Добірка наукової літератури з теми "Acetylation α-Tubulin"
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Статті в журналах з теми "Acetylation α-Tubulin":
1
Chu, Chih-Wen, Fajian Hou, Junmei Zhang, Lilian Phu, Alex V. Loktev, Donald S. Kirkpatrick, Peter K. Jackson, Yingming Zhao та Hui Zou. "A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation". Molecular Biology of the Cell 22, № 4 (15 лютого 2011): 448–56. http://dx.doi.org/10.1091/mbc.e10-03-0203.
Анотація:
Dynamic instability is a critical property of microtubules (MTs). By regulating the rate of tubulin polymerization and depolymerization, cells organize the MT cytoskeleton to accommodate their specific functions. Among many processes, posttranslational modifications of tubulin are implicated in regulating MT functions. Here we report a novel tubulin acetylation catalyzed by acetyltransferase San at lysine 252 (K252) of β-tubulin. This acetylation, which is also detected in vivo, is added to soluble tubulin heterodimers but not tubulins in MTs. The acetylation-mimicking K252A/Q mutants were incorporated into the MT cytoskeleton in HeLa cells without causing any obvious MT defect. However, after cold-induced catastrophe, MT regrowth is accelerated in San-siRNA cells while the incorporation of acetylation-mimicking mutant tubulins is severely impeded. K252 of β-tubulin localizes at the interface of α-/β-tubulins and interacts with the phosphate group of the α-tubulin-bound GTP. We propose that the acetylation slows down tubulin incorporation into MTs by neutralizing the positive charge on K252 and allowing tubulin heterodimers to adopt a conformation that disfavors tubulin incorporation.
2
Calogero, Alessandra Maria, Milo Jarno Basellini, Huseyin Berkcan Isilgan, Francesca Longhena, Arianna Bellucci, Samanta Mazzetti, Chiara Rolando, Gianni Pezzoli та Graziella Cappelletti. "Acetylated α-Tubulin and α-Synuclein: Physiological Interplay and Contribution to α-Synuclein Oligomerization". International Journal of Molecular Sciences 24, № 15 (31 липня 2023): 12287. http://dx.doi.org/10.3390/ijms241512287.
Анотація:
Emerging evidence supports that altered α-tubulin acetylation occurs in Parkinson’s disease (PD), a neurodegenerative disorder characterized by the deposition of α-synuclein fibrillary aggregates within Lewy bodies and nigrostriatal neuron degeneration. Nevertheless, studies addressing the interplay between α-tubulin acetylation and α-synuclein are lacking. Here, we investigated the relationship between α-synuclein and microtubules in primary midbrain murine neurons and the substantia nigra of post-mortem human brains. Taking advantage of immunofluorescence and Proximity Ligation Assay (PLA), a method allowing us to visualize protein–protein interactions in situ, combined with confocal and super-resolution microscopy, we found that α-synuclein and acetylated α-tubulin colocalized and were in close proximity. Next, we employed an α-synuclein overexpressing cellular model and tested the role of α-tubulin acetylation in α-synuclein oligomer formation. We used the α-tubulin deacetylase HDAC6 inhibitor Tubacin to modulate α-tubulin acetylation, and we evaluated the presence of α-synuclein oligomers by PLA. We found that the increase in acetylated α-tubulin significantly induced α-synuclein oligomerization. In conclusion, we unraveled the link between acetylated α-tubulin and α-synuclein and demonstrated that α-tubulin acetylation could trigger the early step of α-synuclein aggregation. These data suggest that the proper regulation of α-tubulin acetylation might be considered a therapeutic strategy to take on PD.
3
Yang, Wulin, Xiangxiang Guo, Shermaine Thein, Feng Xu, Shigeki Sugii, Peter W. Baas, George K. Radda та Weiping Han. "Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of α-tubulin". Biochemical Journal 449, № 3 (9 січня 2013): 605–12. http://dx.doi.org/10.1042/bj20121121.
Анотація:
Cytoskeleton remodelling is a prerequisite step for the morphological transition from preadipocytes to mature adipocytes. Although microtubules play a pivotal role in organizing cellular structure, regulation of microtubule dynamics during adipogenesis remains unclear. In the present paper we show that acetylation of α-tubulin is up-regulated during adipogenesis, and adipocyte development is dependent on α-tubulin acetylation, as expression of an acetylation-resistant α-tubulin mutant significantly inhibits adipogenesis. Moreover, acetylation of α-tubulin is under the control of the acetyltransferase MEC-17 and deacetylases SIRT2 (Sirtuin 2) and HDAC6 (histone deacetylase 6). Adipocyte development is inhibited in MEC-17-knockdown cells, but enhanced in MEC-17-overexpressing cells. Finally, we show that katanin, a microtubule-severing protein with enhanced activity on acetylated α-tubulin, is actively involved in adipogenesis. We propose that co-ordinated up-regulation of α-tubulin acetylation initiates cytoskeleton remodelling by promoting α-tubulin severing by katanin which, in turn, allows expansion of lipid droplets and accelerates the morphological transition toward mature adipocytes.
