Relevant bibliographies by topics / Tubulin

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Tubulin'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 July 2025

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Journal articles on the topic "Tubulin"

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Shu, H. B., and H. C. Joshi. "Gamma-tubulin can both nucleate microtubule assembly and self-assemble into novel tubular structures in mammalian cells." Journal of Cell Biology 130, no. 5 (1995): 1137–47. http://dx.doi.org/10.1083/jcb.130.5.1137.

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alpha-, beta-, and gamma-tubulins are evolutionarily highly conserved members of the tubulin gene superfamily. While the abundant members, alpha- and beta-tubulins, constitute the building blocks of cellular microtubule polymers, gamma-tubulin is a low abundance protein which localized to the pericentriolar material and may play a role in microtubule assembly. To test whether gamma-tubulin mediates the nucleation of microtubule assembly in vivo, and co-assembles with alpha- and beta-tubulins into microtubules or self-assembles into macro-molecular structures, we experimentally elevated the exp
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Inclan, Y. F., and E. Nogales. "Structural models for the self-assembly and microtubule interactions of gamma-, delta- and epsilon-tubulin." Journal of Cell Science 114, no. 2 (2001): 413–22. http://dx.doi.org/10.1242/jcs.114.2.413.

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alphabeta-tubulin heterodimers self-assemble to form microtubules nucleated by gamma-tubulin in the cell. Gamma-tubulin is believed to recruit the alphabeta-tubulin dimers that form the minus ends of microtubules, but the molecular mechanism of this action remains a matter of heated controversy. Still less is known about the function and molecular interactions of delta-tubulin and epsilon-tubulin. delta-tubulin may seed the formation of the C triplet tubules in the basal bodies of Chlamydomonas and epsilon-tubulin is known to localize to the centrosome in a cell cycle-dependent manner. Using t
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Burke, D., P. Gasdaska, and L. Hartwell. "Dominant effects of tubulin overexpression in Saccharomyces cerevisiae." Molecular and Cellular Biology 9, no. 3 (1989): 1049–59. http://dx.doi.org/10.1128/mcb.9.3.1049-1059.1989.

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The consequences of altering the levels of alpha- and beta-tubulin in Saccharomyces cerevisiae were examined by constructing fusions of the structural genes encoding the tubulins to strong galactose-inducible promoters. Overexpression of beta-tubulin (TUB2) was lethal: cells arrested in the G2 stage of the cell cycle exhibited an increased frequency of chromosome loss, were devoid of microtubules, and accumulated beta-tubulin in a novel structure. Overexpression of the major alpha-tubulin gene (TUB1) was not lethal and did not affect chromosome segregation. The rate of alpha-tubulin mRNA and p
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Burke, D., P. Gasdaska, and L. Hartwell. "Dominant effects of tubulin overexpression in Saccharomyces cerevisiae." Molecular and Cellular Biology 9, no. 3 (1989): 1049–59. http://dx.doi.org/10.1128/mcb.9.3.1049.

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The consequences of altering the levels of alpha- and beta-tubulin in Saccharomyces cerevisiae were examined by constructing fusions of the structural genes encoding the tubulins to strong galactose-inducible promoters. Overexpression of beta-tubulin (TUB2) was lethal: cells arrested in the G2 stage of the cell cycle exhibited an increased frequency of chromosome loss, were devoid of microtubules, and accumulated beta-tubulin in a novel structure. Overexpression of the major alpha-tubulin gene (TUB1) was not lethal and did not affect chromosome segregation. The rate of alpha-tubulin mRNA and p
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Burland, T. G., E. C. Paul, M. Oetliker, and W. F. Dove. "A gene encoding the major beta tubulin of the mitotic spindle in Physarum polycephalum plasmodia." Molecular and Cellular Biology 8, no. 3 (1988): 1275–81. http://dx.doi.org/10.1128/mcb.8.3.1275-1281.1988.

