Relevant bibliographies by topics / Tubulins

Academic literature on the topic 'Tubulins'

Author: Grafiati
Published: 4 June 2021
Last updated: 20 February 2023

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

Journal articles on the topic "Tubulins":

1

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 (September 1, 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 expression of gamma-tubulin in the cell cytoplasm. In most cells, overexpression of gamma-tubulin causes a dramatic reorganization of the cellular microtubule network. Furthermore, we show that when overexpressed, gamma-tubulin causes ectopic nucleation of microtubules which are not associated with the centrosome. In a fraction of cells, gamma-tubulin self-assembles into novel tubular structures with a diameter of approximately 50 nm (named gamma-tubules). Furthermore, unlike microtubules, gamma-tubules are resistant to cold or drug induced depolymerization. These data provide evidence that gamma-tubulin can cause nucleation of microtubule assembly and can self-assemble into novel tubular structures.
2

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 (March 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 mitotic spindle. Sequence analysis shows that beta 2 tubulin is only 83% identical to the two beta tubulins expressed in amoebae. This compares with 70 to 83% identity between Physarum beta 2 tubulin and the beta tubulins of yeasts, fungi, alga, trypanosome, fruit fly, chicken, and mouse. On the other hand, Physarum beta 2 tubulin is no more similar to, for example, Aspergillus beta tubulins than it is to those of Drosophila melanogaster or mammals. Several eucaryotes express at least one widely diverged beta tubulin as well as one or more beta tubulins that conform more closely to a consensus beta-tubulin sequence. We suggest that beta-tubulins diverge more when their expression pattern is restricted, especially when this restriction results in their use in fewer functions. This divergence among beta tubulins could have resulted through neutral drift. For example, exclusive use of Physarum beta 2 tubulin in the spindle may have allowed more amino acid substitutions than would be functionally tolerable in the beta tubulins that are utilized in multiple microtubular organelles. Alternatively, restricted use of beta tubulins may allow positive selection to operate more freely to refine beta-tubulin function.
3

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 (March 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 mitotic spindle. Sequence analysis shows that beta 2 tubulin is only 83% identical to the two beta tubulins expressed in amoebae. This compares with 70 to 83% identity between Physarum beta 2 tubulin and the beta tubulins of yeasts, fungi, alga, trypanosome, fruit fly, chicken, and mouse. On the other hand, Physarum beta 2 tubulin is no more similar to, for example, Aspergillus beta tubulins than it is to those of Drosophila melanogaster or mammals. Several eucaryotes express at least one widely diverged beta tubulin as well as one or more beta tubulins that conform more closely to a consensus beta-tubulin sequence. We suggest that beta-tubulins diverge more when their expression pattern is restricted, especially when this restriction results in their use in fewer functions. This divergence among beta tubulins could have resulted through neutral drift. For example, exclusive use of Physarum beta 2 tubulin in the spindle may have allowed more amino acid substitutions than would be functionally tolerable in the beta tubulins that are utilized in multiple microtubular organelles. Alternatively, restricted use of beta tubulins may allow positive selection to operate more freely to refine beta-tubulin function.
4

Khabudaev, Kirill V., Darya P. Petrova, Yekaterina D. Bedoshvili, Yelena V. Likhoshway, and Mikhail A. Grachev. "Molecular Evolution of Tubulins in Diatoms." International Journal of Molecular Sciences 23, no. 2 (January 6, 2022): 618. http://dx.doi.org/10.3390/ijms23020618.

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Microtubules are formed by α- and β-tubulin heterodimers nucleated with γ-tubulin. Tubulins are conserved eukaryotic proteins. Previously, it was shown that microtubules are involved in diatom silica frustule morphogenesis. Diatom frustules are varied, and their morphology is species-specific. Despite the attractiveness of the problem of elucidating the molecular mechanisms of genetically programmed morphogenesis, the structure and evolution of diatom tubulins have not been studied previously. Based on available genomic and transcriptome data, we analyzed the phylogeny of the predicted amino acid sequences of diatom α-, β- and γ-tubulins and identified five groups for α-tubulins, six for β-tubulins and four for γ-tubulins. We identified characteristic amino acids of each of these groups and also analyzed possible posttranslational modification sites of diatom tubulins. According to our results, we assumed what changes occurred in the diatom tubulin structures during their evolution. We also identified which tubulin groups are inherent in large diatom taxa. The similarity between the evolution of diatom tubulins and the evolution of diatoms suggests that molecular changes in α-, β- and γ-tubulins could be one of the factors in the formation of a high morphological diversity of diatoms.
5

