Journal articles on the topic 'Tubuline-B'
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Živković, S., V. Gavrilović, T. Popović, N. Dolovac, and N. Trkulja. "First Report of Colletotrichum clavatum Causing Quince Anthracnose in Serbia." Plant Disease 98, no. 9 (2014): 1272. http://dx.doi.org/10.1094/pdis-01-14-0052-pdn.
Full textZhu, Yuanye, Xiaoyu Liang, Yanjun Li та ін. "F240 of β2-Tubulin Explains why Fusarium graminearum is Less Sensitive to Carbendazim than Botrytis cinerea". Phytopathology® 108, № 3 (2018): 352–61. http://dx.doi.org/10.1094/phyto-09-17-0295-r.
Full textVogel, Jacalyn M., Tim Stearns, Conly L. Rieder та Robert E. Palazzo. "Centrosomes Isolated from Spisula solidissima Oocytes Contain Rings and an Unusual Stoichiometric Ratio of α/β Tubulin". Journal of Cell Biology 137, № 1 (1997): 193–202. http://dx.doi.org/10.1083/jcb.137.1.193.
Full textGaertig, J., M. A. Cruz, J. Bowen, L. Gu, D. G. Pennock, and M. A. Gorovsky. "Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila." Journal of Cell Biology 129, no. 5 (1995): 1301–10. http://dx.doi.org/10.1083/jcb.129.5.1301.
Full textTian, Guoling, Sally A. Lewis, Becket Feierbach, et al. "Tubulin Subunits Exist in an Activated Conformational State Generated and Maintained by Protein Cofactors." Journal of Cell Biology 138, no. 4 (1997): 821–32. http://dx.doi.org/10.1083/jcb.138.4.821.
Full textBaffet, Alexandre D., Béatrice Benoit, Jens Januschke, et al. "Drosophila tubulin-binding cofactor B is required for microtubule network formation and for cell polarity." Molecular Biology of the Cell 23, no. 18 (2012): 3591–601. http://dx.doi.org/10.1091/mbc.e11-07-0633.
Full textGu, W., S. A. Lewis, and N. J. Cowan. "Generation of antisera that discriminate among mammalian alpha-tubulins: introduction of specialized isotypes into cultured cells results in their coassembly without disruption of normal microtubule function." Journal of Cell Biology 106, no. 6 (1988): 2011–22. http://dx.doi.org/10.1083/jcb.106.6.2011.
Full textPiperno, G., and M. T. Fuller. "Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms." Journal of Cell Biology 101, no. 6 (1985): 2085–94. http://dx.doi.org/10.1083/jcb.101.6.2085.
Full textUthman, Aumaid U. "Identification and Molecular Characterization of B-Tubulin Gene from Dermatophyte Pathogen Microsporum Canis." Journal of Zankoy Sulaimani - Part A 10, no. 1 (2007): 1–8. http://dx.doi.org/10.17656/jzs.10157.
Full textGeuens, G., A. M. Hill, N. Levilliers, A. Adoutte, and M. DeBrabander. "Microtubule dynamics investigated by microinjection of Paramecium axonemal tubulin: lack of nucleation but proximal assembly of microtubules at the kinetochore during prometaphase." Journal of Cell Biology 108, no. 3 (1989): 939–53. http://dx.doi.org/10.1083/jcb.108.3.939.
Full textPiperno, G., M. LeDizet, and X. J. Chang. "Microtubules containing acetylated alpha-tubulin in mammalian cells in culture." Journal of Cell Biology 104, no. 2 (1987): 289–302. http://dx.doi.org/10.1083/jcb.104.2.289.
Full textSamson-Himmelstjerna, G. von. "Anthelminthika-Resistenzen bei Pferde- und Wiederkäuerhelminthen: neueste Forschungsergebnisse aus molekularbiologischer Sicht." Tierärztliche Praxis Ausgabe G: Großtiere / Nutztiere 32, no. 06 (2004): 312–15. http://dx.doi.org/10.1055/s-0038-1623506.
Full textMartin-Galiano, Antonio J., María A. Oliva, Laura Sanz, et al. "Bacterial Tubulin Distinct Loop Sequences and Primitive Assembly Properties Support Its Origin from a Eukaryotic Tubulin Ancestor." Journal of Biological Chemistry 286, no. 22 (2011): 19789–803. http://dx.doi.org/10.1074/jbc.m111.230094.