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The multinucleate plasmodium of Physarum polycephalum is unusual among eucaryotic cells in that it uses tubulins only in mitotic-spindle microtubules; cytoskeletal, flagellar, and centriolar microtubules are absent in this cell type. We have identified a beta-tubulin cDNA clone, beta 105, which is shown to correspond to the transcript of the betC beta-tubulin locus and to encode beta 2 tubulin, the beta tubulin expressed specifically in the plasmodium and used exclusively in the mitotic spindle. Physarum amoebae utilize tubulins in the cytoskeleton, centrioles, and flagella, in addition to the
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Burland, T. G., E. C. Paul, M. Oetliker, and W. F. Dove. "A gene encoding the major beta tubulin of the mitotic spindle in Physarum polycephalum plasmodia." Molecular and Cellular Biology 8, no. 3 (1988): 1275–81. http://dx.doi.org/10.1128/mcb.8.3.1275.

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The multinucleate plasmodium of Physarum polycephalum is unusual among eucaryotic cells in that it uses tubulins only in mitotic-spindle microtubules; cytoskeletal, flagellar, and centriolar microtubules are absent in this cell type. We have identified a beta-tubulin cDNA clone, beta 105, which is shown to correspond to the transcript of the betC beta-tubulin locus and to encode beta 2 tubulin, the beta tubulin expressed specifically in the plasmodium and used exclusively in the mitotic spindle. Physarum amoebae utilize tubulins in the cytoskeleton, centrioles, and flagella, in addition to the
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Zhou, Yujun, Jianqiang Xu, Yuanye Zhu, Yabing Duan, and Mingguo Zhou. "Mechanism of Action of the Benzimidazole Fungicide on Fusarium graminearum: Interfering with Polymerization of Monomeric Tubulin But Not Polymerized Microtubule." Phytopathology® 106, no. 8 (2016): 807–13. http://dx.doi.org/10.1094/phyto-08-15-0186-r.

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Tubulins are the proposed target of clinically relevant anticancer drugs, anthelmintic, and fungicide. β2-tubulin of the plant pathogen Fusarium graminearum was considered as the target of benzimidazole compounds by homology modeling in our previous work. In this study, α1-, α2-, and β2-tubulin of F. graminearum were produced in Escherichia coli. Three benzimidazole compounds (carbendazim, benomyl, and thiabendazole) interacted with the recombinant β2-tubulin and reduced the maximum fluorescence intensity of 2 μM β2-tubulin 47, 50, and 25%, respectively, at saturation of compound-tubulin compl
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Rudolph, J. E., M. Kimble, H. D. Hoyle, M. A. Subler, and E. C. Raff. "Three Drosophila beta-tubulin sequences: a developmentally regulated isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-defective mutation of the testis-specific isoform (B2t8) reveal both an ancient divergence in metazoan isotypes and structural constraints for beta-tubulin function." Molecular and Cellular Biology 7, no. 6 (1987): 2231–42. http://dx.doi.org/10.1128/mcb.7.6.2231-2242.1987.

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The genomic DNA sequence and deduced amino acid sequence are presented for three Drosophila melanogaster beta-tubulins: a developmentally regulated isoform beta 3-tubulin, the wild-type testis-specific isoform beta 2-tubulin, and an ethyl methanesulfonate-induced assembly-defective mutation of the testis isoform, B2t8. The testis-specific beta 2-tubulin is highly homologous to the major vertebrate beta-tubulins, but beta 3-tubulin is considerably diverged. Comparison of the amino acid sequences of the two Drosophila isoforms to those of other beta-tubulins indicates that these two proteins are
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Rudolph, J. E., M. Kimble, H. D. Hoyle, M. A. Subler, and E. C. Raff. "Three Drosophila beta-tubulin sequences: a developmentally regulated isoform (beta 3), the testis-specific isoform (beta 2), and an assembly-defective mutation of the testis-specific isoform (B2t8) reveal both an ancient divergence in metazoan isotypes and structural constraints for beta-tubulin function." Molecular and Cellular Biology 7, no. 6 (1987): 2231–42. http://dx.doi.org/10.1128/mcb.7.6.2231.

