation. Biotechnol. Bioeng. 102: 380-389. http://dx.doi.org/10.1002/bit.22083 PMid:18951544 Kiefer J, Egenolf R and Ikpeme S (2002). Heavy ion-induced DNA double-strand breaks in yeast. Radiat. Res. 157: 141- 148. http://dx.doi.org/10.1667/0033-7587(2002)157[0141:HIIDDS]2.0.CO;2 Kim YW, Choi JH, Kim JW, Park C, et al. (2003). Directed evolution of Thermus maltogenic amylase toward enhanced thermal resistance. Appl. Environ. Microbiol. 69: 4866-4874. http://dx.doi.org/10.1128/AEM.69.8.4866-4874.2003 PMid:12902281    PMCid:169122 Li M, Wu YJ, Yu ZL, Sheng GP, et al. (2009). Enhanced nitrogen and phosphorus removal from eutrophic lake water by Ipomoea aquatica with low-energy ion implantation. Water Res. 43: 1247-1256. http://dx.doi.org/10.1016/j.watres.2008.12.013 PMid:19147171 Liu J, Li Q, Yu Y and Fang X (2003). Spectroscopic and electrochemical studies of DNA breakage induced by dopamine and copper ion. Anal. Sci. 19: 1099-1102. http://dx.doi.org/10.2116/analsci.19.1099 PMid:12945659 Machius M, Wiegand G and Huber R (1995). Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution. J. Mol. Biol. 246: 545-559. http://dx.doi.org/10.1006/jmbi.1994.0106 PMid:7877175 Mollania N,Khajeh K,Hosseinkhani S and Dabirmanesh B (2010). Purification and characterization of a thermostable phytate resistant alpha-amylase from Geobacillus sp. LH8. Int. J. Biol. Macromol. 46: 27-36. http://dx.doi.org/10.1016/j.ijbiomac.2009.10.010 PMid:19874846 Nordhoff E, Cramer R, Karas M, Hillenkamp F, et al. (1993). Ion stability of nucleic acids in infrared matrix-assisted laser desorption/ionization mass spectrometry. Nucleic Acids Res. 21: 3347-3357. http://dx.doi.org/10.1093/nar/21.15.3347 PMid:7688451    PMCid:331430 Okita TW, Greenberg E, Kuhn DN and Preiss J (1979). Subcellular localization of the starch degradative and biosynthetic enzymes of spinach leaves. Plant Physiol. 64: 187-192. http://dx.doi.org/10.1104/pp.64.2.187 PMid:16660929    PMCid:543051 Sandstrom BE, Granstrom M and Marklund SL (1994). New roles for quin2: powerful transition-metal ion chelator that inhibits copper-, but potentiates iron-driven, Fenton-type reactions. Free Radic. Biol. Med. 16: 177-185. http://dx.doi.org/10.1016/0891-5849(94)90141-4 Shareghi B, Arabi M and Zargham M (2007). Denaturation of Bacillus amyloliquefaciens alpha-amylase with urea. Pak. J. Biol. Sci. 10: 3154-3157. http://dx.doi.org/10.3923/pjbs.2007.3154.3157 Tee BL and Kaletunc G (2009). Immobilization of a thermostable alpha-amylase by covalent binding to an alginate matrix increases high temperature usability. Biotechnol. Prog. 25: 436-445. http://dx.doi.org/10.1002/btpr.117 PMid:19353735 Xie C,Yao J,Pan R,Wu L,et al. (2003). Mutagenesis of ion beam implantation and identification of two newrifampicin resistance determining sites in rpoB gene in Escherichia coli. Wei Sheng Wu Xue Bao 43: 732-739. PMid:16276894 Yamate N and Yamazaki T (1999). Is the difference in alpha-amylase activity in the strains of Drosophila melanogaster with different allozymes due to transcriptional or posttranscriptional control? Biochem. Genet. 37: 345-356. http://dx.doi.org/10.1023/A:1018715528413 PMid:10690430