中国生物工程杂志

[1] Xu Z D, Wu Q. Research progress in tubulin. J Anhui Instit Edu, 1999,2(86):73-74.
[2] Zhou H T, Xu L, Zhen W Z, et al. Research on relationship between α-tubulin and cutoplasmic male sterility in Maize. J Xianmen U(Natural Sci), 2003,42(1):107-111.
[3] Zhao J L, Zhao Z J, Zhang H. Relationship between freezing tolerance of root-tip cells and cold stability of microtubules and tubulin in cucumber. J Hebei U(Natural Sci), 2006,26(2):188-192.
[4] Yang Y, Wang B H, Li Z F, et al. The polymerization and denaturation of brain tubulin and the effect of taxol by differential scanning calorimetry. Acta Physico-Chimica Sinica, 1999,15(2):182-185.
[5] Shan S, Yan H, Li C, et al. Primary expression analysis of differential genes in peanut seed capsule with resistance to A. flavus. J Peanut Sci, 2005,34(4): 21-24.
[6] Hegde R S, Kang S. The concept of translocational regulation. J Cell Biol, 2008, 182(2): 225-232.
[7] Powers T, Walter D P. Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor. EMBO J, 1997, 16(16): 4880-4886.
[8] Mandon E C, Jiang Y, Gilmore R. Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum. J Cell Biol, 2003, 162(4): 575-585.
[9] Herskovits A A, Seluanov A, Rajsbaum R, et al. Evidence for coupling of membrane targeting and function of the signal recognition particle (SRP) receptor FtsY. EMBO Report, 2001, 2(11): 1040-1046.
[10] Jiang Y, Cheng Z, Mandon E C, et al. An interaction between the SRP receptor and the translocon is critical during co-translational protein translocation. J Cell Biol, 2008, 180(6): 1149-1161.
[11] Zhang X, Kung S, Shan S. Demonstration of a multi-step mechanism for assembly of the SRP-SRP Receptor complex: implications for the catalytic role of SRP RNA. Journal of Mol Biol, 2008, 381(3): 581-593.
[12] Young J C, Andrews D W. The Signal recognition particle receptor alpha subunit assembles co-translationally on the endoplasmic reticulum membrane during an mRNA-encoded translation pause in vitro. EMBO J, 1996, 15(1): 172-181.
[13] Bürk J, Weiche B, Wenk M, et al. Depletion of the signal recognition particle receptor inactivates ribosomes in Escherichia coli. J Bacteriol, 2009, 191(22): 7017-7026.
[14] Ogg S C, Poritz M A, Walter P. Signal Recognition Particle receptor is important for cell growth and protein secretion in Saccharomyces cerevisiae. Mol Biol Cell, 1992, 3(8): 895-911.
[15] Maruyama N, Mun L C, Tatsuhara M, et al. Multiple vacuolar sorting determinants exist in soybean 11S globulin. Plant Cell, 2006,18(5): 1253-1273.
[16] Zong C. Study of Aspergillus flavus resistance genes in developing peanut. Wuhan: South-Central University for Nationalities, College of life sciences, 2010.
[17] Yan H Y, Ding Y, Wu Y X. Laboratory manual for molecular biology and genomic engineering. Wuhan: Wuhan University Publisher, 2009.18-41.
[18] Yan H Y, Zong C Z, Bao W Z, et al. Relationship between peanut Aspergillus flavus resistance and glycogen synthase kinase-3. Acta Agriculturae Boreali-sinica,2011,26 (5):1-4.
[19] Yan H Y, Zong C Z, Jing C H, et al. Analysis of relativity of receptor-like kinase to Aspergillus flavus resistance in peanut. Acta Agriculturae Boreali-sinica,2011,26 (4):198-201.
[20] Ji R C, Tang Z X, Li G X, et al. Determination of resistance to Aspergillus flavus and productivity of five peanut cultivars. Fujian Agri Sci Technol, 2000,(3):10-11.
[21] Zhou G Y, Liang X Q, Li Y C, et al. Evaluation and application of introduced peanut cultivars for resistance to Aspergillus flavus. J Peanut Sci, 2002,31(2):14-17.
[22] Liang X, Zhou G, Pan R. Wax and curticle of peanut seed coat in relation to infection and aflatoxin production by Aspergillus flavus. J Trop Subtrop Bot, 2003, 11(1): 11-14.
[23] Yan H Y, Zong C Z, Ma G H,et al. Relationship between ribosome protein L41 and resistance to Aspergillus flavus. Acta Agriculturae Boreali-sinica,2011,26(6):16-19.
[24] Scales T M E, Lin S, Kraus M, et al. Nonprimed and DYRK1A-primed GSK3β-phosphorylation sites on MAP1B regulate microtubule dynamics in growing axons. J Cell Sci, 2009, 122(14): 2424-2435.
[25] Wang S, Huang J, He J, et al. RPL41, a small ribosomal peptide deregulated in tumors, is essential for mitosis and centrosome integrity. Neoplasia, 2010,12(3): 284-293.
[26] Ferralli J, Ashby J, Fasler M, et al. Disruption of microtubule organization and centrosome function by expression of tobacco mosaic virus movement protein. J Virol, 2006,80(12): 5807-5821.
[27] Morrissette N S, Mitra A, Sept D, et al. Dinitroanilines bind α-tubulin to disrupt microtubules. Mol Biol of the Cell, 2004,15(4):1960-1968.
[28] Ma C, Li C, Ganesan L, et al. Mutations in α-tubulin confer dinitroaniline resistance at a cost to microtubule function. Molecular Biol Cell, 2007, 18(12):4711-4720.
[29] Migliaccio G, Nicchitta C V, Blobel G. The signal sequence receptor, unlike the Signal Recognition Particle receptor, is not essential for protein translocation. J Cell Biol, 1992, 117(1): 15-25.
[30] Friedman J R, Webster B M, Mastronarde D N, et al. ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules. J Cell Biol, 2010,190(3): 363-375.
[31] Liang X Q, Pan R Z, Bin J H. Research progress in mechanism of A. flavus resistance of peanut. Chinese J Oil Crop Sci, 2000,22(3):77-80.
[32] Zhou G, Liang X, Li Y, et al. Comparative study on seed coat ultrastructure of resistant and susceptible varieties to Aspergillus flavas in peanut. Chinese J of Oil Crop, 1999,17(1):43-53.
[33] Guo B, Chen X, Dang P, et al. Peanut gene expression profiling in developing seeds at different reproduction stages during Aspergillus parasiticus infection. BMC Dev Biol, 2008, 8(2): 12-27.
[34] Liang X, Pan R, Zhou G. Relation of trypsin inhibitor in peanut seed and resistance to Aspergillus Flavus invasion. Acta Agro Sinica, 2003, 29(2): 295-299.