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The genomic DNA sequence and deduced amino acid sequence are presented for three Drosophila melanogaster beta-tubulins: a developmentally regulated isoform beta 3-tubulin, the wild-type testis-specific isoform beta 2-tubulin, and an ethyl methanesulfonate-induced assembly-defective mutation of the testis isoform, B2t8. The testis-specific beta 2-tubulin is highly homologous to the major vertebrate beta-tubulins, but beta 3-tubulin is considerably diverged. Comparison of the amino acid sequences of the two Drosophila isoforms to those of other beta-tubulins indicates that these two proteins are
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Chu, Chih-Wen, Fajian Hou, Junmei Zhang та ін. "A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation". Molecular Biology of the Cell 22, № 4 (2011): 448–56. http://dx.doi.org/10.1091/mbc.e10-03-0203.

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Dynamic instability is a critical property of microtubules (MTs). By regulating the rate of tubulin polymerization and depolymerization, cells organize the MT cytoskeleton to accommodate their specific functions. Among many processes, posttranslational modifications of tubulin are implicated in regulating MT functions. Here we report a novel tubulin acetylation catalyzed by acetyltransferase San at lysine 252 (K252) of β-tubulin. This acetylation, which is also detected in vivo, is added to soluble tubulin heterodimers but not tubulins in MTs. The acetylation-mimicking K252A/Q mutants were inc
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Dissertations / Theses on the topic "Tubulin"

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Nacoulma, Aminata. "Reprogrammation métabolique induite dans les tissus hyperplasiques formés chez le tabac infecté par Rhodococcus fascians: aspects fondamentaux et applications." Doctoral thesis, Universite Libre de Bruxelles, 2013. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/209429.

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Les pathosystèmes, plante-bactérie, aboutissent souvent au niveau de la plante à de profondes reprogrammations tant au niveau de la morphogenèse que du métabolome. Dans le cas de l’interaction plante-Rhodococcus fascians, une bactérie phytopathogène, il se développe au niveau du site d’infection, une structure morphologique particulière nommée « galle feuillée ». <p>Au sein de cette hyperplasie, les altérations métaboliques induites concernent non seulement les produits du métabolisme primaire mais également le métabolisme secondaire et plus particulièrement des composés qui interviennent dans
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Mackeh, Rafah. "Mécanisme de l’hyperacétylation de la tubuline en réponse aux stress." Thesis, Paris 11, 2013. http://www.theses.fr/2013PA114852.

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Au-delà de sa présence sur les microtubules stables, l'acétylation de l’-tubuline peut être augmentée après exposition des cellules aux UV ou après une carence en nutriments, phénomène que l’on appelle « hyperacétylation ». Cependant, le mécanisme d’induction de cette hyperacétylation est encore inconnu. Dans cette étude, nous montrons que l’hyperacétylation de la tubuline est une réponse générale aux stress cellulaire, et nous avons cherché à caractériser cette réponse, à identifier la voie de signalisation activée par le stress et conduisant à cette réponse, et à étudier la signification bi
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Cao, Luyan. "bases structurales de la motilité des kinésines." Thesis, Université Paris-Saclay (ComUE), 2016. http://www.theses.fr/2016SACLS267/document.

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Les kinésines sont des protéines moteur liées au cytosquelette de microtubules. Elles convertissent l’énergie provenant de l’hydrolyse de l’ATP en un travail mécanique. Leur fonction typique est de se déplacer le long du microtubule pour véhiculer des charges. La plupart des kinésines sont des dimères. Elles comprennent un domaine moteur, qui porte à la fois les sites de liaison du nucléotide et du microtubule, un domaine intermédiaire de dimérisation et une partie dite « queue » qui confère la spécificité des charges à transporter. Mon objectif est d’établir le mécanisme moléculaire à la base
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Bladh, Håkan. "Structure-activity studies of novel colchicine analogs synthesis, conformation and tublin binding /." Lund : Lund University, 1998. http://books.google.com/books?id=1sBqAAAAMAAJ.

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Francisco, Samuel Nuno Furtado da Conceição. "Toxoplasma gondii Tubulin Cofactor B plays a key role in host cell invasion and replication." Doctoral thesis, Universidade de Lisboa, Faculdade de Medicina Vterinária, 2020. http://hdl.handle.net/10400.5/20149.

