Artículos de revistas sobre el tema "Acetylation α-Tubulin"
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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 completoTomas-Roig, Jordi, Shyam Ramasamy, Diana Zbarsky, Ursula Havemann-Reinecke y Sigrid Hoyer-Fender. "Psychosocial stress and cannabinoid drugs affect acetylation of α-tubulin (K40) and gene expression in the prefrontal cortex of adult mice". PLOS ONE 17, n.º 9 (21 de septiembre de 2022): e0274352. http://dx.doi.org/10.1371/journal.pone.0274352.
Texto completoXie, Xi, Ruibao Ren, Bao yuan Zhang y Ping Liu. "Suppression of Microtubule Acetylation Mediates Theanti-Leukemic Effect of CDK9 Inhibition". Blood 142, Supplement 1 (28 de noviembre de 2023): 5772. http://dx.doi.org/10.1182/blood-2023-187901.
Texto completoAguilar, Andrea, Lars Becker, Thomas Tedeschi, Stefan Heller, Carlo Iomini y Maxence V. Nachury. "α-Tubulin K40 acetylation is required for contact inhibition of proliferation and cell–substrate adhesion". Molecular Biology of the Cell 25, n.º 12 (15 de junio de 2014): 1854–66. http://dx.doi.org/10.1091/mbc.e13-10-0609.
Texto completoKalebic, Nereo, Concepcion Martinez, Emerald Perlas, Philip Hublitz, Daniel Bilbao-Cortes, Karol Fiedorczuk, Annapaola Andolfo y Paul A. Heppenstall. "Tubulin Acetyltransferase αTAT1 Destabilizes Microtubules Independently of Its Acetylation Activity". Molecular and Cellular Biology 33, n.º 6 (28 de diciembre de 2012): 1114–23. http://dx.doi.org/10.1128/mcb.01044-12.
Texto completoRahimi, Amir Mohammad, Mingfang Cai, Irem Kılıҫ, Zahra Basir Kazerouni, Constanza Tapia Contreras y Sigrid Hoyer-Fender. "Expression of α-Tubulin Acetyltransferase 1 and Tubulin Acetylation as Selective Forces in Cell Competition". Cells 10, n.º 2 (14 de febrero de 2021): 390. http://dx.doi.org/10.3390/cells10020390.
Texto completoDorsch, Schuldt, Remedios, Schinkel, Jong, Michels, Kuster, Brundel y Velden. "Protein Quality Control Activation and Microtubule Remodeling in Hypertrophic Cardiomyopathy". Cells 8, n.º 7 (18 de julio de 2019): 741. http://dx.doi.org/10.3390/cells8070741.
Texto completoAslan, Joseph E., Kevin G. Phillips, Laura D. Healy, Asako Itakura, Jiaqing Pang y Owen J. T. McCarty. "Histone deacetylase 6-mediated deacetylation of α-tubulin coordinates cytoskeletal and signaling events during platelet activation". American Journal of Physiology-Cell Physiology 305, n.º 12 (15 de diciembre de 2013): C1230—C1239. http://dx.doi.org/10.1152/ajpcell.00053.2013.
Texto completoCoombes, Courtney, Ami Yamamoto, Mark McClellan, Taylor A. Reid, Melissa Plooster, G. W. Gant Luxton, Joshua Alper, Jonathon Howard y Melissa K. Gardner. "Mechanism of microtubule lumen entry for the α-tubulin acetyltransferase enzyme αTAT1". Proceedings of the National Academy of Sciences 113, n.º 46 (1 de noviembre de 2016): E7176—E7184. http://dx.doi.org/10.1073/pnas.1605397113.
Texto completoLabisso, Wajana, Ana-Caroline Raulin, Lucky Nwidu, Artur Kocon, Declan Wayne, Amaia Erdozain, Benito Morentin et al. "The Loss of α- and β-Tubulin Proteins Are a Pathological Hallmark of Chronic Alcohol Consumption and Natural Brain Ageing". Brain Sciences 8, n.º 9 (11 de septiembre de 2018): 175. http://dx.doi.org/10.3390/brainsci8090175.
