Publications
Found 5 results
Filters: Author is J.L. Zhang [Clear All Filters]
, “Effects of intravenous analgesia with combined dezocine and butorphanol on postoperative cognitive function in elderly patients”, vol. 14, pp. 5571-5576, 2015.
, “Investigation of genes in chronic and acute morphine-treated mice using microarray datasets”, vol. 14, pp. 10193-10205, 2015.
, “Meloxicam increases intracellular accumulation of doxorubicin via downregulation of multidrug resistance-associated protein 1 (MRP1) in A549 cells”, vol. 14, pp. 14548-14560, 2015.
, “MicroRNA-122 is involved in oxidative stress in isoniazid-induced liver injury in mice”, vol. 14, pp. 13258-13265, 2015.
, “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