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Journal articles on the topic 'Tubulin code'

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Published: 10 December 2022
Last updated: 28 January 2023

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1

Verhey, Kristen J., and Jacek Gaertig. "The Tubulin Code." Cell Cycle 6, no. 17 (September 2007): 2152–60. http://dx.doi.org/10.4161/cc.6.17.4633.

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2

Raunser, Stefan, and Christos Gatsogiannis. "Deciphering the Tubulin Code." Cell 161, no. 5 (May 2015): 960–61. http://dx.doi.org/10.1016/j.cell.2015.05.004.

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3

Lopes, Danilo, and Helder Maiato. "The Tubulin Code in Mitosis and Cancer." Cells 9, no. 11 (October 26, 2020): 2356. http://dx.doi.org/10.3390/cells9112356.

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The “tubulin code” combines different α/β-tubulin isotypes with several post-translational modifications (PTMs) to generate microtubule diversity in cells. During cell division, specific microtubule populations in the mitotic spindle are differentially modified, but only recently, the functional significance of the tubulin code, with particular emphasis on the role specified by tubulin PTMs, started to be elucidated. This is the case of α-tubulin detyrosination, which was shown to guide chromosomes during congression to the metaphase plate and allow the discrimination of mitotic errors, whose correction is required to prevent chromosomal instability—a hallmark of human cancers implicated in tumor evolution and metastasis. Although alterations in the expression of certain tubulin isotypes and associated PTMs have been reported in human cancers, it remains unclear whether and how the tubulin code has any functional implications for cancer cell properties. Here, we review the role of the tubulin code in chromosome segregation during mitosis and how it impacts cancer cell properties. In this context, we discuss the existence of an emerging “cancer tubulin code” and the respective implications for diagnostic, prognostic and therapeutic purposes.
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4

Wehenkel, Annemarie, and Carsten Janke. "Towards elucidating the tubulin code." Nature Cell Biology 16, no. 4 (April 2014): 303–5. http://dx.doi.org/10.1038/ncb2938.

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5

Strzyz, Paulina. "Extension of the tubulin code." Nature Reviews Molecular Cell Biology 17, no. 10 (August 24, 2016): 609. http://dx.doi.org/10.1038/nrm.2016.117.

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6

Pamula, Melissa C., Shih-Chieh Ti, and Tarun M. Kapoor. "The structured core of human β tubulin confers isotype-specific polymerization properties." Journal of Cell Biology 213, no. 4 (May 16, 2016): 425–33. http://dx.doi.org/10.1083/jcb.201603050.

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Diversity in cytoskeleton organization and function may be achieved through variations in primary sequence of tubulin isotypes. Recently, isotype functional diversity has been linked to a “tubulin code” in which the C-terminal tail, a region of substantial sequence divergence between isotypes, specifies interactions with microtubule-associated proteins. However, it is not known whether residue changes in this region alter microtubule dynamic instability. Here, we examine recombinant tubulin with human β isotype IIB and characterize polymerization dynamics. Microtubules with βIIB have catastrophe frequencies approximately threefold lower than those with isotype βIII, a suppression similar to that achieved by regulatory proteins. Further, we generate chimeric β tubulins with native tail sequences swapped between isotypes. These chimeras have catastrophe frequencies similar to that of the corresponding full-length construct with the same core sequence. Together, our data indicate that residue changes within the conserved β tubulin core are largely responsible for the observed isotype-specific changes in dynamic instability parameters and tune tubulin’s polymerization properties across a wide range.
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7

Silflow, C. D., R. L. Chisholm, T. W. Conner, and L. P. Ranum. "The two alpha-tubulin genes of Chlamydomonas reinhardi code for slightly different proteins." Molecular and Cellular Biology 5, no. 9 (September 1985): 2389–98. http://dx.doi.org/10.1128/mcb.5.9.2389-2398.1985.

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Full-length cDNA clones corresponding to the transcripts of the two alpha-tubulin genes in Chlamydomonas reinhardi were isolated. DNA sequence analysis of the cDNA clones and cloned gene fragments showed that each gene contains 1,356 base pairs of coding sequence, predicting alpha-tubulin products of 451 amino acids. Of the 27 nucleotide differences between the two genes, only two result in predicted amino acid differences between the two gene products. In the more divergent alpha 2 gene, a leucine replaces an arginine at amino acid 308, and a valine replaces a glycine at amino acid 366. The results predicted that two alpha-tubulin proteins with different net charges are produced as primary gene products. The predicted amino acid sequences are 86 and 70% homologous with alpha-tubulins from rat brain and Schizosaccharomyces pombe, respectively. Each gene had two intervening sequences, located at identical positions. Portions of an intervening sequence highly conserved between the two beta-tubulin genes are also found in the second intervening sequence of each of the alpha genes. These results, together with our earlier report of the beta-tubulin sequences in C. reinhardi, present a picture of the total complement of genetic information for tubulin in this organism.
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8

Silflow, C. D., R. L. Chisholm, T. W. Conner, and L. P. Ranum. "The two alpha-tubulin genes of Chlamydomonas reinhardi code for slightly different proteins." Molecular and Cellular Biology 5, no. 9 (September 1985): 2389–98. http://dx.doi.org/10.1128/mcb.5.9.2389.