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Tese de Doutoramento em Ciências Veterinárias na Especialidade de Ciências Biológicas e Biomédicas<br>Tubulin cofactors participate in the folding, dimerization, and dissociation pathways of the tubulin dimer, being implicated in the control of tubulin proteostasis and consequently in the control of microtubule (MT) dynamics in vivo. We hypothesise that these proteins have a role in the regulation of MT cytoskeleton dynamics during Toxoplasma gondii host cell invasion. In this context, we characterized the Tubulin cofactor B (TBCB) in T. gondii. TBCB is a CAPGly domain-containing protein
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Imboden, Martin Alex. "Tubulin genes of Trypanosoma brucei /." [S.l : s.n.], 1987. http://www.ub.unibe.ch/content/bibliotheken_sammlungen/sondersammlungen/dissen_bestellformular/index_ger.html.

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Deshpande, Amit. "α-Tubulin nitrotyrosination affects cell growth and is regulated by tubulin tyrosine ligase like 12". Strasbourg, 2009. https://publication-theses.unistra.fr/restreint/theses_doctorat/2009/DESHPANDE_Amit_2009.pdf.

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Les microtubules sont un élément important du cytosquelette et de réaliser une variété de fonctions essentielles. La diversité fonctionnelle des microtubules provient de différentes diverses - et-tubuline isotypes qui sont exprimés dans la cellule, et une vaste gamme de réversibles modifications post-traductionnelles. tyrosination Tubulin est l'un de ces modifications exécutées par la tubuline tyrosine ligase (TTL). TTL est le membre fondateur du 14 tyrosine ligase membres tubuline comme (TTLL) de la famille. Wasylyk laboratoire a trouvé TTLL12 être exprimés de manière différentielle dans la t
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Karamtzioti, Paraskevi 1990. "Tubulin modifications in human gametes : from the oocytes spindle to the sperm flagellum : Characterization of tubulin post translational modifications in female meiosis and sperm pathologies." Doctoral thesis, TDX (Tesis Doctorals en Xarxa), 2021. http://hdl.handle.net/10803/670643.

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This thesis aimed to characterize the tubulin PTM profile of human oocytes and spermatozoa. Tubulin rich structures play critical roles in the cellular behavior of human gametes. Mutations in tubulin or related proteins can affect oocyte maturation and flagellum motility. We first focused on tubulin post-translational modifications (PTMs) in the oocyte spindle and sperm flagellum. We characterized the PTM spindle profile of MII oocytes cultured in vitro and matured in vivo, and compared PTM enzyme transcript levels with two additional groups: GV and failed to mature oocytes. Further determinat
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Paul, E. C. A. "The biology of tubulin in Physarum." Thesis, University of Kent, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.371147.

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Doll, John M. 1976. "Catalysis of tubulin heterodimerization in vivo." Thesis, Massachusetts Institute of Technology, 2004. http://hdl.handle.net/1721.1/32259.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2004.<br>Includes bibliographical references.<br>The heterodimerization of α- and β-tubulin represents a critical early step in microtubule morphogenesis. In vitro studies have defined a pathway that mediates the incorporation of monomeric tubulin polypeptides into heterodimer. The components of this pathway, tubulin cofactors, are dispensable for growth in Saccharomyces cerevisiae under laboratory conditions. Yet, these proteins are required for survival under conditions of stress or in the presence of a weakened tubuli
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Books on the topic "Tubulin"

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Carlomagno, Teresa, ed. Tubulin-Binding Agents. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-69039-9.

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Yamauchi, Wei. Tubulin: Structure, functions, and roles in disease. Nova Science, 2011.

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Read, M. Tubulin in the erythrocytic stages of phasmodium falciparum. UMIST, 1995.

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service), SpringerLink (Online, ed. Tubulin-binding agents: Synthetic, structural and mechanistic insights. Springer, 2009.

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Pape, Michaela. Charakterisierung des [beta]-Tubulin-Gens der kleinen Strongyliden des Pferdes. [s.n.], 1999.

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Leyland, Steven. A unique tubulin antiserum inhibits poleward chromosome movement in anaphase. National Library of Canada, 1990.

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Lamb, Jeremy Charles. Fluorescent derivatives of tubulin as probes for the analysis of microtubule dynamics. University of East Anglia, 1985.

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Poetsch, Bettina. Zur Expression und Funktion von Aktin und Tubulin in der Photomorphogenese von Physarum polycephalum. Intemann, 1989.