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 (August 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 complexes. Furthermore, carbendazim significantly inhibited the polymerization of α1-/β2-tubulins and α2-/β2-tubulins 90.9 ± 0.4 and 93.5 ± 0.05%, respectively, in vitro. A similar result appeared with benomyl on the polymerization of α1-/β2-tubulins and α2-/β2-tubulins at 89.9 ± 0.1% and 92.6 ± 1.2% inhibition ratios, respectively. In addition, thiabendazole inhibited 81.6 ± 1% polymerization of α1-/β2-tubulins, whereas it had less effect on α2-/β2-tubulin polymerization, with 20.1 ± 1.9% inhibition ratio. However, the three compounds cannot destabilize the polymerized microtubule. To illuminate the issue, mapping the carbendazim binding sites and β/α subunit interface on β/α-tubulin complexes by homology modeling showed that the two domains were closed to each other. Understanding the nature of the interaction between benzimidazole compounds and F. graminearum tubulin is fundamental for the development of tubulin-specific anti-F. graminearum compounds.
6

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 (June 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 representative of an ancient sequence divergence event which at least preceded the split between lines leading to vertebrates and invertebrates. The intron/exon structures of the genes for beta 2- and beta 3-tubulin are not the same. The structure of the gene for the variant beta 3-tubulin isoform, but not that of the testis-specific beta 2-tubulin gene, is similar to that of vertebrate beta-tubulins. The mutation B2t8 in the gene for the testis-specific beta 2-tubulin defines a single amino acid residue required for normal assembly function of beta-tubulin. The sequence of the B2t8 gene is identical to that of the wild-type gene except for a single nucleotide change resulting in the substitution of lysine for glutamic acid at residue 288. This position falls at the junction between two major structural domains of the beta-tubulin molecule. Although this hinge region is relatively variable in sequence among different beta-tubulins, the residue corresponding to glu 288 of Drosophila beta 2-tubulin is highly conserved as an acidic amino acid not only in all other beta-tubulins but in alpha-tubulins as well.
7

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 (June 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 representative of an ancient sequence divergence event which at least preceded the split between lines leading to vertebrates and invertebrates. The intron/exon structures of the genes for beta 2- and beta 3-tubulin are not the same. The structure of the gene for the variant beta 3-tubulin isoform, but not that of the testis-specific beta 2-tubulin gene, is similar to that of vertebrate beta-tubulins. The mutation B2t8 in the gene for the testis-specific beta 2-tubulin defines a single amino acid residue required for normal assembly function of beta-tubulin. The sequence of the B2t8 gene is identical to that of the wild-type gene except for a single nucleotide change resulting in the substitution of lysine for glutamic acid at residue 288. This position falls at the junction between two major structural domains of the beta-tubulin molecule. Although this hinge region is relatively variable in sequence among different beta-tubulins, the residue corresponding to glu 288 of Drosophila beta 2-tubulin is highly conserved as an acidic amino acid not only in all other beta-tubulins but in alpha-tubulins as well.
8

Xie, Yixin, and Lin Li. "Computational Study on E-Hooks of Tubulins in the Binding Process with Kinesin." International Journal of Molecular Sciences 23, no. 4 (February 12, 2022): 2035. http://dx.doi.org/10.3390/ijms23042035.

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Cargo transport within cells is essential to healthy cells, which requires microtubules-based motors, including kinesin. The C-terminal tails (E-hooks) of alpha and beta tubulins of microtubules have been proven to play important roles in interactions between the kinesins and tubulins. Here, we implemented multi-scale computational methods in E-hook-related analyses, including flexibility investigations of E-hooks, binding force calculations at binding interfaces between kinesin and tubulins, electrostatic potential calculations on the surface of kinesin and tubulins. Our results show that E-hooks have several functions during the binding process: E-hooks utilize their own high flexibilities to increase the chances of reaching a kinesin; E-hooks help tubulins to be more attractive to kinesin. Besides, we also observed the differences between alpha and beta tubulins: beta tubulin shows a higher flexibility than alpha tubulin; beta tubulin generates stronger attractive forces (about twice the strengths) to kinesin at different distances, no matter with E-hooks in the structure or not. Those facts may indicate that compared to alpha tubulin, beta tubulin contributes more to attracting and catching a kinesin to microtubule. Overall, this work sheds the light on microtubule studies, which will also benefit the treatments of neurodegenerative diseases, cancer treatments, and preventions in the future.
9