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Full-length cDNA clones corresponding to the transcripts of the two alpha-tubulin genes in Chlamydomonas reinhardi were isolated. DNA sequence analysis of the cDNA clones and cloned gene fragments showed that each gene contains 1,356 base pairs of coding sequence, predicting alpha-tubulin products of 451 amino acids. Of the 27 nucleotide differences between the two genes, only two result in predicted amino acid differences between the two gene products. In the more divergent alpha 2 gene, a leucine replaces an arginine at amino acid 308, and a valine replaces a glycine at amino acid 366. The results predicted that two alpha-tubulin proteins with different net charges are produced as primary gene products. The predicted amino acid sequences are 86 and 70% homologous with alpha-tubulins from rat brain and Schizosaccharomyces pombe, respectively. Each gene had two intervening sequences, located at identical positions. Portions of an intervening sequence highly conserved between the two beta-tubulin genes are also found in the second intervening sequence of each of the alpha genes. These results, together with our earlier report of the beta-tubulin sequences in C. reinhardi, present a picture of the total complement of genetic information for tubulin in this organism.
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9

Janke, Carsten. "The tubulin code: Molecular components, readout mechanisms, and functions." Journal of Cell Biology 206, no. 4 (August 18, 2014): 461–72. http://dx.doi.org/10.1083/jcb.201406055.

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Microtubules are cytoskeletal filaments that are dynamically assembled from α/β-tubulin heterodimers. The primary sequence and structure of the tubulin proteins and, consequently, the properties and architecture of microtubules are highly conserved in eukaryotes. Despite this conservation, tubulin is subject to heterogeneity that is generated in two ways: by the expression of different tubulin isotypes and by posttranslational modifications (PTMs). Identifying the mechanisms that generate and control tubulin heterogeneity and how this heterogeneity affects microtubule function are long-standing goals in the field. Recent work on tubulin PTMs has shed light on how these modifications could contribute to a “tubulin code” that coordinates the complex functions of microtubules in cells.
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10

Gadadhar, Sudarshan, Satish Bodakuntla, Kathiresan Natarajan, and Carsten Janke. "The tubulin code at a glance." Journal of Cell Science 130, no. 8 (March 21, 2017): 1347–53. http://dx.doi.org/10.1242/jcs.199471.

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11

Park, James H., and Antonina Roll-Mecak. "The tubulin code in neuronal polarity." Current Opinion in Neurobiology 51 (August 2018): 95–102. http://dx.doi.org/10.1016/j.conb.2018.03.001.

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12

Barisic, Marin, and Helder Maiato. "Cracking the (tubulin) code of mitosis." Oncotarget 6, no. 23 (August 6, 2015): 19356–57. http://dx.doi.org/10.18632/oncotarget.5108.

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13

Yu, Ian, Christopher P. Garnham, and Antonina Roll-Mecak. "Writing and Reading the Tubulin Code." Journal of Biological Chemistry 290, no. 28 (May 8, 2015): 17163–72. http://dx.doi.org/10.1074/jbc.r115.637447.

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14

Verdier-Pinard, Pascal, Eddy Pasquier, Hui Xiao, Berta Burd, Claude Villard, Daniel Lafitte, Leah M. Miller, Ruth H. Angeletti, Susan Band Horwitz, and Diane Braguer. "Tubulin proteomics: Towards breaking the code." Analytical Biochemistry 384, no. 2 (January 2009): 197–206. http://dx.doi.org/10.1016/j.ab.2008.09.020.

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15

Trisciuoglio, Daniela, and Francesca Degrassi. "The Tubulin Code and Tubulin-Modifying Enzymes in Autophagy and Cancer." Cancers 14, no. 1 (December 21, 2021): 6. http://dx.doi.org/10.3390/cancers14010006.

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Microtubules are key components of the cytoskeleton of eukaryotic cells. Microtubule dynamic instability together with the “tubulin code” generated by the choice of different α- and β- tubulin isoforms and tubulin post-translational modifications have essential roles in the control of a variety of cellular processes, such as cell shape, cell motility, and intracellular trafficking, that are deregulated in cancer. In this review, we will discuss available evidence that highlights the crucial role of the tubulin code in determining different cancer phenotypes, including metastatic cell migration, drug resistance, and tumor vascularization, and the influence of modulating tubulin-modifying enzymes on cancer cell survival and aggressiveness. We will also discuss the role of post-translationally modified microtubules in autophagy—the lysosomal-mediated cellular degradation pathway—that exerts a dual role in many cancer types, either promoting or suppressing cancer growth. We will give particular emphasis to the role of tubulin post-translational modifications and their regulating enzymes in controlling the different stages of the autophagic process in cancer cells, and consider how the experimental modulation of tubulin-modifying enzymes influences the autophagic process in cancer cells and impacts on cancer cell survival and thereby represents a new and fruitful avenue in cancer therapy.
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16

Garnham, Christopher P., Ian Yu, Yan Li, and Antonina Roll-Mecak. "Crystal structure of tubulin tyrosine ligase-like 3 reveals essential architectural elements unique to tubulin monoglycylases." Proceedings of the National Academy of Sciences 114, no. 25 (June 2, 2017): 6545–50. http://dx.doi.org/10.1073/pnas.1617286114.