4
Carmona, Bruno, H. Susana Marinho, Catarina Lopes Matos, Sofia Nolasco, and Helena Soares. "Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation." Biology 12, no. 4 (April 6, 2023): 561. http://dx.doi.org/10.3390/biology12040561.
Анотація:
Microtubules (MTs), dynamic polymers of α/β-tubulin heterodimers found in all eukaryotes, are involved in cytoplasm spatial organization, intracellular transport, cell polarity, migration and division, and in cilia biology. MTs functional diversity depends on the differential expression of distinct tubulin isotypes and is amplified by a vast number of different post-translational modifications (PTMs). The addition/removal of PTMs to α- or β-tubulins is catalyzed by specific enzymes and allows combinatory patterns largely enriching the distinct biochemical and biophysical properties of MTs, creating a code read by distinct proteins, including microtubule-associated proteins (MAPs), which allow cellular responses. This review is focused on tubulin-acetylation, whose cellular roles continue to generate debate. We travel through the experimental data pointing to α-tubulin Lys40 acetylation role as being a MT stabilizer and a typical PTM of long lived MTs, to the most recent data, suggesting that Lys40 acetylation enhances MT flexibility and alters the mechanical properties of MTs, preventing MTs from mechanical aging characterized by structural damage. Additionally, we discuss the regulation of tubulin acetyltransferases/desacetylases and their impacts on cell physiology. Finally, we analyze how changes in MT acetylation levels have been found to be a general response to stress and how they are associated with several human pathologies.
5
Antel, Matthew, Taylor Simao, Muhammed Burak Bener, and Mayu Inaba. "Drosophila CG17003/leaky (lky) is required for microtubule acetylation in early germ cells in Drosophila ovary." PLOS ONE 17, no. 11 (November 7, 2022): e0276704. http://dx.doi.org/10.1371/journal.pone.0276704.
Анотація:
Microtubule acetylation is found in populations of stable, long-lived microtubules, occurring on the conserved lysine 40 (K40) residue of α-tubulin by α-tubulin acetyltransferases (αTATs). α-tubulin K40 acetylation has been shown to stabilize microtubules via enhancing microtubule resilience against mechanical stress. Here we show that a previously uncharacterized αTAT, Drosophila CG17003/leaky (lky), is required for α-tubulin K40 acetylation in early germ cells in Drosophila ovary. We found that loss of lky resulted in a progressive egg chamber fusion phenotype accompanied with mislocalization of germline-specific Vasa protein in somatic follicle cells. The same phenotype was observed upon replacement of endogenous α-tubulin84B with non-acetylatable α-tubulin84BK40A, suggesting α-tubulin K40 acetylation is responsible for the phenotype. Chemical disturbance of microtubules by Colcemid treatment resulted in a mislocalization of Vasa in follicle cells within a short period of time (~30 min), suggesting that the observed mislocalization is likely caused by direct leakage of cellular contents between germline and follicle cells. Taken together, this study provides a new function of α-tubulin acetylation in maintaining the cellular identity possibly by preventing the leakage of tissue-specific gene products between juxtaposing distinct cell types.
6
Niu, Xiaoxiao, Chuan-Xi Mao, Shan Wang, Xiongxiong Wang, Youyu Zhang, Juncheng Hu, Ran Bi, Zhihua Liu та Jin Shan. "α-Tubulin acetylation at lysine 40 regulates dendritic arborization and larval locomotion by promoting microtubule stability in Drosophila". PLOS ONE 18, № 2 (24 лютого 2023): e0280573. http://dx.doi.org/10.1371/journal.pone.0280573.
Анотація:
Posttranslational modification of tubulin increases the dynamic complexity and functional diversity of microtubules. Acetylation of α-tubulin at Lys-40 is a highly conserved posttranslational modification that has been shown to improve the flexibility and resilience of microtubules. Here we studied the in vivo functions of α-tubulin acetylation by knocking-out Atat, the Drosophila α-tubulin acetyltransferase, and by mutating Lys-40 to Arg in α1-tubulin. We found a reduction in the dendritic arborization of larval class I dendritic arborization (da) neurons in both mutants. The dendritic developmental defects in atat mutants could be reversed by enhancing the stability of microtubules either through knocking down the microtubule severing protein Katanin 60 or through overexpressing tubulin-specific chaperone E, suggesting that α-tubulin deacetylation impairsed dendritic morphology by decreasing the stability of microtubules. Using time-lapse recordings, we found that atat and α1-tubulinK40R mutations dramatically increased the number of dendritic protrusions that were likely to be immature dendritic precursors. Finally, we showed that both Atat and α-tubulin acetylation were required in class I da neurons to control larval locomotion. These findings add novel insight into the current knowledge of the role of α-tubulin acetylation in regulating neuronal development and functions.