Texto completoOthman, Ahmad, Marcus Winogradzki, Shreya Patel, Waddell Holmes, Alan Blank y Jitesh Pratap. "The Role of Runx2 in Microtubule Acetylation in Bone Metastatic Breast Cancer Cells". Cancers 14, n.º 14 (15 de julio de 2022): 3436. http://dx.doi.org/10.3390/cancers14143436.
Texto completoYu, Jinyan, Zhongsen Ma, Sreerama Shetty, Mengshi Ma y Jian Fu. "Selective HDAC6 inhibition prevents TNF-α-induced lung endothelial cell barrier disruption and endotoxin-induced pulmonary edema". American Journal of Physiology-Lung Cellular and Molecular Physiology 311, n.º 1 (1 de julio de 2016): L39—L47. http://dx.doi.org/10.1152/ajplung.00051.2016.
Texto completoLiu, Pengfei, Shengwei Zhang, Jingyi Ma, Dongning Jin, Yali Qin y Mingzhou Chen. "Vimentin inhibits α-tubulin acetylation via enhancing α-TAT1 degradation to suppress the replication of human parainfluenza virus type 3". PLOS Pathogens 18, n.º 9 (15 de septiembre de 2022): e1010856. http://dx.doi.org/10.1371/journal.ppat.1010856.
Texto completoLuo, J., S. Megee y I. Dobrinski. "288 THE EXPRESSION PATTERN OF ACETYLATED ALPHA-TUBULIN IS CONSERVED IN PORCINE AND MURINE SPERMATOGONIAL STEM CELLS". Reproduction, Fertility and Development 20, n.º 1 (2008): 223. http://dx.doi.org/10.1071/rdv20n1ab288.
Texto completoSun, Wanwei, Xiaojian Ma, Heping Wang, Yanyun Du, Jianwen Chen, Huijun Hu, Ru Gao et al. "MYO1F regulates antifungal immunity by regulating acetylation of microtubules". Proceedings of the National Academy of Sciences 118, n.º 30 (23 de julio de 2021): e2100230118. http://dx.doi.org/10.1073/pnas.2100230118.
Texto completoDelgado, Inês L. S., João Gonçalves, Rita Fernandes, Sara Zúquete, Afonso P. Basto, Alexandre Leitão, Helena Soares y Sofia Nolasco. "Balancing Act: Tubulin Glutamylation and Microtubule Dynamics in Toxoplasma gondii". Microorganisms 12, n.º 3 (28 de febrero de 2024): 488. http://dx.doi.org/10.3390/microorganisms12030488.
Texto completoStoner, Michael W., Dharendra Thapa, Manling Zhang, Gregory A. Gibson, Michael J. Calderon, Claudette M. St. Croix y Iain Scott. "α-Lipoic acid promotes α-tubulin hyperacetylation and blocks the turnover of mitochondria through mitophagy". Biochemical Journal 473, n.º 12 (10 de junio de 2016): 1821–30. http://dx.doi.org/10.1042/bcj20160281.
Texto completoShi, Lang, Zhixia Song, Chenglong Li, Fangjing Deng, Yao Xia, Jing Huang, Xiongfei Wu y Jiefu Zhu. "HDAC6 Inhibition Alleviates Ischemia- and Cisplatin-Induced Acute Kidney Injury by Promoting Autophagy". Cells 11, n.º 24 (7 de diciembre de 2022): 3951. http://dx.doi.org/10.3390/cells11243951.
Texto completoCreppe, Catherine y Marcus Buschbeck. "Elongator: An Ancestral Complex Driving Transcription and Migration through Protein Acetylation". Journal of Biomedicine and Biotechnology 2011 (2011): 1–8. http://dx.doi.org/10.1155/2011/924898.
Texto completoHowes, Stuart C., Gregory M. Alushin, Toshinobu Shida, Maxence V. Nachury y Eva Nogales. "Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure". Molecular Biology of the Cell 25, n.º 2 (15 de enero de 2014): 257–66. http://dx.doi.org/10.1091/mbc.e13-07-0387.
Texto completoSharma, Chiranjeev, Yong Jin Oh, Byoungduck Park, Sooyeun Lee, Chul-Ho Jeong, Sangkil Lee, Ji Hae Seo y Young Ho Seo. "Development of Thiazolidinedione-Based HDAC6 Inhibitors to Overcome Methamphetamine Addiction". International Journal of Molecular Sciences 20, n.º 24 (9 de diciembre de 2019): 6213. http://dx.doi.org/10.3390/ijms20246213.