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Glycylation and glutamylation, the posttranslational addition of glycines and glutamates to genetically encoded glutamates in the intrinsically disordered tubulin C-terminal tails, are crucial for the biogenesis and stability of cilia and flagella and play important roles in metazoan development. Members of the diverse family of tubulin tyrosine ligase-like (TTLL) enzymes catalyze these modifications, which are part of an evolutionarily conserved and complex tubulin code that regulates microtubule interactions with cellular effectors. The site specificity of TTLL enzymes and their biochemical interplay remain largely unknown. Here, we report an in vitro characterization of a tubulin glycylase. We show that TTLL3 glycylates the β-tubulin tail at four sites in a hierarchical order and that TTLL3 and the glutamylase TTLL7 compete for overlapping sites on the tubulin tail, providing a molecular basis for the anticorrelation between glutamylation and glycylation observed in axonemes. This anticorrelation demonstrates how a combinatorial tubulin code written in two different posttranslational modifications can arise through the activities of related but distinct TTLL enzymes. To elucidate what structural elements differentiate TTLL glycylases from glutamylases, with which they share the common TTL scaffold, we determined the TTLL3 X-ray structure at 2.3-Å resolution. This structure reveals two architectural elements unique to glycyl initiases and critical for their activity. Thus, our work sheds light on the structural and functional diversification of TTLL enzymes, and constitutes an initial important step toward understanding how the tubulin code is written through the intersection of activities of multiple TTLL enzymes.
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17

Lockhead, Dean, Erich M. Schwarz, Robert O’Hagan, Sebastian Bellotti, Michael Krieg, Maureen M. Barr, Alexander R. Dunn, Paul W. Sternberg, and Miriam B. Goodman. "The tubulin repertoire of Caenorhabditis elegans sensory neurons and its context‑dependent role in process outgrowth." Molecular Biology of the Cell 27, no. 23 (November 15, 2016): 3717–28. http://dx.doi.org/10.1091/mbc.e16-06-0473.

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Microtubules contribute to many cellular processes, including transport, signaling, and chromosome separation during cell division. They comprise αβ‑tubulin heterodimers arranged into linear protofilaments and assembled into tubes. Eukaryotes express multiple tubulin isoforms, and there has been a longstanding debate as to whether the isoforms are redundant or perform specialized roles as part of a tubulin code. Here we use the well‑characterized touch receptor neurons (TRNs) of Caenorhabditis elegans to investigate this question through genetic dissection of process outgrowth both in vivo and in vitro. With single‑cell RNA-seq, we compare transcription profiles for TRNs with those of two other sensory neurons and present evidence that each sensory neuron expresses a distinct palette of tubulin genes. In the TRNs, we analyze process outgrowth and show that four tubulins (tba‑1, tba‑2, tbb‑1, and tbb‑2) function partially or fully redundantly, whereas two others (mec‑7 and mec‑12) perform specialized, context‑dependent roles. Our findings support a model in which sensory neurons express overlapping subsets of tubulin genes whose functional redundancy varies among cell types and in vivo and in vitro contexts.
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18

Wethekam, Linnea C., and Jeffrey K. Moore. "Microtubule cytoskeleton: Revealing new readers of the tubulin code." Current Biology 32, no. 18 (September 2022): R960—R962. http://dx.doi.org/10.1016/j.cub.2022.08.023.

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19

Groebner, Jennifer, and Pamela Tuma. "The Altered Hepatic Tubulin Code in Alcoholic Liver Disease." Biomolecules 5, no. 3 (September 18, 2015): 2140–59. http://dx.doi.org/10.3390/biom5032140.

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20

Roll-Mecak, Antonina. "The Tubulin Code in Microtubule Dynamics and Information Encoding." Developmental Cell 54, no. 1 (July 2020): 7–20. http://dx.doi.org/10.1016/j.devcel.2020.06.008.

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21

Santiago-Mujika, Estibaliz, Ruth Luthi-Carter, Flaviano Giorgini, and Elizabeta B. Mukaetova-Ladinska. "Tubulin Isotypes and Posttranslational Modifications in Vascular Dementia and Alzheimer’s Disease." Journal of Alzheimer's Disease Reports 6, no. 1 (November 24, 2022): 739–48. http://dx.doi.org/10.3233/adr-220068.

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Background: Vascular dementia (VaD) and Alzheimer’s disease (AD) are the two most common forms of dementia. Although these two types of dementia have different etiologies, they share some similarities in their pathophysiology, such as neuronal loss and decreased levels of tau protein. We hypothesize that these can have an impact upon the molecular changes in tubulin, precede the neuronal cell loss, and lead to changes in cytoskeletal associated proteins, as documented in both VaD and AD. Objective: We characterized different isotypes of tubulin together with their posttranslational modifications, as well as several microtubule associated proteins (MAPs), such as tau protein, MAP2 and MAP6, all together known as the tubulin code. Methods: We performed western blotting in human brain homogenates of controls and AD and VaD subjects. Results: We report that the levels of different tubulin isotypes differ depending on the dementia type and the brain area being studied: whereas α-tubulin is increased in the temporal lobe of VaD patients, it is decreased in the frontal lobe of AD patients. In VaD patients, the frontal lobe had a decrease in tyrosinated tubulin, which was accompanied by a decrease in tau protein and a tendency for lower levels of MAP2. Conclusion: Our findings highlight distinct changes in the tubulin code in VaD and AD, suggesting a therapeutic opportunity for different dementia subtypes in the future.
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22

Roll-Mecak, Antonina. "Readout of the Tubulin Code by Cellular Effectors: Graded Control of Microtubule Severing by Tubulin Glutamylation." Biophysical Journal 112, no. 3 (February 2017): 10a. http://dx.doi.org/10.1016/j.bpj.2016.11.082.