Lajoie-Mazenc, I., C. Detraves, V. Rotaru, M. Gares, Y. Tollon, C. Jean, M. Julian, M. Wright, and B. Raynaud-Messina. "A single gamma-tubulin gene and mRNA, but two gamma-tubulin polypeptides differing by their binding to the spindle pole organizing centres." Journal of Cell Science 109, no. 10 (October 1, 1996): 2483–92. http://dx.doi.org/10.1242/jcs.109.10.2483.

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Cells of eukaryotic organisms exhibit microtubules with various functions during the different developmental stages. The identification of multiple forms of alpha- and beta-tubulins had raised the question of their possible physiological roles. In the myxomycete Physarum polycephalum a complex polymorphism for alpha- and beta-tubulins has been correlated with a specific developmental expression pattern. Here, we have investigated the potential heterogeneity of gamma-tubulin in this organism. A single gene, with 3 introns and 4 exons, and a single mRNA coding for gamma-tubulin were detected. They coded for a polypeptide of 454 amino acids, with a predicted molecular mass of 50,674, which presented 64–76% identity with other gamma-tubulins. However, immunological studies identified two gamma-tubulin polypeptides, both present in the two developmental stages of the organism, uninucleate amoebae and multinucleate plasmodia. The two gamma-tubulins, called gamma s- and gamma f-tubulin for slow and fast electrophoretic mobility, exhibited apparent molecular masses of 52,000 and 50,000, respectively. They were recognized by two antibodies (R70 and JH46) raised against two distinct conserved sequences of gamma-tubulins. They were present both in the preparations of amoebal centrosomes possessing two centrioles and in the preparations of plasmodial nuclear metaphases devoid of structurally distinct polar structures. These two gamma-tubulins exhibited different sedimentation properties as shown by ultracentrifugation and sedimentation in sucrose gradients. Moreover, gamma s-tubulin was tightly bound to microtubule organizing centers (MTOCs) while gamma f-tubulin was loosely associated with these structures. This first demonstration of the presence of two gamma-tubulins with distinct properties in the same MTOC suggests a more complex physiological role than previously assumed.
10

Chumová, Jana, Hana Kourová, Lucie Trögelová, Petr Halada, and Pavla Binarová. "Microtubular and Nuclear Functions of γ-Tubulin: Are They LINCed?" Cells 8, no. 3 (March 19, 2019): 259. http://dx.doi.org/10.3390/cells8030259.

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γ-Tubulin is a conserved member of the tubulin superfamily with a function in microtubule nucleation. Proteins of γ-tubulin complexes serve as nucleation templates as well as a majority of other proteins contributing to centrosomal and non-centrosomal nucleation, conserved across eukaryotes. There is a growing amount of evidence of γ-tubulin functions besides microtubule nucleation in transcription, DNA damage response, chromatin remodeling, and on its interactions with tumor suppressors. However, the molecular mechanisms are not well understood. Furthermore, interactions with lamin and SUN proteins of the LINC complex suggest the role of γ-tubulin in the coupling of nuclear organization with cytoskeletons. γ-Tubulin that belongs to the clade of eukaryotic tubulins shows characteristics of both prokaryotic and eukaryotic tubulins. Both human and plant γ-tubulins preserve the ability of prokaryotic tubulins to assemble filaments and higher-order fibrillar networks. γ-Tubulin filaments, with bundling and aggregating capacity, are suggested to perform complex scaffolding and sequestration functions. In this review, we discuss a plethora of γ-tubulin molecular interactions and cellular functions, as well as recent advances in understanding the molecular mechanisms behind them.
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You might also be interested in the extended bibliographies on the topic 'Tubulins' for particular source types:
Journal articles Dissertations / Theses Books

Dissertations / Theses on the topic "Tubulins":

1

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 ».

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 les mécanismes de défense ou qui affectent la prolifération cellulaire végétale.

Dans le cadre de notre travail de thèse, nous nous sommes fixé deux objectifs principaux qui sont de caractériser les altérations métaboliques au niveau des tissus hyperplasiques de tabac mais aussi de rechercher des applications potentielles du point de vue thérapeutique de cette interaction.

