Literatura académica sobre el tema "Acetylation α-Tubulin"
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Artículos de revistas sobre el tema "Acetylation α-Tubulin"
Chu, Chih-Wen, Fajian Hou, Junmei Zhang, Lilian Phu, Alex V. Loktev, Donald S. Kirkpatrick, Peter K. Jackson, Yingming Zhao y Hui Zou. "A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation". Molecular Biology of the Cell 22, n.º 4 (15 de febrero de 2011): 448–56. http://dx.doi.org/10.1091/mbc.e10-03-0203.
Texto completoCalogero, Alessandra Maria, Milo Jarno Basellini, Huseyin Berkcan Isilgan, Francesca Longhena, Arianna Bellucci, Samanta Mazzetti, Chiara Rolando, Gianni Pezzoli y Graziella Cappelletti. "Acetylated α-Tubulin and α-Synuclein: Physiological Interplay and Contribution to α-Synuclein Oligomerization". International Journal of Molecular Sciences 24, n.º 15 (31 de julio de 2023): 12287. http://dx.doi.org/10.3390/ijms241512287.
Texto completoYang, Wulin, Xiangxiang Guo, Shermaine Thein, Feng Xu, Shigeki Sugii, Peter W. Baas, George K. Radda y Weiping Han. "Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of α-tubulin". Biochemical Journal 449, n.º 3 (9 de enero de 2013): 605–12. http://dx.doi.org/10.1042/bj20121121.
Texto completoCarmona, Bruno, H. Susana Marinho, Catarina Lopes Matos, Sofia Nolasco y Helena Soares. "Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation". Biology 12, n.º 4 (6 de abril de 2023): 561. http://dx.doi.org/10.3390/biology12040561.
Texto completoAntel, Matthew, Taylor Simao, Muhammed Burak Bener y Mayu Inaba. "Drosophila CG17003/leaky (lky) is required for microtubule acetylation in early germ cells in Drosophila ovary". PLOS ONE 17, n.º 11 (7 de noviembre de 2022): e0276704. http://dx.doi.org/10.1371/journal.pone.0276704.
Texto completoNiu, Xiaoxiao, Chuan-Xi Mao, Shan Wang, Xiongxiong Wang, Youyu Zhang, Juncheng Hu, Ran Bi, Zhihua Liu y Jin Shan. "α-Tubulin acetylation at lysine 40 regulates dendritic arborization and larval locomotion by promoting microtubule stability in Drosophila". PLOS ONE 18, n.º 2 (24 de febrero de 2023): e0280573. http://dx.doi.org/10.1371/journal.pone.0280573.
Texto completoFernández-Barrera, Jaime, Miguel Bernabé-Rubio, Javier Casares-Arias, Laura Rangel, Laura Fernández-Martín, Isabel Correas y Miguel A. Alonso. "The actin-MRTF-SRF transcriptional circuit controls tubulin acetylation via α-TAT1 gene expression". Journal of Cell Biology 217, n.º 3 (10 de enero de 2018): 929–44. http://dx.doi.org/10.1083/jcb.201702157.
Texto completoEven, Aviel, Giovanni Morelli, Loïc Broix, Chiara Scaramuzzino, Silvia Turchetto, Ivan Gladwyn-Ng, Romain Le Bail et al. "ATAT1-enriched vesicles promote microtubule acetylation via axonal transport". Science Advances 5, n.º 12 (diciembre de 2019): eaax2705. http://dx.doi.org/10.1126/sciadv.aax2705.
Texto completoOlenieva, V. D., D. I. Lytvyn, A. I. Yemets y Ya B. Blume. "Expression profiling of kinesins, involved in the development of autophagy in Arabidopsis thaliana, and the role of tubulin acetylation in the interaction of Atg8 protein with microtubules". Faktori eksperimental'noi evolucii organizmiv 22 (9 de septiembre de 2018): 162–68. http://dx.doi.org/10.7124/feeo.v22.942.
