Publications
Found 19 results
Filters: Author is X.Y. Li [Clear All Filters]
, ,
“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.
, “Antibody study in canine distemper virus nucleocapsid protein gene-immunized mice”, vol. 14, pp. 3098-3105, 2015.
, “Association between methionine synthase reductase A66G polymorphism and primary infertility in Chinese males”, vol. 14, pp. 3491-3500, 2015.
, “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.
, “Eosinophil cationic protein mRNA expression in children with bronchial asthma”, vol. 14, pp. 14279-14285, 2015.
, “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.
, “Pre-B-cell colony-enhancing factor is markedly elevated in childhood hemophagocytic lymphohistiocytosis”, vol. 14, pp. 5287-5295, 2015.
, “Stripe rust resistance and dough quality of new wheat - Dasypyrum villosum translocation lines”, vol. 14, pp. 8077-8083, 2015.
, “Tissue culture characteristics of maize (Zea mays L.) haploid coleoptile sections”, vol. 14, pp. 16265-16275, 2015.
, “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.
, “Correlation analysis between starch properties and single nucleotide polymorphisms of waxy genes in common rye (Secale cereale L.)”, vol. 13, pp. 2574-2589, 2014.
, , , , ,
“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
“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