7
Fernández-Barrera, Jaime, Miguel Bernabé-Rubio, Javier Casares-Arias, Laura Rangel, Laura Fernández-Martín, Isabel Correas та Miguel A. Alonso. "The actin-MRTF-SRF transcriptional circuit controls tubulin acetylation via α-TAT1 gene expression". Journal of Cell Biology 217, № 3 (10 січня 2018): 929–44. http://dx.doi.org/10.1083/jcb.201702157.
Анотація:
The role of formins in microtubules is not well understood. In this study, we have investigated the mechanism by which INF2, a formin mutated in degenerative renal and neurological hereditary disorders, controls microtubule acetylation. We found that silencing of INF2 in epithelial RPE-1 cells produced a dramatic drop in tubulin acetylation, increased the G-actin/F-actin ratio, and impaired myocardin-related transcription factor (MRTF)/serum response factor (SRF)–dependent transcription, which is known to be repressed by increased levels of G-actin. The effect on tubulin acetylation was caused by the almost complete absence of α-tubulin acetyltransferase 1 (α-TAT1) messenger RNA (mRNA). Activation of the MRTF-SRF transcriptional complex restored α-TAT1 mRNA levels and tubulin acetylation. Several functional MRTF-SRF–responsive elements were consistently identified in the α-TAT1 gene. The effect of INF2 silencing on microtubule acetylation was also observed in epithelial ECV304 cells, but not in Jurkat T cells. Therefore, the actin-MRTF-SRF circuit controls α-TAT1 transcription. INF2 regulates the circuit, and hence microtubule acetylation, in cell types where it has a prominent role in actin polymerization.
8
Even, 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, no. 12 (December 2019): eaax2705. http://dx.doi.org/10.1126/sciadv.aax2705.
Анотація:
Microtubules are polymerized dimers of α- and β-tubulin that underlie a broad range of cellular activities. Acetylation of α-tubulin by the acetyltransferase ATAT1 modulates microtubule dynamics and functions in neurons. However, it remains unclear how this enzyme acetylates microtubules over long distances in axons. Here, we show that loss of ATAT1 impairs axonal transport in neurons in vivo, and cell-free motility assays confirm a requirement of α-tubulin acetylation for proper bidirectional vesicular transport. Moreover, we demonstrate that the main cellular pool of ATAT1 is transported at the cytosolic side of neuronal vesicles that are moving along axons. Together, our data suggest that axonal transport of ATAT1-enriched vesicles is the predominant driver of α-tubulin acetylation in axons.
9
Olenieva, V. D., D. I. Lytvyn, A. I. Yemets, and Ya B. Blume. "Expression profiling of kinesins, involved in the development of autophagy in Arabidopsis thaliana, and the role of tubulin acetylation in the interaction of Atg8 protein with microtubules." Faktori eksperimental'noi evolucii organizmiv 22 (September 9, 2018): 162–68. http://dx.doi.org/10.7124/feeo.v22.942.
Анотація:
Aim. To investigate the interrelation between changes in the expression levels of kinesin genes that are potentially involved in the development of stress-induced autophagy in Arabidopsis thaliana by means of microtubules, and the structural biology analysis of the role of α-tubulin acetylation in the regulation of interaction of α-tubulin with Atg8. Methods. The simulation of the influence of abiotic stresses. PCR analysis of changes in expression levels of kinesin genes. The molecular dynamics simulations of α-tubulin and Atg8 complexes were performed using the GROMACS 4.5.5 program. Results. It was shown that the changes in expression levels were caused by the influence of stressful stimuli. A significant increase in the transcriptional activity of the KIN5B, KIN12B, KIN12F genes after UV-B irradiation, the KIN6, KIN7O, KIN7D, KIN12B genes under osmotic-, and KIN6, KIN12B under salt stress was detected. By means of bioinformatics it was demonstrated that α-tubulin acetylation provides an enhanced interaction of α-tubulin and Atg8 protein. Conclusions. Obtained data point out the important role of kinesins and α-tubulin acetylation in realization of microtubules’ partaking in the development of stress-induced autophagy in plants.
Keywords: microtubules, α-tubulin, kinesins, Atg8 protein, stress-induced autophagy.