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Kaluzienski, Mark Henry. Changes in rat skeletal muscle phenotype following colchicine disruption of motor axonal tubulin. Laurentian University, Behavioural Neuroscience Program, 1999.

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A, Cross R., and Kendrick-Jones J, eds. Motor proteins: A volume based on the EMBO Workshop, Cambridge, September 1990. Company of Biologists, 1991.

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Book chapters on the topic "Tubulin"

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Yariv, Joseph. "Tubulin." In The Discreet Charm of Protein Binding Sites. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24996-4_2.

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Carlier, Marie-France, and Dominique Pantaloni. "Tubulin as a G-Protein: Regulation of Tubulin-Tubulin Interactions by GTP Hydrolysis." In The Guanine — Nucleotide Binding Proteins. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4757-2037-2_37.

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Stephens, R. E. "Ciliary Membrane Tubulin." In Ciliary and Flagellar Membranes. Springer US, 1990. http://dx.doi.org/10.1007/978-1-4613-0515-6_9.

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Amos, Linda A., and W. Bradshaw Amos. "Properties of Tubulin." In Molecules of the Cytoskeleton. Macmillan Education UK, 1991. http://dx.doi.org/10.1007/978-1-349-21739-7_7.

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Stearns, Tim. "The Tubulin Superfamily." In Centrosomes in Development and Disease. Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/3527603808.ch2.

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Young, David H. "Anti-tubulin Agents." In Fungicide Resistance in Plant Pathogens. Springer Japan, 2015. http://dx.doi.org/10.1007/978-4-431-55642-8_7.

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Schomburg, Dietmar, and Dörte Stephan. "Tubulin N-acetyltransferase." In Enzyme Handbook 11. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61030-1_240.

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Sebastian de Bono, Johann, Anthony W. Tolcher, and Eric K. Rowinsky. "Tubulin-Targeting Drugs." In Current Cancer Therapeutics. Current Medicine Group, 2001. http://dx.doi.org/10.1007/978-1-4613-1099-0_5.

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Miñana, Maria-Dolores, Vicente Felipo, and Santiago Grisolía. "Hyperammonemia Induces Brain Tubulin." In Advances in Experimental Medicine and Biology. Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5826-8_4.

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Breviario, Diego. "Tubulin Genes and Promotors." In Plant Microtubules. Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-662-22300-0_7.

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Conference papers on the topic "Tubulin"

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Zoghi, M., M. Batarseh, R. Wu, J. A. Tuszynski, and A. Dogariu. "Dynamics of Delayed Luminescence in Tubulin and Microtubule Constructs: an Insight into Collective Radiative Effects." In Bio-Optics: Design and Application. Optica Publishing Group, 2025. https://doi.org/10.1364/boda.2025.dtu1a.5.

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We report, for the first time, measurements of delayed luminescence on tubulin constructs. The results demonstrate the role of mesoscopic structure on emission strength and decay dynamics, which provides a new perspective on radiative phenomena.
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Deriu, Marco A., Søren Enemark, Emiliano Votta, Franco M. Montevecchi, Alberto Redaelli, and Monica Soncini. "Bottom-Up Mesoscale Model of Microtubule." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176115.

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Microtubules (MTs) are fundamental structural elements in the cytoskeleton of all eukaryotic cells. The MTs are hollow cylinder-shaped biopolymers with inner and outer diameter of about 18 and 30 nm respectively and length ranging from 1 to 10 μm. They are constituted by αβ-tubulins arranged in protofilaments with head-to-tail motif. The protofilaments bind together laterally along the MT’s long axis with a slight shift generating a spiral with a pitch of 2, 3 or 4 monomers’ length [1]. The building-block of the MT, αβ-tubulin, is a hetero-dimer made of two globular monomers, α- and β-tubulin.
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Deriu, Marco A., Monica Soncini, Mario Orsi, et al. "Elastic Network Normal Mode Analysis for Microtubule Mechanics." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206618.