L’approche métabolomique globale basée sur une analyse comparative des spectres 1H-RMN d’extraits bruts de tissus infectés et de tissus non-infectés couplée à des analyses statistiques de données multivariées (ACP, OPLS-DA) a été utilisé pour l’étude de la reprogrammation métabolique. Le résultat indique une accumulation de composés phénoliques et des métabolites de la famille des diterpènes dans les tissus de la galle feuillée.

Les activités biologiques des extraits de la galle feuillée ont ensuite été évaluées, notamment des activités antioxydantes (DPPH, FRAP), anti-inflammatoire (15-LOX) et antiproliférative (MTT). Il ressort de cette analyse une augmentation du potentiel réducteur et anti-radicalaire des extraits de la galle feuillée, une activité inhibitrice de la lipoxygénase ainsi qu'une activité antiproliférative sur lignées tumorales humaines, comparée à la plante non infectée.

L’étude des composés affectant la prolifération des cellules cancéreuses humaines a aboutit à la mise en évidence d’un mélange de molécules (F3.1.1) appartenant au groupe des incensoles (cembrènoïdes). Ces composés ralentissent la durée de la division cellulaire, affectent la taille des cellules et induisent des anomalies de la karyokinèse et de la cytokinèse des cellules de glioblastome U373. La dynamique tubuline/microtubule est identifiée comme étant la cible des cembrènoïdes (F3.1.1). L’effet des ces composés est original comparé aux anti-tubulines usuels tel que la colchicine et le paclitaxel. Le mécanisme d’action des incensoles est unique et donc prometteur du fait que la dynamique des microtubules reste une cible de choix dans le traitement des cellules cancéreuses.


Doctorat en Sciences biomédicales et pharmaceutiques
info:eu-repo/semantics/nonPublished

2

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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Lo, Wai Hong. "Biochemical, structural and functional characterization of the light chains of the microtubule-based motor dynein /." View Abstract or Full-Text, 2003. http://library.ust.hk/cgi/db/thesis.pl?BICH%202003%20LO.

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Thesis (Ph. D.)--Hong Kong University of Science and Technology, 2003.
Includes bibliographical references (leaves 133-154). Also available in electronic version. Access restricted to campus users.
4

Tang, Liang. "Characterization of tubulins from parasitic nematodes (Brugia malayi, B. pahangi and Nippostrongylus brasiliensis) and comparison with mammalian brain tubulin." Thesis, McGill University, 1988. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=75933.

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The properties of tubulins from Brugia malayi, B. pahangi, Nippostrongylus brasiliensis and rat brain were compared. Tubulins from all nematodes and rat brain were partially purified by polylysine agarose chromatography, those of brain also by cycles of assembly/disassembly, and all by taxol-induced assembly. The tubulins were compared with respect to concentration ($ mu$g tubulin/mg soluble protein), drugs binding and isoforms. The tubulins of B. malayi and B. pahangi were similar. However, the tubulin from these filariae were different from those of N. brasiliensis. Even larger differences were detected between the nematode tubulins and those of rat brain. However, all tubulins reacted to $ alpha$- and $ beta$-tubulin monoclonal antibodies, and had similar mobility on SDS-PAGE. Different peptide maps were obtained for N. brasiliensis tubulin compared with rat brain tubulin. Tubulins of N. brasiliensis bound more mebendazole than did those of Brugia nematodes (B$ sb{ rm max}$: pmoles/$ mu$g tubulin). The binding of benzimidazoles to nematode tubulins was much higher than to rat brain tubulin. Benzimidazole binding to brain tubulin was influenced by the degree of assembly of the tubulin. This did not appear to be the case for the nematode tubulins. In vitro translation of B. malayi mRNA resulted in two isoforms for both $ alpha$- and $ beta$-tubulins in contrast to the 4 $ alpha$- and 4-5 $ beta$-isoforms found naturally. This suggest post translational modification of tubulin may take place in B. malayi. This study has characterized some of the differences that exist between mammalian tubulins and those of nematodes on the one hand, and between the tubulins of a gastrointestinal nematode (N. brasiliensis) and those of filariae (B. malayi and B. pahangi) on the other hand.
5

Akkari, Yassmine M. Nazih. "Investigation of tubulins in Aspergillus nidulans and Cyanidium caldarium /." The Ohio State University, 1997. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487942739806417.