10
Sadoul, Karin, and Saadi Khochbin. "The growing landscape of tubulin acetylation: lysine 40 and many more." Biochemical Journal 473, no. 13 (June 28, 2016): 1859–68. http://dx.doi.org/10.1042/bcj20160172.
Анотація:
Tubulin heterodimers are the building block of microtubules, which are major elements of the cytoskeleton. Several types of post-translational modifications are found on tubulin subunits as well as on the microtubule polymer to regulate the multiple roles of microtubules. Acetylation of lysine 40 (K40) of the α-tubulin subunit is one of these post-translational modifications which has been extensively studied. We summarize the current knowledge about the structural aspects of K40 acetylation, the functional consequences, the enzymes involved and their regulation. Most importantly, we discuss the potential importance of the recently discovered additional acetylation acceptor lysines in tubulin subunits and highlight the urgent need to study tubulin acetylation in a more integrated perspective.
Дисертації з теми "Acetylation α-Tubulin":
1
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/.
Анотація:
Sperm motility is a vital function required for fertility and is a consequence of interactions between components of the axoneme in the sperm flagellum. Microtubules, made up of α and β-tubulin, are a central component of the axoneme and undergo various post translational modifications. One such modification is the acetylation of the lysine 40 residue of α-tubulin which is carried out by α-tubulin acetyltransferase (α-TAT1), and is deacetylated by the activities of histone deacetylase 6 (HDAC6) and SIRT2. Recently, research has implicated α-tubulin acetylation in the regulation of sperm motility. The work presented in this thesis therefore aimed to study the influence that the state of α-tubulin acetylation has on sperm function by assessing the role of α-tubulin deacetylation in sperm motility modulation. To do this, murine sperm were treated with the HDAC6-specific inhibitor, tubacin; the general Class I and II HDAC inhibitor trichostatin A (TSA); and the general Class III HDAC inhibitor, nicotinamide. Exposure to the inhibitors did not significantly affect sperm motility or levels of acetylated α-tubulin. Furthermore, high baseline levels of acetylated α-tubulin were found in sperm. Subsequent examination of HDAC activity demonstrated that HDAC6 was active and could be inhibited in live murine sperm. Taken together, the results indicated that HDAC6 activity in sperm was low, suggesting that highly acetylated α-tubulin may be important for sperm function. As acetylation is indicative of microtubule stability, the effect of microtubule destabilisation using the drug, nocodazole, was assessed. Both α-tubulin organisation and acetylation remained intact in sperm following treatment, though nocodazole was found to significantly enhance certain motility parameters. This thesis therefore reports the novel finding that treatment with a microtubule depolymerising drug can alter sperm motility, indicating that subtle changes in microtubule conformation may influence flagellar motion which could have important implications for infertility caused by impaired sperm motility.
2
Wu, Yu-Ting, та 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.
Анотація:
碩士中山醫學大學
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.
3
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.
Анотація:
The phenotype-linked fertility hypothesis predicts that both, male carotenoid-based sexual ornamentation and their spermatozoa are phenotypically plastic and may be co-affected by the environment. One of the factors affecting their phenotype may be oxidative stress and the ability of organism to eliminate its effect. Oxidative stress may reduce sperm quality because sperm lack the ability to repair DNA, but it can also affect spermatogenesis itself. However, some substances may function as antioxidants, and thus eliminate effect of reactive oxygen species (oxidative stress) in the body. In this study, adult zebra finch males (Taeniopygia guttata) originating from the domesticated and recently wild-derived populations were exposed to the diquat (D), which enhances the oxidative stress, and carotenoid lutein (L), which could have an antioxidant function. Experimental design had factorial character 2x2 with a control (group L, D, LD, control). Neither oxidative stress, carotenoids, nor their interactions affected sperm morphology or velocity and it also did not increase abnormal sperm proportion in the ejaculate. However, the differences were observed at the molecular level, where by inducing the oxidative stress, the sperm had reduced signal intensity of acetylated α-tubulin in the sperm tails....
4
Palma, 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.
Анотація:
Trabalho final de mestrado integrado em Medicina (Biologia Molecular), apresentado à Faculdade de Medicina da Universidade de Coimbra.Sporadic 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.
Тези доповідей конференцій з теми "Acetylation α-Tubulin":
1
Boggs, Amanda E., Michele I. Vitolo, Rebecca A. Bettes, Jana Slovic, Monica S. Charpentier та Stuart S. Martin. "Abstract 2627: Acetylation of α-tubulin contributes to microtentacle formation and re-attachment in suspended breast tumor cells." У 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.
2
Chang, Jang-Yang, та 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". У 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.