Texto completoSadoul, Karin y Saadi Khochbin. "The growing landscape of tubulin acetylation: lysine 40 and many more". Biochemical Journal 473, n.º 13 (28 de junio de 2016): 1859–68. http://dx.doi.org/10.1042/bcj20160172.
Texto completoTesis sobre el tema "Acetylation α-Tubulin"
Francis, Sarah Louise. "The role of α-tubulin acetylation in the regulation of murine sperm motility". Thesis, Durham University, 2019. http://etheses.dur.ac.uk/12953/.
Texto completoWu, Yu-Ting y 吳雨亭. "Increase in Mitochondrial Mass and α-tubulin Acetylation of Human Cells in Response to Oxidative Stress". Thesis, 2003. http://ndltd.ncl.edu.tw/handle/86269180229037111337.
Texto completo中山醫學大學
生物化學研究所
91
Recent results suggest that both the mitochondrial mass and the mitochondrial DNA (mtDNA) copy number are increased during in vivo aging process and in vitro cellular replicative senescence. During the aging process, oxidative damage and mutation of mtDNA are accumulated and they contribute to the decline in mitochondrial respiratory function. Moreover, the increase in mitochondrial mass and mtDNA copy number in aged tissues was suggested as a result of a feedback mechanism to compensate for the impaired mitochondrial function with age. In a previous study, non-lethal concentration of H2O2 caused an increase in the mitochondrial mass and mtDNA copy number of human lung fibroblast cell MRC-5. However, the molecular mechanism is still unclear. In this thesis, I evaluated the mechanism and the effects of the increase in mitochondria and mtDNA by a previously established experimental model that the MRC-5 cells were treated with 180 μM of H2O2 for 48 hr. The results revealed that non-lethal concentration of H2O2 induced the increase in mitochondrial mass but not elevated the protein expressions of mitochondrial respiratory enzymes, which may thus lead to an increase in the ROS production in the cells harboring increased mitochondrial mass. Morever, the increase in mitochondrial mass induced by H2O2 is not a PPARγ coactivator-1 (PGC-1)-dependent event. On the other hand, it was shown that H2O2 induced an increase in the intracellular level of acetylated α-tubulin in a dose-dependent manner, and which was not dependent on the de novo protein synthesis. Morever, the level of acetylation in α-tubulin was not induced by CCCP treatment, which caused a loss of mitochondrial membrane potential or by oligomycin treatment, which inhibited mitochondrial ATP synthesis. In addition, an increased level of acetylation in α-tubulin was detected in the cells harboring no mtDNA or higher proportion of mutant mtDNA. The increased acetylated α-tubulin can be detected in the mitochondrial and cytosol fractions. Because the ROS content in these cybrid cells was not significantly changed, the results suggest that the increase in the level of acetylation in α-tubulin may be caused by a ROS-independent pathway.
Bílková, Karolína. "Vliv suplementace karotenoidy a oxidačního stresu na morfologii, kvalitu spermií a spermatogenezi u zebřičky pestré". Master's thesis, 2018. http://www.nusl.cz/ntk/nusl-380194.
Texto completoPalma, Andreia Filipa Martins. "The role of SIRT2 in alpha-tubulin, Tau and alpha-synuclein post-translational modifications in parkinson's disease". Master's thesis, 2015. http://hdl.handle.net/10316/30668.