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23

Chakraborti, Soumyananda, Kathiresan Natarajan, Julian Curiel, Carsten Janke, and Judy Liu. "The emerging role of the tubulin code: From the tubulin molecule to neuronal function and disease." Cytoskeleton 73, no. 10 (May 9, 2016): 521–50. http://dx.doi.org/10.1002/cm.21290.

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24

Zheng, Pengli, Christopher J. Obara, Ewa Szczesna, Jonathon Nixon-Abell, Kishore K. Mahalingan, Antonina Roll-Mecak, Jennifer Lippincott-Schwartz, and Craig Blackstone. "ER proteins decipher the tubulin code to regulate organelle distribution." Nature 601, no. 7891 (December 15, 2021): 132–38. http://dx.doi.org/10.1038/s41586-021-04204-9.

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AbstractOrganelles move along differentially modified microtubules to establish and maintain their proper distributions and functions1,2. However, how cells interpret these post-translational microtubule modification codes to selectively regulate organelle positioning remains largely unknown. The endoplasmic reticulum (ER) is an interconnected network of diverse morphologies that extends promiscuously throughout the cytoplasm3, forming abundant contacts with other organelles4. Dysregulation of endoplasmic reticulum morphology is tightly linked to neurologic disorders and cancer5,6. Here we demonstrate that three membrane-bound endoplasmic reticulum proteins preferentially interact with different microtubule populations, with CLIMP63 binding centrosome microtubules, kinectin (KTN1) binding perinuclear polyglutamylated microtubules, and p180 binding glutamylated microtubules. Knockout of these proteins or manipulation of microtubule populations and glutamylation status results in marked changes in endoplasmic reticulum positioning, leading to similar redistributions of other organelles. During nutrient starvation, cells modulate CLIMP63 protein levels and p180–microtubule binding to bidirectionally move endoplasmic reticulum and lysosomes for proper autophagic responses.
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25

Barisic, Marin, and Helder Maiato. "The Tubulin Code: A Navigation System for Chromosomes during Mitosis." Trends in Cell Biology 26, no. 10 (October 2016): 766–75. http://dx.doi.org/10.1016/j.tcb.2016.06.001.

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26

Patel, Shreya, Marcus Winogradzki, Ahmad Othman, Waddell Holmes, and Jitesh Pratap. "Abstract 270: The novel control mechanism of the tubulin code and vesicular trafficking in breast cancer bone metastatic cells." Cancer Research 82, no. 12_Supplement (June 15, 2022): 270. http://dx.doi.org/10.1158/1538-7445.am2022-270.

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Abstract Metastasis of breast cancer (BC) to bone results in severe bone loss, fractures, and death. The crosstalk between BC cells and bone resident cells dramatically increases osteoclast activity, resulting in the release of growth factors from the bone matrix that causes aggressive tumor growth and bone loss. A potentially important aspect of this process is vesicular trafficking on microtubules (MTs) which can affect the output of signaling pathways and secretory activity of metastatic bone cells. MTs are cytoskeletal filaments composed of heterodimers, α- and β-tubulin. The tubulin isotypes and their variety of post-translational modifications (PTMs) control the properties and functions of MT filaments, a concept known as the ‘tubulin code’. Recent studies show an emerging link between alterations of the tubulin code with poor prognosis of breast cancer. However, the regulation of the code in metastatic bone cells is currently unknown. Tubulin acetylation occurs via α-tubulin N-acetyl transferase-1 (αTAT1) and can be reversed by histone deacetylase-6 (HDAC6). MTs lacking acetylation lose flexural rigidity and are prone to breaks following repetitive bending during vesicular trafficking. We found that HDAC6 interaction with α-tubulin is inhibited by a Runt-related factor (Runx2). Our biochemical, mass spectrometry and IPs analyses of MTs revealed that loss of Runx2 can reduce (i) acetylation and stability of MTs, (ii) interaction of HSP90 with α-tubulin, and (iii) levels of β 2a-tubulin. Our studies with Runx2 mutants indicate that the C-terminal of Runx2 serves a scaffolding function by interacting with MTs and HDAC6. Confocal microscopy revealed reduced puncta and altered distribution of endosomal vesicles and autophagosomes with Runx2 silencing. As MT targeting agents are often used as chemotherapeutics, we found that loss of Runx2 sensitizes breast cancer cells to docetaxel and vinblastine and reduces the secretion of IL-6. We found MDA-MB-231 cells metastasized to the bone show significant differences in microtubule isotype expression, with 10 of 19 studied showing 1.3 to 4.1 fold increases. Further analysis of whether Runx2 knockdown affects isotype expression, we found the majority of the 19 studied remain unchanged. Immunohistochemistry for Ac-α-Tub levels in bone metastatic patient samples shows significantly more Ac-α-Tub positive cells in metastatic bone tumors than primary tumors. These findings suggest a novel control mechanism of MTs stability via Runx2-HDAC6 interactions that can impact trafficking and cellular activity. Our results indicate that inhibition of Runx2 may sensitize metastatic tumors to MT targeting agents, and Runx2/HDAC6/Ac-α-Tub levels may serve as markers for metastatic tumors to help stratify patients for optimal treatment for metastatic bone disease. Citation Format: Shreya Patel, Marcus Winogradzki, Ahmad Othman, Waddell Holmes, Jitesh Pratap. The novel control mechanism of the tubulin code and vesicular trafficking in breast cancer bone metastatic cells [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022; 2022 Apr 8-13. Philadelphia (PA): AACR; Cancer Res 2022;82(12_Suppl):Abstract nr 270.
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27