Full textDhonukshe, Pankaj, Bastiaan O. R. Bargmann та Theodorus W. J. Gadella. "Arabidopsis Tubulin Folding Cofactor B Interacts with α-Tubulin In Vivo". Plant and Cell Physiology 47, № 10 (2006): 1406–11. http://dx.doi.org/10.1093/pcp/pcl001.
Full textJohnson, K. A. "The axonemal microtubules of the Chlamydomonas flagellum differ in tubulin isoform content." Journal of Cell Science 111, no. 3 (1998): 313–20. http://dx.doi.org/10.1242/jcs.111.3.313.
Full textAillaud, Chrystelle, Christophe Bosc, Yasmina Saoudi та ін. "Evidence for new C-terminally truncated variants of α- and β-tubulins". Molecular Biology of the Cell 27, № 4 (2016): 640–53. http://dx.doi.org/10.1091/mbc.e15-03-0137.
Full textFeierbach, Becket, Eva Nogales, Kenneth H. Downing та Tim Stearns. "Alf1p, a CLIP-170 Domain-containing Protein, Is Functionally and Physically Associated with α-Tubulin". Journal of Cell Biology 144, № 1 (1999): 113–24. http://dx.doi.org/10.1083/jcb.144.1.113.
Full textFaruki, S., R. L. Geahlen, and D. J. Asai. "Syk-dependent phosphorylation of microtubules in activated B-lymphocytes." Journal of Cell Science 113, no. 14 (2000): 2557–65. http://dx.doi.org/10.1242/jcs.113.14.2557.
Full textSchlieper, D., and J. Löwe. "Bacterial tubulin BtubA/B: a folding mystery." Acta Crystallographica Section A Foundations of Crystallography 62, a1 (2006): s24. http://dx.doi.org/10.1107/s0108767306099521.
Full textLuduen̄a, Richard F., Mary Carmen Roach, Veena Prasad, and George R. Pettit. "Interaction of halichondrin B and homohalichondrin B with bovine brain tubulin." Biochemical Pharmacology 45, no. 2 (1993): 421–27. http://dx.doi.org/10.1016/0006-2952(93)90079-c.
Full textRaff, J. W., D. R. Kellogg, and B. M. Alberts. "Drosophila gamma-tubulin is part of a complex containing two previously identified centrosomal MAPs." Journal of Cell Biology 121, no. 4 (1993): 823–35. http://dx.doi.org/10.1083/jcb.121.4.823.
Full textINABA, KAZUO, KOUSAKU OHKAWA, and MASAAKI MORISAWA. "IDENTIFICATION OF TUBULINS ASSOCIATED WITH THE 950 KDA PROTEASE FROM SALMON SPERM ." Biomedical Research 17, no. 1 (1996): 87–93. http://dx.doi.org/10.2220/biomedres.17.87.
Full textBai, Ruoli, Tam Luong Nguyen, James C. Burnett, et al. "Interactions of Halichondrin B and Eribulin with Tubulin." Journal of Chemical Information and Modeling 51, no. 6 (2011): 1393–404. http://dx.doi.org/10.1021/ci200077t.
Full textSong, Y. H., and E. Mandelkow. "The anatomy of flagellar microtubules: polarity, seam, junctions, and lattice." Journal of Cell Biology 128, no. 1 (1995): 81–94. http://dx.doi.org/10.1083/jcb.128.1.81.
Full textVinnik, Yuriy, Yulia Belevtsova, and Marina Sadchikova. "PROSPECTS FOR INCREASING THE EFFICIENCY OF TREATMENT OF PATIENTS HEAVING OF LOCALLY- DISTRIBUTED BREAST CANCER." EUREKA: Health Sciences 3 (May 31, 2020): 6–12. http://dx.doi.org/10.21303/2504-5679.2020.001286.
Full textVee, S., L. Lafanechere, D. Fisher, J. Wehland, D. Job, and A. Picard. "Evidence for a role of the (alpha)-tubulin C terminus in the regulation of cyclin B synthesis in developing oocytes." Journal of Cell Science 114, no. 5 (2001): 887–98. http://dx.doi.org/10.1242/jcs.114.5.887.