Texto completoPatel, Shreya, Marcus Winogradzki, Ahmad Othman, Waddell Holmes y Jitesh Pratap. "Abstract 270: The novel control mechanism of the tubulin code and vesicular trafficking in breast cancer bone metastatic cells". Cancer Research 82, n.º 12_Supplement (15 de junio de 2022): 270. http://dx.doi.org/10.1158/1538-7445.am2022-270.
Texto completoHu, Yi. "Post-translational modification of cytoskeleton regulates anti-tumor cytotoxicity in γδ T cells". Journal of Immunology 204, n.º 1_Supplement (1 de mayo de 2020): 88.19. http://dx.doi.org/10.4049/jimmunol.204.supp.88.19.
Texto completoEshun-Wilson, Lisa, Rui Zhang, Didier Portran, Maxence V. Nachury, Daniel B. Toso, Thomas Löhr, Michele Vendruscolo, Massimiliano Bonomi, James S. Fraser y Eva Nogales. "Effects of α-tubulin acetylation on microtubule structure and stability". Proceedings of the National Academy of Sciences 116, n.º 21 (9 de mayo de 2019): 10366–71. http://dx.doi.org/10.1073/pnas.1900441116.
Texto completoSolinger, Jachen A., Roberta Paolinelli, Holger Klöß, Francesco Berlanda Scorza, Stefano Marchesi, Ursula Sauder, Dai Mitsushima, Fabrizio Capuani, Stephen R. Stürzenbaum y Giuseppe Cassata. "The Caenorhabditis elegans Elongator Complex Regulates Neuronal α-tubulin Acetylation". PLoS Genetics 6, n.º 1 (22 de enero de 2010): e1000820. http://dx.doi.org/10.1371/journal.pgen.1000820.
Texto completoKim, Byeong-Seong, Taegwan Yoon y Jee-Yin Ahn. "Id2 regulates α-tubulin acetylation by Sirt2, promoting axon growth". IBRO Reports 6 (septiembre de 2019): S471. http://dx.doi.org/10.1016/j.ibror.2019.07.1484.
Texto completoKim, Go-Woon, Lin Li, Mohammad Ghorbani, Linya You y Xiang-Jiao Yang. "Mice lacking α-tubulin acetyltransferase 1 are viable but display α-tubulin acetylation deficiency and dentate gyrus distortion." Journal of Biological Chemistry 291, n.º 48 (25 de noviembre de 2016): 25279. http://dx.doi.org/10.1074/jbc.a113.464792.
Texto completoKim, Go-Woon, Lin Li, Mohammad Gorbani, Linya You y Xiang-Jiao Yang. "Mice Lacking α-Tubulin Acetyltransferase 1 Are Viable but Display α-Tubulin Acetylation Deficiency and Dentate Gyrus Distortion". Journal of Biological Chemistry 288, n.º 28 (28 de mayo de 2013): 20334–50. http://dx.doi.org/10.1074/jbc.m113.464792.
Texto completoStemberger, Megan B., Julia A. Ju, Keyata N. Thompson, Trevor J. Mathias, Alexandra E. Jerrett, Katarina T. Chang, Eleanor C. Ory et al. "Hydrogen Peroxide Induces α-Tubulin Detyrosination and Acetylation and Impacts Breast Cancer Metastatic Phenotypes". Cells 12, n.º 9 (27 de abril de 2023): 1266. http://dx.doi.org/10.3390/cells12091266.
Texto completoPongrakhananon, Varisa, Hiroko Saito, Sylvain Hiver, Takaya Abe, Go Shioi, Wenxiang Meng y Masatoshi Takeichi. "CAMSAP3 maintains neuronal polarity through regulation of microtubule stability". Proceedings of the National Academy of Sciences 115, n.º 39 (6 de septiembre de 2018): 9750–55. http://dx.doi.org/10.1073/pnas.1803875115.