Schvartz, Tomer, Noa Aloush, Inna Goliand, Inbar Segal, Dikla Nachmias, Eyal Arbely, and Natalie Elia. "Direct fluorescent-dye labeling of α-tubulin in mammalian cells for live cell and superresolution imaging." Molecular Biology of the Cell 28, no. 21 (October 15, 2017): 2747–56. http://dx.doi.org/10.1091/mbc.e17-03-0161.

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Genetic code expansion and bioorthogonal labeling provide for the first time a way for direct, site-specific labeling of proteins with fluorescent-dyes in live cells. Although the small size and superb photophysical parameters of fluorescent-dyes offer unique advantages for high-resolution microscopy, this approach has yet to be embraced as a tool in live cell imaging. Here we evaluated the feasibility of this approach by applying it for α-tubulin labeling. After a series of calibrations, we site-specifically labeled α-tubulin with silicon rhodamine (SiR) in live mammalian cells in an efficient and robust manner. SiR-labeled tubulin successfully incorporated into endogenous microtubules at high density, enabling video recording of microtubule dynamics in interphase and mitotic cells. Applying this labeling approach to structured illumination microscopy resulted in an increase in resolution, highlighting the advantages in using a smaller, brighter tag. Therefore, using our optimized assay, genetic code expansion provides an attractive tool for labeling proteins with a minimal, bright tag in quantitative high-resolution imaging.
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28

Alper, Joshua D., Franziska Decker, Bernice Agana, and Jonathon Howard. "The Motility of Axonemal Dynein Is Regulated by the Tubulin Code." Biophysical Journal 107, no. 12 (December 2014): 2872–80. http://dx.doi.org/10.1016/j.bpj.2014.10.061.

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29

Alper, Joshua, Franziska Decker, Bernice Agana, and Jonathon Howard. "The Motility of Axonemal Dynein is Regulated by the Tubulin Code." Biophysical Journal 110, no. 3 (February 2016): 458a. http://dx.doi.org/10.1016/j.bpj.2015.11.2453.

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30

Zheng, Pengli, Christopher J. Obara, Ewa Szczesna, Jonathon Nixon-Abell, Kishore K. Mahalingan, Antonina Roll-Mecak, Jennifer Lippincott-Schwartz, and Craig Blackstone. "Publisher Correction: ER proteins decipher the tubulin code to regulate organelle distribution." Nature 604, no. 7904 (March 23, 2022): E11. http://dx.doi.org/10.1038/s41586-022-04656-7.

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31

Janke, Carsten, and Maria M. Magiera. "The tubulin code and its role in controlling microtubule properties and functions." Nature Reviews Molecular Cell Biology 21, no. 6 (February 27, 2020): 307–26. http://dx.doi.org/10.1038/s41580-020-0214-3.

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32

Bulinski, J. Chloë. "Microtubules and Neurodegeneration: The Tubulin Code Sets the Rules of the Road." Current Biology 29, no. 1 (January 2019): R28—R30. http://dx.doi.org/10.1016/j.cub.2018.11.031.

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33

Ferlini, C., G. Raspaglio, F. Filippetti, and G. Scambia. "629 POSTER Hypoxia, TUBB3 expression and tissue selectivity. Does a tubulin code exist?" European Journal of Cancer Supplements 4, no. 12 (November 2006): 189. http://dx.doi.org/10.1016/s1359-6349(06)70634-6.

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34

Stearns, T., and D. Botstein. "Unlinked noncomplementation: isolation of new conditional-lethal mutations in each of the tubulin genes of Saccharomyces cerevisiae." Genetics 119, no. 2 (June 1, 1988): 249–60. http://dx.doi.org/10.1093/genetics/119.2.249.

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Abstract Mutations in genes of Saccharomyces cerevisiae that code for proteins that interact with beta-tubulin were sought by screening for unlinked mutations that fail to complement mutations in the single beta-tubulin-encoding gene (TUB2). Among the first three noncomplementing mutations examined, two are linked to TUB2 while one is unlinked. The unlinked mutation was shown to be a conditional-lethal allele of the major alpha-tubulin-encoding gene (TUB1) and represents the first such mutation in that gene. The tub1-1 mutation itself causes a cold-sensitive cell-cycle arrest, and confers supersensitivity to the antimicrotubule drug benomyl. These phenotypes occur in the presence of a wild-type copy of the minor alpha-tubulin-encoding gene, TUB3; the combination of tub1-1 and a tub3 null mutation is inviable in haploids. Through further application of this method, new mutations in TUB2 and TUB3 were isolated as unlinked noncomplementers of tub1-1. The noncomplementation between tub1 and tub2 mutations is gene specific and allele specific, suggesting that the phenotype is due to an interaction at the protein level. We conclude that isolation of unlinked noncomplementing mutations is likely to be a generally useful method for isolating mutations in interacting gene products.
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35

Theurkauf, W. E., H. Baum, J. Bo, and P. C. Wensink. "Tissue-specific and constitutive alpha-tubulin genes of Drosophila melanogaster code for structurally distinct proteins." Proceedings of the National Academy of Sciences 83, no. 22 (November 1, 1986): 8477–81. http://dx.doi.org/10.1073/pnas.83.22.8477.