Texto completoSporadic Parkinson’s disease (sPD) is characterized by mitochondrial dysfunction and the accumulation of protein aggregates in a specific group of neurons. It has already been demonstrated by our group that microtubule (MT) - dependent dynamics disruption due to mitochondrial dysfunction have a major role in sPD etiopathogenesis. Given that the MT network is disrupted in sPD cells and that microtubule associated proteins (MAPs) allow MT stabilization we aim to clarify the role of Sirtuin-2 (SIRT2), a NAD+ dependent protein that deacetylates α-tubulin in PD cellular neurodegeneration. We used human neuroblastoma SHSY-5Y cell lines that overexpressed α-synuclein (ASYN) and transmitochondrial cybrids that recapitulate pathogenic alterations observed in sPD patient brains. We confirmed that Tau protein and ASYN are MT-associated proteins. Moreover, our results suggested that α-tubulin acetylation induced by SIRT2 inhibition is functionally associated with the improvement of MT dynamic determined by decrease in phospho-Tau levels, or by increase in Tau/Tubulin and ASYN/tubulin binding. Our data provide a strong evidence for a functional role of tubulin and MAPs acetylation on autophagic vesicular traffic and cargos clearance. Additionally, we showed that an inherited mitochondrial dysfunction (sPD cybrids) or an accumulation of ASYN oligomers (overexpressed ASYN cells) imbalance mitochondrial fusion and fission events which further compromised autophagy. Moreover, this study indicates that MT can be a promising therapeutic target in the field of neurodegenerative disorders, like sPD, in which intracellular transport is altered.
Os casos esporádicos da doença de Parkinson (sPD) são caracterizados por disfunção mitocondrial, assim como, pela acumulação de agregados proteicos num grupo específico de neurónios. Já foi previamente demonstrado pelo nosso grupo que, a alteração dos mecanismos mediados por microtúbulos (MTs) em consequência da disfunção mitocondrial, tem um papel importante na etiopatogenia do sPD. Dado que a rede de MT está alterada nas células de doentes com sPD e que as proteínas associadas a microtúbulos (MAPs) permitem a estabilização dessa rede de MT, nós pretendemos clarificar o papel desempenhado pela Sirtuina-2, uma proteína dependente de NAD+ que induz a desacetilação da α-tubulina logo alterando a estabilidade dos MTs. Nós utilizámos células de neuroblastoma humano (SHSY-5Y) que sobreexpressam α-sinucleína (ASYN) e cíbridos transmitocondriais que recapitulam as alterações patogénicas observadas nos cérebros de sPD. Confirmámos que a proteína Tau e a ASYN são proteínas associadas aos microtúbulos. Os nossos resultados sugerem, inclusivamente, que os níveis de acetilação da α-tubulina estão associados à melhoria da dinâmica dos MT, evidenciada quer pelo decréscimo dos níveis de proteína Tau fosforilada, quer pelo aumento da interacção entre Tau/α-tubulina e ASYN/α-tubulina em células tratadas com um inibidor de SIRT2. Os nossos resultados sugerem fortemente que a acetilação da α-tubulina e das proteínas MAPs tem uma elevada importância funcional no transporte de vesículas autofágicas, assim como na eliminação de mitocôndrias disfuncionais e agregados proteicos. Demonstrámos também que, tanto a disfunção mitocondrial (cíbridos de sPD), como a acumulação de oligómeros de ASYN (células que sobreexpressam ASYN) promovem uma alteração dos mecanismos de fissão e fusão mitocondriais comprometendo a autofagia. Assim sendo, este estudo aponta para os MT como sendo um alvo terapêutico promissor no campo das doenças neurodegenerativas, como o sPD, em que o transporte intracelular está alterado.
Actas de conferencias sobre el tema "Acetylation α-Tubulin"
Boggs, Amanda E., Michele I. Vitolo, Rebecca A. Bettes, Jana Slovic, Monica S. Charpentier y Stuart S. Martin. "Abstract 2627: Acetylation of α-tubulin contributes to microtentacle formation and re-attachment in suspended breast tumor cells." En 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.am2013-2627.
Texto completoChang, Jang-Yang y Yun-Ching Cheng. "Abstract 4379: MPT0B292 enhances acetylation of α-tubulin through up-regulation of acetyltransferase gene, MEC-17 and exhibits potent anti-tumor, anti-angiogenesis and anti-metastatic effects in vitro and in vivo". En 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.am2015-4379.
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