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The cellular microtubules MTs are hollow cylinder-shaped biopolymers with inner and outer diameter of about 17 and 25 nm and length ranging from 1 to 10 μm. They are constituted by αβ-tubulins arranged in protofilaments with a head-to-tail motif [1]. The protofilaments bind together laterally along the MT’s long axis with a slight shift generating a spiral with a pitch of 2, 3 or 4 monomers’ length (Fig.1a). The building-block of the MT, the αβ-tubulin, is a hetero-dimer made of two globular monomers, α- and β-tubulin, each of them consisting of about 450 residues with high degree of sequence
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Sheldon, Kely L., and Dan L. Sackett. "Abstract 3044: The ability of tubulin to close mitochondrial VDAC pores depends on beta tubulin isotype." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-3044.

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Yang, Chia-Ping H., та Susan B. Horwitz. "Abstract 664: Polymerization of human βIII-tubulin is distinct from βI-tubulin in a cell-free system". У Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-664.

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Ringel, Israel, Varda Gottfried, Lila Levdansky, James W. Winkelman, and Sol Kimel. "Photodynamic activity of porphines on tubulin assembly." In BiOS Europe '95, edited by Benjamin Ehrenberg, Giulio Jori, and Johan Moan. SPIE, 1996. http://dx.doi.org/10.1117/12.230982.

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Cifra, Michal, and Saurabh Kumar Pandey. "SubTHz absorption spectra of vibration modes of tubulin." In 4th URSI Atlantic RadioScience Conference. URSI – International Union of Radio Science, 2024. http://dx.doi.org/10.46620/ursiatrasc24/itop5460.

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Enemark, So̸ren, Marco A. Deriu, and Monica Soncini. "Mechanical Properties of Tubulin Molecules by Molecular Dynamics Simulations." In ASME 8th Biennial Conference on Engineering Systems Design and Analysis. ASMEDC, 2006. http://dx.doi.org/10.1115/esda2006-95674.

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The basic unit in microtubules is αβ-tubulin, a hetero-dimer consisting of an α- and a β-tubulin monomer. The mechanical characteristics of the dimer as well as of the individual monomers may be used to obtain new insight into the microtubule tensile properties. In the present work we evaluate the elastic constants of each of the monomers and the interaction force between them by means of molecular dynamics simulations. Molecular models of α-, β-, and αβ-tubulin were developed starting from the 1TUB.pdb structure from the RSCB database. Simulations were carried out in a solvated environment us
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Sackett, Dan L., and Adrian Begaye. "Abstract 1219: Tubulin binding to mitochondrial VDAC: A new regulator of oxidative metabolism and apoptosis? A new role for tubulin." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1219.

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Tamura, Daisuke, Tokuzo Arao, Tomoyuki Nagai, et al. "Slug Increases Sensitivity To Tubulin Binding Agents Via The Downregulation Of Beta III And IVa-Tubulin In Lung Cancer Cells." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a6284.

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Reports on the topic "Tubulin"

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Banerjee, Asok. Characterization of Tubulin Isoforms in Breast Cancer. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada393136.

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2

Banerjee, Asok. Characterization of Tubulin Isoforms in Breast Cancer. Defense Technical Information Center, 1999. http://dx.doi.org/10.21236/ada381325.

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3

Yang, KyoungLang, and Gunda I. Georg. Synthesis of Cryptophycin Affinity Labels and Tubulin Labeling. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada443679.

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4

Banerjee, Asok. Characterization of Tubulin Isoforms in Breast Cancer Cells. Defense Technical Information Center, 2001. http://dx.doi.org/10.21236/ada395082.

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Yang, Kyounglang, and AGunda I. Georg. Synthesis of Cryptophycin Affinity Labels and Tubulin Labeling. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada432471.

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Ramadas, Vidya. Synthesis of Cryptophycin Affinity Labels and Tubulin Labeling. Defense Technical Information Center, 2003. http://dx.doi.org/10.21236/ada416994.

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7

Luduena, Richard. Nuclear Tubulin: A Novel for Breast Cancer Chemotherapy. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada392981.

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8

Yang, KyoungLang, and Gunda I. Georg. Synthesis of Cryptophycin Affinity Labels and Tubulin Labeling. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada474734.

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9

Susan M. Wick. Growth and development of maize that contains mutant tubulin genes. Office of Scientific and Technical Information (OSTI), 2004. http://dx.doi.org/10.2172/826290.

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Luduena, Richard F. The Role of Nuclear Beta II-Tubulin in Breast Cancer Cells. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada405620.

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