Full textSaxton, W. M., and J. R. McIntosh. "Interzone microtubule behavior in late anaphase and telophase spindles." Journal of Cell Biology 105, no. 2 (1987): 875–86. http://dx.doi.org/10.1083/jcb.105.2.875.
Full textBudiapsari, Putu Indah, I. Kadek Swastika, and Sri Masyeni. "Prevalence of Soil-transmitted Helminths Infection in Students of Klungkung, Bali, after Mass Treatment with AlbendazolePrevalence of Soil-transmitted Helminths Infection in Students of Klungkung, Bali, after Mass Treatment with Albendazole." Open Access Macedonian Journal of Medical Sciences 9, A (2021): 433–39. http://dx.doi.org/10.3889/oamjms.2021.6266.
Full textSchmidt-Cernohorska, M., I. Zhernov, E. Steib, et al. "Flagellar microtubule doublet assembly in vitro reveals a regulatory role of tubulin C-terminal tails." Science 363, no. 6424 (2019): 285–88. http://dx.doi.org/10.1126/science.aav2567.
Full textPyles, Erica A., and Susan Bane Hastie. "Role of the B-ring substituent in the fluorescence of colchicinoid-tubulin and allocolchicinoid-tubulin complexes." Biochemistry 31, no. 31 (1992): 7086–93. http://dx.doi.org/10.1021/bi00146a009.
Full textBuendia, B., G. Draetta, and E. Karsenti. "Regulation of the microtubule nucleating activity of centrosomes in Xenopus egg extracts: role of cyclin A-associated protein kinase." Journal of Cell Biology 116, no. 6 (1992): 1431–42. http://dx.doi.org/10.1083/jcb.116.6.1431.
Full textKikkawa, M., T. Ishikawa, T. Nakata, T. Wakabayashi, and N. Hirokawa. "Direct visualization of the microtubule lattice seam both in vitro and in vivo." Journal of Cell Biology 127, no. 6 (1994): 1965–71. http://dx.doi.org/10.1083/jcb.127.6.1965.
Full textSilverman-Gavrila, R. V., and A. Forer. "Evidence that actin and myosin are involved in the poleward flux of tubulin in metaphase kinetochore microtubules of crane-fly spermatocytes." Journal of Cell Science 113, no. 4 (2000): 597–609. http://dx.doi.org/10.1242/jcs.113.4.597.
Full textKrólewska-Golińska, Karolina, Marcin J. Cieślak, Milena Sobczak, et al. "Novel Benzo[B]Furans with Anti-Microtubule Activity Upregulate Expression of Apoptotic Genes and Arrest Leukemia Cells in G2/M Phase." Anti-Cancer Agents in Medicinal Chemistry 19, no. 3 (2019): 375–88. http://dx.doi.org/10.2174/1871520619666181122123552.
Full textShpetner, H. S., B. M. Paschal, and R. B. Vallee. "Characterization of the microtubule-activated ATPase of brain cytoplasmic dynein (MAP 1C)." Journal of Cell Biology 107, no. 3 (1988): 1001–9. http://dx.doi.org/10.1083/jcb.107.3.1001.
Full textLarsson, Niklas, Bo Segerman, Bonnie Howell, Kajsa Fridell, Lynne Cassimeris, and Martin Gullberg. "Op18/Stathmin Mediates Multiple Region-Specific Tubulin and Microtubule-Regulating Activities." Journal of Cell Biology 146, no. 6 (1999): 1289–302. http://dx.doi.org/10.1083/jcb.146.6.1289.
Full textBlume, R. Ya, A. N. Rabokon та Ya V. Pirko. "β-tubulin intron length polymorphism among forms var. glabra and var. laxa of napa cabbage". Faktori eksperimental'noi evolucii organizmiv 26 (1 вересня 2020): 87–92. http://dx.doi.org/10.7124/feeo.v26.1247.
Full textWaterhouse, N. J., J. Oliaro та M. J. Pinkoski. "A ‘polarized’ look at α-tubulin cleavage by granzyme B". Cell Death & Differentiation 13, № 11 (2006): 1839–41. http://dx.doi.org/10.1038/sj.cdd.4402023.