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36

Braglia, Luca, Laura Morello, Floriana Gavazzi, Silvia Gianì, Francesco Mastromauro, Diego Breviario, Hélia Guerra Cardoso, Vera Valadas, and Maria Doroteia Campos. "Interlaboratory Comparison of Methods Determining the Botanical Composition of Animal Feed." Journal of AOAC INTERNATIONAL 101, no. 1 (January 1, 2018): 227–34. http://dx.doi.org/10.5740/jaoacint.17-0150.

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Abstract A consortium of European enterprises and research institutions has been engaged in the Feed-Code Project with the aim of addressing the requirements stated in European Union Regulation No. 767/2009, concerning market placement and use of feed of known and ascertained botanical composition. Accordingly, an interlaboratory trial was set up to compare the performance of different assays based either on optical microscope or DNA analysis for the qualitative and quantitative identification of the composition of compound animal feeds. A tubulin-based polymorphism method, on which the Feed-Code platform was developed, provided the most accurate results. The present study highlights the need for the performance of ring trials for the determination of the botanical composition of animal feeds and raises an alarm on the actual status of analytical inaccuracy.
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37

Amargant, Farners, Montserrat Barragan, Rita Vassena, and Isabelle Vernos. "Insights of the tubulin code in gametes and embryos: from basic research to potential clinical applications in humans†." Biology of Reproduction 100, no. 3 (September 21, 2018): 575–89. http://dx.doi.org/10.1093/biolre/ioy203.

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38

Varikoti, Rohith Anand, Hewafonsekage Yasan Y. Fonseka, Maria S. Kelly, Alex Javidi, Mangesh Damre, Sarah Mullen, Jimmie L. Nugent, Christopher M. Gonzales, George Stan, and Ruxandra I. Dima. "Exploring the Effect of Mechanical Anisotropy of Protein Structures in the Unfoldase Mechanism of AAA+ Molecular Machines." Nanomaterials 12, no. 11 (May 28, 2022): 1849. http://dx.doi.org/10.3390/nano12111849.

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Essential cellular processes of microtubule disassembly and protein degradation, which span lengths from tens of μm to nm, are mediated by specialized molecular machines with similar hexameric structure and function. Our molecular simulations at atomistic and coarse-grained scales show that both the microtubule-severing protein spastin and the caseinolytic protease ClpY, accomplish spectacular unfolding of their diverse substrates, a microtubule lattice and dihydrofolate reductase (DHFR), by taking advantage of mechanical anisotropy in these proteins. Unfolding of wild-type DHFR requires disruption of mechanically strong β-sheet interfaces near each terminal, which yields branched pathways associated with unzipping along soft directions and shearing along strong directions. By contrast, unfolding of circular permutant DHFR variants involves single pathways due to softer mechanical interfaces near terminals, but translocation hindrance can arise from mechanical resistance of partially unfolded intermediates stabilized by β-sheets. For spastin, optimal severing action initiated by pulling on a tubulin subunit is achieved through specific orientation of the machine versus the substrate (microtubule lattice). Moreover, changes in the strength of the interactions between spastin and a microtubule filament, which can be driven by the tubulin code, lead to drastically different outcomes for the integrity of the hexameric structure of the machine.
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39

Dupuis-Williams, P. "The tubulin gene family of Paramecium: Characterization and expression of the αPT1 and αPT2 genes which code for α-tubulins with unusual C-terminal amino acids, GLY and ALA." Biology of the Cell 87, no. 1-2 (1996): 83–93. http://dx.doi.org/10.1016/s0248-4900(97)89840-1.

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40

Dupuis-Williams, Pascale, Catherine Klotz, Honoré Mazarguil, and Janine Beisson. "The tubulin gene family of Paramecium: Characterization and expression of the αPT1 and αPT2 genes which code for α-tubulins with unusual C-terminal amino acids, GLY and ALA." Biology of the Cell 87, no. 1-2 (1996): 82–93. http://dx.doi.org/10.1111/j.1768-322x.1996.tb00969.x.

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41

Oca-Cossio, Jose, Lesley Kenyon, Huiling Hao, and Carlos T. Moraes. "Limitations of Allotopic Expression of Mitochondrial Genes in Mammalian Cells." Genetics 165, no. 2 (October 1, 2003): 707–20. http://dx.doi.org/10.1093/genetics/165.2.707.