Texto completoValenzuela-Fernández, Agustín, Susana Álvarez, Mónica Gordon-Alonso, Marta Barrero, Ángeles Ursa, J. Román Cabrero, Gerónimo Fernández et al. "Histone Deacetylase 6 Regulates Human Immunodeficiency Virus Type 1 Infection". Molecular Biology of the Cell 16, n.º 11 (noviembre de 2005): 5445–54. http://dx.doi.org/10.1091/mbc.e05-04-0354.
Texto completoAdamakis, Ioannis-Dimosthenis S., Emmanuel Panteris y Eleftherios P. Eleftheriou. "Tubulin Acetylation Mediates Bisphenol A Effects on the Microtubule Arrays of Allium cepa and Triticum turgidum". Biomolecules 9, n.º 5 (11 de mayo de 2019): 185. http://dx.doi.org/10.3390/biom9050185.
Texto completoCarbajal, Agustín, María E. Chesta, C. Gastón Bisig y Carlos A. Arce. "A novel method for purification of polymerizable tubulin with a high content of the acetylated isotype". Biochemical Journal 449, n.º 3 (9 de enero de 2013): 643–48. http://dx.doi.org/10.1042/bj20121439.
Texto completoQu, Pengxiang, Zhenzi Zuo, Zhengqing Liu, Zhihan Niu, Ying Zhang, Yue Du, Xiaonan Ma et al. "Sperm-borne small RNAs regulate α-tubulin acetylation and epigenetic modification of early bovine somatic cell nuclear transfer embryos". Molecular Human Reproduction 25, n.º 8 (1 de mayo de 2019): 471–82. http://dx.doi.org/10.1093/molehr/gaz023.
Texto completoCueva, Juan G., Jen Hsin, Kerwyn Casey Huang y Miriam B. Goodman. "Posttranslational Acetylation of α-Tubulin Constrains Protofilament Number in Native Microtubules". Current Biology 22, n.º 12 (junio de 2012): 1066–74. http://dx.doi.org/10.1016/j.cub.2012.05.012.
Texto completoOhkawa, Noriaki, Shunichiro Sugisaki, Eri Tokunaga, Kazuko Fujitani, Mitsutoshi Setou y Kaoru Inokuchi. "ARD1-NAT1 complex regulates neuronal dendritic arborization through α-tubulin acetylation". Neuroscience Research 58 (enero de 2007): S88. http://dx.doi.org/10.1016/j.neures.2007.06.1080.
Texto completoLi, Wande, Yinzhi Zhao y Iih-Nan Chou. "Nickel (Ni2+) Enhancement of α-Tubulin Acetylation in Cultured 3T3 Cells". Toxicology and Applied Pharmacology 140, n.º 2 (octubre de 1996): 461–70. http://dx.doi.org/10.1006/taap.1996.0243.
Texto completoRyu, Na Mi y Jung Min Kim. "The role of the α-tubulin acetyltransferase αTAT1 in the DNA damage response". Journal of Cell Science 133, n.º 17 (11 de agosto de 2020): jcs246702. http://dx.doi.org/10.1242/jcs.246702.
Texto completoSanto, Loredana, Teru Hideshima, Andrew L. Kung, Jen-Chieh Tseng, David Tamang, Min Yang, Matthew Jarpe et al. "Pharmacodynamic and Pharmacokinetic Properties of a Novel and Selective HDAC6 Inhibitor, ACY-1215, in Combination with Bortezomib in Multiple Myeloma". Blood 118, n.º 21 (18 de noviembre de 2011): 2912. http://dx.doi.org/10.1182/blood.v118.21.2912.2912.
Texto completoRead, M., T. Sherwin, S. P. Holloway, K. Gull y J. E. Hyde. "Microtubular organization visualized by immunofluorescence microscopy during erythrocytic schizogony in Plasmodium falciparum and investigation of post-translational modifications of parasite tubulin". Parasitology 106, n.º 3 (abril de 1993): 223–32. http://dx.doi.org/10.1017/s0031182000075041.
Texto completoShimazu, Tadahiro, Sueharu Horinouchi y Minoru Yoshida. "Multiple Histone Deacetylases and the CREB-binding Protein Regulate Pre-mRNA 3′-End Processing". Journal of Biological Chemistry 282, n.º 7 (17 de diciembre de 2006): 4470–78. http://dx.doi.org/10.1074/jbc.m609745200.
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