Full textOta, Shintaro, Shougo Tomioka, Haruki Sogawa, et al. "Binding properties between curcumin and malarial tubulin: molecular-docking and ab initio fragment molecular orbital calculations." Chem-Bio Informatics Journal 18 (2018): 44–57. http://dx.doi.org/10.1273/cbij.18.44.
Full textBoyé, O., A. Brossi, H. J. C. Yeh, E. Hamel, B. Wegrzynski, and V. Toome. "Natural products. Antitubulin effect of congeners of N-acetylcolchinyl methyl ether: synthesis of optically active 5-acetamidodeaminocolchinyl methyl ether and of demethoxy analogues of deaminocolchinyl methyl ether." Canadian Journal of Chemistry 70, no. 5 (1992): 1237–49. http://dx.doi.org/10.1139/v92-160.
Full textAl-Karmalawy, Ahmed A., and Muhammad Khattab. "Molecular modelling of mebendazole polymorphs as a potential colchicine binding site inhibitor." New Journal of Chemistry 44, no. 33 (2020): 13990–96. http://dx.doi.org/10.1039/d0nj02844d.
Full textOlenieva, V. D., D. I. Lytvyn, A. I. Yemets, and Ya B. Blume. "Expression profiling of kinesins, involved in the development of autophagy in Arabidopsis thaliana, and the role of tubulin acetylation in the interaction of Atg8 protein with microtubules." Faktori eksperimental'noi evolucii organizmiv 22 (September 9, 2018): 162–68. http://dx.doi.org/10.7124/feeo.v22.942.
Full textPathak, Narendra, Tomoko Obara, Steve Mangos, Yan Liu, and Iain A. Drummond. "The Zebrafish fleer Gene Encodes an Essential Regulator of Cilia Tubulin Polyglutamylation." Molecular Biology of the Cell 18, no. 11 (2007): 4353–64. http://dx.doi.org/10.1091/mbc.e07-06-0537.
Full textOegema, Karen, Christiane Wiese, Ona C. Martin та ін. "Characterization of Two Related Drosophila γ-tubulin Complexes that Differ in Their Ability to Nucleate Microtubules". Journal of Cell Biology 144, № 4 (1999): 721–33. http://dx.doi.org/10.1083/jcb.144.4.721.
Full textCaron, J. M., A. L. Jones, and M. W. Kirschner. "Autoregulation of tubulin synthesis in hepatocytes and fibroblasts." Journal of Cell Biology 101, no. 5 (1985): 1763–72. http://dx.doi.org/10.1083/jcb.101.5.1763.
Full textWang, Xiaojuan, Mine Tanaka, Herbenya Silva Peixoto, and Michael Wink. "Cucurbitacins: elucidation of their interactions with the cytoskeleton." PeerJ 5 (May 30, 2017): e3357. http://dx.doi.org/10.7717/peerj.3357.
Full textIto, Yuko, Akiko Kanamaru, and Akihiro Tada. "A novel agent, methylophiopogonanone B, promotes Rho activation and tubulin depolymerization." Molecular and Cellular Biochemistry 297, no. 1-2 (2006): 121–29. http://dx.doi.org/10.1007/s11010-006-9336-y.
Full textSchlieper, D., M. A. Oliva, J. M. Andreu, and J. Lowe. "Structure of bacterial tubulin BtubA/B: Evidence for horizontal gene transfer." Proceedings of the National Academy of Sciences 102, no. 26 (2005): 9170–75. http://dx.doi.org/10.1073/pnas.0502859102.
Full textSarkar, Taradas, Tam Luong Nguyen, Zhi-Wei Su, et al. "Interaction of pseudolaric acid B with the colchicine site of tubulin." Biochemical Pharmacology 84, no. 4 (2012): 444–50. http://dx.doi.org/10.1016/j.bcp.2012.05.014.
Full textTong, Yun-Guang, Xiong-Wen Zhang, Mei-Yu Geng, et al. "Pseudolarix Acid B, a New Tubulin-Binding Agent, Inhibits Angiogenesis by Interacting with a Novel Binding Site on Tubulin." Molecular Pharmacology 69, no. 4 (2006): 1226–33. http://dx.doi.org/10.1124/mol.105.020537.
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