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Abstract The possibility of expressing mitochondrial DNA-coded genes in the nuclear-cytoplasmic compartment provides an attractive system for genetic treatment of mitochondrial disorders associated with mitochondrial DNA mutations. In theory, by recoding mitochondrial genes to adapt them to the universal genetic code and by adding a DNA sequence coding for a mitochondrial-targeting sequence, one could achieve correct localization of the gene product. Such transfer has occurred in nature, and certain species of algae and plants express a number of polypeptides that are commonly coded by mtDNA in the nuclear-cytoplasmic compartment. In the present study, allotopic expression of three different mtDNA-coded polypeptides (ATPase8, apocytochrome b, and ND4) into COS-7 and HeLa cells was analyzed. Among these, only ATPase8 was correctly expressed and localized to mitochondria. The full-length, as well as truncated forms, of apocytochrome b and ND4 decorated the periphery of mitochondria, but also aggregated in fiber-like structures containing tubulin and in some cases also vimentin. The addition of a hydrophilic tail (EGFP) to the C terminus of these polypeptides did not change their localization. Overexpression of molecular chaperones also did not have a significant effect in preventing aggregations. Allotopic expression of apocytochrome b and ND4 induced a loss of mitochondrial membrane potential in transfected cells, which can lead to cell death. Our observations suggest that only a subset of mitochondrial genes can be replaced allotopically. Analyses of the hydrophobic patterns of different polypeptides suggest that hydrophobicity of the N-terminal segment is the main determinant for the importability of peptides into mammalian mitochondria.
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42

Wickham, Louise, Thomas Duchaîne, Ming Luo, Ivan R. Nabi, and Luc DesGroseillers. "Mammalian Staufen Is a Double-Stranded-RNA- and Tubulin-Binding Protein Which Localizes to the Rough Endoplasmic Reticulum." Molecular and Cellular Biology 19, no. 3 (March 1, 1999): 2220–30. http://dx.doi.org/10.1128/mcb.19.3.2220.

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ABSTRACT Staufen (Stau) is a double-stranded RNA (dsRNA)-binding protein involved in mRNA transport and localization in Drosophila.To understand the molecular mechanisms of mRNA transport in mammals, we cloned human (hStau) and mouse (mStau)staufen cDNAs. In humans, four transcripts arise by differential splicing of the Stau gene and code for two proteins with different N-terminal extremities. In vitro, hStau and mStau bind dsRNA via each of two full-length dsRNA-binding domains and tubulin via a region similar to the microtubule-binding domain of MAP-1B, suggesting that Stau cross-links cytoskeletal and RNA components. Immunofluorescent double labeling of transfected mammalian cells revealed that Stau is localized to the rough endoplasmic reticulum (RER), implicating this RNA-binding protein in mRNA targeting to the RER, perhaps via a multistep process involving microtubules. These results are the first demonstration of the association of an RNA-binding protein in addition to ribosomal proteins, with the RER, implicating this class of proteins in the transport of RNA to its site of translation.
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43

Pratt, L. F., S. Okamura, and D. W. Cleveland. "A divergent testis-specific alpha-tubulin isotype that does not contain a coded C-terminal tyrosine." Molecular and Cellular Biology 7, no. 1 (January 1987): 552–55. http://dx.doi.org/10.1128/mcb.7.1.552-555.1987.

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On the basis of analysis of cDNA clones of alpha-tubulin RNAs expressed during spermiogenesis in chickens, we report the identification of a novel alpha-tubulin which is expressed exclusively in chicken testes. Comparison of its sequence with those previously determined not only demonstrates that the encoded polypeptide is significantly divergent from other alpha-tubulins but also supports the hypothesis that alpha-tubulin isotypes are distinguished by a carboxy-terminal variable region sequence and, to a lesser extent, by a domain near the amino terminus. Since essentially all previously known alpha-tubulins undergo a unique cycle of removal and posttranslational readdition of a tyrosine residue at the extreme carboxy terminus, the presence in this testes alpha-tubulin of a very divergent carboxy terminus that does not contain an encoded tyrosine raises the possibility that this polypeptide does not participate in the usual cycle of tyrosination/detyrosination.
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44

Pratt, L. F., S. Okamura, and D. W. Cleveland. "A divergent testis-specific alpha-tubulin isotype that does not contain a coded C-terminal tyrosine." Molecular and Cellular Biology 7, no. 1 (January 1987): 552–55. http://dx.doi.org/10.1128/mcb.7.1.552.

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On the basis of analysis of cDNA clones of alpha-tubulin RNAs expressed during spermiogenesis in chickens, we report the identification of a novel alpha-tubulin which is expressed exclusively in chicken testes. Comparison of its sequence with those previously determined not only demonstrates that the encoded polypeptide is significantly divergent from other alpha-tubulins but also supports the hypothesis that alpha-tubulin isotypes are distinguished by a carboxy-terminal variable region sequence and, to a lesser extent, by a domain near the amino terminus. Since essentially all previously known alpha-tubulins undergo a unique cycle of removal and posttranslational readdition of a tyrosine residue at the extreme carboxy terminus, the presence in this testes alpha-tubulin of a very divergent carboxy terminus that does not contain an encoded tyrosine raises the possibility that this polypeptide does not participate in the usual cycle of tyrosination/detyrosination.
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45

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.
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46

Weatherbee, J. A., G. S. May, J. Gambino, and N. R. Morris. "Involvement of a particular species of beta-tubulin (beta 3) in conidial development in Aspergillus nidulans." Journal of Cell Biology 101, no. 3 (September 1, 1985): 706–11. http://dx.doi.org/10.1083/jcb.101.3.706.