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Bittermann, Elizabeth A. "The Roles of Tubulins in the Developing Mouse Brain." University of Cincinnati / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1523630790076922.

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Cheung, Po Yan. "Interaction between MKK6 and p150 glued dynactin is required for microtubule-mediated p38 MAPK activation /." View Abstract or Full-Text, 2002. http://library.ust.hk/cgi/db/thesis.pl?BICH%202002%20CHEUNG.

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Thesis (M. Phil.)--Hong Kong University of Science and Technology, 2002.
On t.p. glued is superscript. Includes bibliographical references (leaves 84-94). Also available in electronic version. Access restricted to campus users.
8

Washington, Ashley L. "FUNCTIONAL TESTS OF β TUBULINS IN DROSOPHILA SPERM TAIL MORPHOLOGY." University of Dayton / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=dayton1229709260.

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Washington, Ashley. "Functional tests of [beta] tubulins in Drosophila sperm tail morphology." Dayton, Ohio : University of Dayton, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=dayton1229709260.

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Cushion, Thomas David. "Tubulin genes in human disorders of cerebral cortex development." Thesis, Swansea University, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.678290.

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Books on the topic "Tubulins":

1

Carlomagno, Teresa, and Karl-Heinz Altmann. Tubulin-binding agents: Synthetic, structural and mechanistic insights. Edited by SpringerLink (Online service). Berlin: Springer, 2009.

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Jesús, Avila, ed. Microtubule proteins. Boca Raton, Fla: CRC Press, 1990.

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3

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

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Thomas, Kreis, and Vale Ronald, eds. Guidebook to the cytoskeletal and motor proteins. 2nd ed. Oxford: Oxford University Press, 1999.

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EMBO Workshop (1990 Cambridge, England). Motor proteins: A volume based on the EMBO Workshop, Cambridge, September 1990. Cambridge [England]: Company of Biologists, 1991.

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Carlomagno, Teresa, ed. Tubulin-Binding Agents. Berlin, Heidelberg: 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. Hauppauge, N.Y: Nova Science, 2011.

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

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

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

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Book chapters on the topic "Tubulins":

1

Morejohn, Louis C., and Donald E. Fosket. "Tubulins from Plants, Fungi, and Protists." In Cell and Molecular Biology of the Cytoskeleton, 257–329. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2151-4_11.

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Yu, Nuo, and Niels Galjart. "Purification of Mammalian Tubulins and Tubulin-Associated Proteins Using a P2A-Based Expression System." In Methods in Molecular Biology, 1–17. New York, NY: Springer US, 2019. http://dx.doi.org/10.1007/978-1-0716-0219-5_1.

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Burns, Roy G., Kevin W. Farrell, and Christopher D. Surridge. "Should the Tubulins be Members of the GTPase Superfamily?" In Ciba Foundation Symposium 176 - The GTPase Superfamily, 248–77. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514450.ch16.

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O’Connell, Paul A., and Thomas H. MacRae. "Preparation and Characterization of Posttranslationally Modified Tubulins From Artemia franciscana." In Methods in Molecular Medicine™, 45–63. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-442-1_4.

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Tian, Huaize, and Sanetaka Shirahata. "Some Characteristics of UNC-51 Phosphorylations of Both Actins and Tubulins." In Animal Cell Technology: Basic & Applied Aspects, 333–39. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-9646-4_50.

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Yariv, Joseph. "Tubulin." In The Discreet Charm of Protein Binding Sites, 19–26. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24996-4_2.

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Schatten, Heide, and Qing-Yuan Sun. "Posttranslationally Modified Tubulins and Other Cytoskeletal Proteins: Their Role in Gametogenesis, Oocyte Maturation, Fertilization and Pre-implantation Embryo Development." In Advances in Experimental Medicine and Biology, 57–87. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0817-2_4.

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Tian, Huaize, and Sanetaka Shirahata. "Protein Phosphotase 1α Reverses UNC-51 Phosphorylations of Both Actins and Tubulins and a New Model of UNC-51-Inducing Axon Formation." In Animal Cell Technology: Basic & Applied Aspects, 341–45. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-9646-4_51.

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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, 379–84. Boston, MA: 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, 217–40. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4613-0515-6_9.

