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“imDC: an ensemble learning method for imbalanced classification with miRNA data”, vol. 14, pp. 123-133, 2015.
, , “cDNA cloning and characterization of two trehalases from Spodoptera litura (Lepidoptera; Noctuidade)”, vol. 12, pp. 901-915, 2013.
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http://dx.doi.org/10.1371/journal.pone.0010133
PMid:20405036 PMCid:2853572
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http://dx.doi.org/10.1126/science.223.4637.701
PMid:17841031
Davidson P and Sun WQ (2001). Effect of sucrose/raffinose mass ratios on the stability of co-lyophilized protein during storage above the Tg. Pharm. Res. 18: 474-479.
http://dx.doi.org/10.1023/A:1011002326825
PMid:11451034
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http://dx.doi.org/10.1016/j.pep.2008.11.010
PMid:19073263
Elbein AD, Pan YT, Pastuszak I and Carroll D (2003). New insights on trehalose: a multifunctional molecule. Glycobiology 13: 17R-27R.
http://dx.doi.org/10.1093/glycob/cwg047
PMid:12626396
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http://dx.doi.org/10.1016/0304-4165(93)90040-F
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http://dx.doi.org/10.1016/j.febslet.2007.07.036
PMid:17673210
Kamimura M, Takahashi M, Tomita S, Fujiwara H, et al. (1999). Expression of ecdysone receptor isoforms and trehalase in the anterior silk gland of Bombyx mori during an extra larval molt and precocious pupation induced by 20-hydroxyecdysone administration. Arch. Insect Biochem. Physiol. 41: 79-88.
http://dx.doi.org/10.1002/(SICI)1520-6327(1999)41:2<79::AID-ARCH4>3.0.CO;2-7
Lee JH, Tsuji M, Nakamura M, Nishimoto M, et al. (2001). Purification and identification of the essential ionizable groups of honeybee, Apis mellifera L., trehalase. Biosci. Biotechnol. Biochem. 65: 2657-2665.
http://dx.doi.org/10.1271/bbb.65.2657
PMid:11826961
Lee JH, Saito S, Mori H, Nishimoto M, et al. (2007). Molecular cloning of cDNA for trehalase from the European honeybee, Apis mellifera L., and its heterologous expression in Pichia pastoris. Biosci. Biotechnol. Biochem. 71: 2256-2265.
http://dx.doi.org/10.1271/bbb.70239
PMid:17827701
Mariano AC, Santos R, Gonzalez MS, Feder D, et al. (2009). Synthesis and mobilization of glycogen and trehalose in adult male Rhodnius prolixus. Arch. Insect Biochem. Physiol. 72: 1-15.
http://dx.doi.org/10.1002/arch.20319
PMid:19514081
Mitsumasu K, Azuma M, Niimi T, Yamashita O, et al. (2005). Membrane-penetrating trehalase from silkworm Bombyx mori. Molecular cloning and localization in larval midgut. Insect Mol. Biol. 14: 501-508.
http://dx.doi.org/10.1111/j.1365-2583.2005.00581.x
PMid:16164606
Mitsumasu K, Azuma M, Niimi T, Yamashita O, et al. (2008). Changes in the expression of soluble and integral-membrane trehalases in the midgut during metamorphosis in Bombyx mori. Zoolog. Sci. 25: 693-698.
http://dx.doi.org/10.2108/zsj.25.693
PMid:18828655
Parkinson NM, Conyers CM, Keen JN, MacNicoll AD, et al. (2003). cDNAs encoding large venom proteins from the parasitoid wasp Pimpla hypochondriaca identified by random sequence analysis. Comp. Biochem. Physiol. C. Toxicol. Pharmacol. 134: 513-520.
http://dx.doi.org/10.1016/S1532-0456(03)00041-3
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http://dx.doi.org/10.1016/S0965-1748(97)00059-3
Silva MC, Terra WR and Ferreira C (2010). The catalytic and other residues essential for the activity of the midgut trehalase from Spodoptera frugiperda. Insect Biochem. Mol. Biol. 40: 733-741.
http://dx.doi.org/10.1016/j.ibmb.2010.07.006
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http://dx.doi.org/10.1186/1471-2199-9-51
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Tatun N, Singtripop T, Tungjitwitayakul J and Sakurai S (2008). Regulation of soluble and membrane-bound trehalase activity and expression of the enzyme in the larval midgut of the bamboo borer Omphisa fuscidentalis. Insect Biochem. Mol. Biol. 38: 788-795.
http://dx.doi.org/10.1016/j.ibmb.2008.05.003
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http://dx.doi.org/10.1016/j.jbiosc.2010.08.020
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http://dx.doi.org/10.1242/jeb.00217
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Yamoah E, Jones EE, Weld RJ, Suckling DM, et al. (2008). Microbial population and diversity on the exoskeletons of 4 insect species associated with gorse (Ulex europaeus L.). Aust. J. Entomol. 47: 370-379.
http://dx.doi.org/10.1111/j.1440-6055.2008.00655.x
“Benchmark comparison of ab initio microRNA identification methods and software”, vol. 11, pp. 4525-4538, 2012.
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http://dx.doi.org/10.1093/bioinformatics/btp107
PMid:19233894
Bentwich I, Avniel A, Karov Y, Aharonov R, et al. (2005). Identification of hundreds of conserved and nonconserved human microRNAs. Nat. Genet. 37: 766-770.
http://dx.doi.org/10.1038/ng1590
PMid:15965474
Borchert GM, Lanier W and Davidson BL (2006). RNA polymerase III transcribes human microRNAs. Nat. Struct. Mol. Biol. 13: 1097-1101.
http://dx.doi.org/10.1038/nsmb1167
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PMid:19433510 PMCid:2703919
Hofacker IL (2003). Vienna RNA secondary structure server. Nucleic Acids Res. 31: 3429-3431.
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Huang Y, Shen XJ, Zou Q, Wang SP, et al. (2011a). Biological functions of microRNAs: a review. J. Physiol. Biochem. 67: 129-139.
http://dx.doi.org/10.1007/s13105-010-0050-6
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Huang Y, Zou Q, Wang SP, Tang SM, et al. (2011b). The discovery approaches and detection methods of microRNAs. Mol. Biol. Rep. 38: 4125-4135.
http://dx.doi.org/10.1007/s11033-010-0532-1
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Jiang P, Wu H, Wang W, Ma W, et al. (2007). MiPred: classification of real and pseudo microRNA precursors using random forest prediction model with combined features. Nucleic Acids Res. 35: W339-W344.
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Kumar S, Ansari FA and Scaria V (2009). Prediction of viral microRNA precursors based on human microRNA precursor sequence and structural features. Virol. J. 6: 129.
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“Improved method for predicting protein fold patterns with ensemble classifiers”, vol. 11, pp. 174-181, 2012.
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