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Strains of Aspergillus containing the benA22 mutation are resistant to benomyl for vegetative growth but do not produce conidia. To test whether conidiation involved an additional benomyl-sensitive tubulin (i.e., was mediated by a tubulin other than the tubulins coded for by the benA locus), a collection of mutants was produced that formed conidia in the presence of benomyl, i.e., were conidiation-resistant (CR-) mutants. We analyzed the tubulins of these CR- mutants using two-dimensional gel electrophoresis and found that the mutants lacked one species of beta-tubulin (designated beta 3). We have examined two of these mutants in detail. In crosses with strains containing wild-type tubulins, we found that the absence of the beta 3-tubulin co-segregated perfectly with the CR- phenotype. In diploids containing both the benA22 and CR- mutations, we found that the CR- phenotype was recessive and that beta 3-tubulin was present on two-dimensional gels of tubulins prepared from these diploids. In another set of crosses, these two CR- strains and seven others were first made auxotrophic for uridine and then crossed against strains that had homologously integrated a plasmid containing an incomplete internal fragment of the beta 3-tubulin gene and the pyr4 gene of Neurospora crassa (which confers uridine prototrophy on transformants). If the CR- phenotype were produced by a mutation in a gene distinct from the structural gene for beta 3-tubulin (designated the tubC gene), then crossing over should have produced some CR+ segregants among the uridine auxotrophic progeny of the second cross. All of the uridine auxotrophs from this type of cross, however, showed the CR- phenotype, suggesting that the mutation in these strains is at or closely linked to the tubC locus. The most obvious explanation of these results is that beta 3-tubulin is ordinarily used during conidiation and the presence of this species of beta-tubulin renders conidiation sensitive to benomyl. In the CR- mutants, beta 3-tubulin is absent, and in the presence of the benA22 mutation the benomyl-resistant beta 1-and/or beta 2-tubulin substitutes for beta 3 to make conidiation benomyl resistant. We discuss these results and give two models to explain the interactions between these beta-tubulin species.
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47

May, G. S., J. Gambino, J. A. Weatherbee, and N. R. Morris. "Identification and functional analysis of beta-tubulin genes by site specific integrative transformation in Aspergillus nidulans." Journal of Cell Biology 101, no. 3 (September 1, 1985): 712–19. http://dx.doi.org/10.1083/jcb.101.3.712.

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We have cloned two different beta-tubulin sequences from the filamentous fungus Aspergillus nidulans. Each was used in the construction of transforming plasmids that carry the pyr4 gene of Neurospora crassa. We used these plasmids to transform a pyrG-strain of Aspergillus to uridine prototrophy. Both plasmids were shown to integrate site specifically into the homologous chromosomal sequences. We then used transformant strains in genetic crosses to demonstrate that one of the cloned beta-tubulin sequences was the benA beta-tubulin gene, which codes for the beta 1-and beta 2-tubulins. The other cloned beta-tubulin sequence was shown to be the structural gene for beta 3-tubulin by gene disruption and to participate in conidial development. This is the first report of a gene disruption by site specific, integrative recombination in Aspergillus nidulans.
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48

Sadoul, Karin, Clotilde Joubert, Sophie Michallet, Elsie Nolte, Lauralie Peronne, Sacnicté Ramirez-Rios, Anne-Sophie Ribba, and Laurence Lafanechère. "Déchiffrage du code tubuline." médecine/sciences 34, no. 12 (December 2018): 1047–55. http://dx.doi.org/10.1051/medsci/2018295.

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Les microtubules sont des fibres du cytosquelette formées par l’assemblage d’hétérodimères d’α- et de β-tubuline. Ils contribuent à l’établissement de la forme des cellules et de leur polarité, ainsi qu’à leur mobilité. Ils jouent aussi un rôle important dans le transport intracellulaire et dans la division cellulaire. Le réseau microtubulaire s’adapte constamment aux besoins de la cellule. Il peut être constitué de microtubules très dynamiques ou d’autres plus stables. Pour moduler dans l’espace et le temps les différentes fonctions de ces fibres, de nombreuses modifications post-traductionnelles réversibles de la tubuline sont mises en jeu, à l’origine de ce qui est maintenant appelé le « code tubuline ». Dans cette revue, nous nous intéresserons au rôle de deux modifications caractéristiques des microtubules stables : l’acétylation et la détyrosination de l’α-tubuline. Nous discuterons également de l’implication de leur dérégulation dans certaines pathologies.
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49

Sherman, Donald R. "Impact of code differences for tubular members." Journal of Constructional Steel Research 18, no. 4 (January 1991): 317–25. http://dx.doi.org/10.1016/0143-974x(91)90011-o.

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50

Ghiţă, Ana-Maria. "Seismic Design Of Low-Rise Office Buildings According To Romanian Seismic Codes. Case Study." Mathematical Modelling in Civil Engineering 11, no. 2 (May 1, 2015): 10–18. http://dx.doi.org/10.1515/mmce-2015-0007.

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Abstract The paper presents a study case and highlights the changes made by the new, in force, seismic Code P100-1/2013 in comparison with the former P100-1/2006, concerning the reinforced concrete frame structural systems design. Different seismic designed RC frames systems, compatible with modern office requirements, were studied. The influence of the earthquake codes provisions on design of regular buildings, having openings fitted for open spaces, with a story height of 3.50m, was assessed. The benefits of tubular structures, with rigid frames made of closely spaced columns on the building perimeter, were analyzed as well. The results of the study case are presented emphasizing the consequences of the application of the new seismic Code on the computation of the reinforced concrete frame structures.
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