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Conference papers on the topic "Tubulins":

1

Deriu, Marco A., Monica Soncini, Mario Orsi, Mishal Patel, Jonathan W. Essex, Franco M. Montevecchi, and Alberto Redaelli. "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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Abstract:
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 similarity from the primary to the tertiary structure level [1].
2

Das, Somenath, Ramana Pidaparti, and Preetam Ghosh. "Modeling Self-organization of Microtubules from Tubulins." In 8th International Conference on Bio-inspired Information and Communications Technologies (formerly BIONETICS). ACM, 2015. http://dx.doi.org/10.4108/icst.bict.2014.257891.

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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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Abstract:
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. α- and β-tubulin monomers consists of about 450 residues and shows a high degree of similarity from the primary to the tertiary structure level. However, one important difference is that the α-monomer binds a GTP molecule while the β-monomer binds a GDP molecule [2].
4

Singh, Shivendra V., Marie Lue Antony, Joomin Lee, Eun-Ryeong Hahm, Su-Hyeong Kim, Guillermo Romero, Adam I. Marcus, et al. "Abstract 228: Withaferin A downregulates tubulins and covalently binds β-tubulin at cysteine-303 in human breast cancer cells." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-228.

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Yang, Chia-Ping H., Hui Xiao, and Susan Band Horwitz. "Abstract 4496: Differential inhibition by microtubule stabilizing agents of 2-(m-azidobenzoyl)Taxol photoaffinity labeling of tubulins from different eukaryotic sources." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4496.

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Sohrabi, Salman, Seyyed Mahdi Nemati Mehr, and Pedram Falsafi. "A Novel Approach for Compensating the Significance of Tubule’s Architecture in Urine Concentrating Mechanism of Renal Medulla." In ASME 2013 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/imece2013-63747.

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Abstract:
Many theories and mathematical simulations have been proposed concerning urine concentrating mechanism (UCM). The WKM and region approach are the two most valuable methods for compensating the effect of tubule’s architecture in renal medulla. They both have tried to simulate tubule’s confinement within a particular region mathematically in one spatial dimension. In this study, continuity, momentum and species transport equations along with standard expressions for transtubular solutes and water transports on tubule’s membrane were solved numerically in three spatial dimensions which practically is the main significance of our novel approach. Model structure has been chosen as simple as possible to minimize the effect of other factors in tubule’s solute and water exchange. It has been tried to simulate the preferential interaction between tubules by introducing different diffusion coefficients for solutes in the intermediate media in order that changing this physical parameter directly could influence tubule’s confinement with respect to each other. The results have been discussed in detail and then the effect of solute’s diffusivity on UCM has been investigated subsequently. In overall, it has been found out that this simulation can validate the integrity of our proposed approach for further investigation in this field.
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Stewart, R. B., F. Marketz, W. C. M. Lohbeck, F. D. Fischer, W. Daves, F. G. Rammerstorfer, and H. J. Böhm. "Expandable Wellbore Tubulars." In SPE Technical Symposium. Society of Petroleum Engineers, 1999. http://dx.doi.org/10.2118/60766-ms.

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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., and Susan B. Horwitz. "Abstract 664: Polymerization of human βIII-tubulin is distinct from βI-tubulin in a cell-free system." In 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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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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Abstract:
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 using explicit water molecules. In order to measure the monomers’ elastic constants, simulations were performed by mimicking experiments carried out with atomic force microscopy. A different approach was used to determine the interaction force between the α- and β-monomers using 8 different monomer configurations based on different inter-monomer distances. The obtained results show an elastic constant value for α-tubulin of 3.4–3.9 N/m, while for the β-tubulin the elastic constant was measured to be 1.8–2.4 N/m. The maximum interaction force between the monomers was estimated to be 11.2 nN. In perspective, these outcomes will allow exchanging atomic level description with key mechanical features enabling microtubule characterisation by continuum mechanics approach.

Reports on the topic "Tubulins":

1

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

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

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

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Banerjee, Asok. Characterization of Tubulin Isoforms in Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, May 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. Fort Belvoir, VA: Defense Technical Information Center, May 2004. http://dx.doi.org/10.21236/ada432471.

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

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

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

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Susan M. Wick. Growth and development of maize that contains mutant tubulin genes. Office of Scientific and Technical Information (OSTI), July 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. Fort Belvoir, VA: Defense Technical Information Center, May 2002. http://dx.doi.org/10.21236/ada405620.

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To the bibliography