Zeitschriftenartikel zum Thema „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 und Hui Zou. „A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation“. Molecular Biology of the Cell 22, Nr. 4 (15.02.2011): 448–56. http://dx.doi.org/10.1091/mbc.e10-03-0203.
Der volle Inhalt der QuelleCalogero, Alessandra Maria, Milo Jarno Basellini, Huseyin Berkcan Isilgan, Francesca Longhena, Arianna Bellucci, Samanta Mazzetti, Chiara Rolando, Gianni Pezzoli und Graziella Cappelletti. „Acetylated α-Tubulin and α-Synuclein: Physiological Interplay and Contribution to α-Synuclein Oligomerization“. International Journal of Molecular Sciences 24, Nr. 15 (31.07.2023): 12287. http://dx.doi.org/10.3390/ijms241512287.
Der volle Inhalt der QuelleYang, Wulin, Xiangxiang Guo, Shermaine Thein, Feng Xu, Shigeki Sugii, Peter W. Baas, George K. Radda und Weiping Han. „Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of α-tubulin“. Biochemical Journal 449, Nr. 3 (09.01.2013): 605–12. http://dx.doi.org/10.1042/bj20121121.
Der volle Inhalt der QuelleCarmona, Bruno, H. Susana Marinho, Catarina Lopes Matos, Sofia Nolasco und Helena Soares. „Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation“. Biology 12, Nr. 4 (06.04.2023): 561. http://dx.doi.org/10.3390/biology12040561.
Der volle Inhalt der QuelleAntel, Matthew, Taylor Simao, Muhammed Burak Bener und Mayu Inaba. „Drosophila CG17003/leaky (lky) is required for microtubule acetylation in early germ cells in Drosophila ovary“. PLOS ONE 17, Nr. 11 (07.11.2022): e0276704. http://dx.doi.org/10.1371/journal.pone.0276704.
Der volle Inhalt der QuelleNiu, Xiaoxiao, Chuan-Xi Mao, Shan Wang, Xiongxiong Wang, Youyu Zhang, Juncheng Hu, Ran Bi, Zhihua Liu und Jin Shan. „α-Tubulin acetylation at lysine 40 regulates dendritic arborization and larval locomotion by promoting microtubule stability in Drosophila“. PLOS ONE 18, Nr. 2 (24.02.2023): e0280573. http://dx.doi.org/10.1371/journal.pone.0280573.
Der volle Inhalt der QuelleFernández-Barrera, Jaime, Miguel Bernabé-Rubio, Javier Casares-Arias, Laura Rangel, Laura Fernández-Martín, Isabel Correas und Miguel A. Alonso. „The actin-MRTF-SRF transcriptional circuit controls tubulin acetylation via α-TAT1 gene expression“. Journal of Cell Biology 217, Nr. 3 (10.01.2018): 929–44. http://dx.doi.org/10.1083/jcb.201702157.
Der volle Inhalt der QuelleEven, 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, Nr. 12 (Dezember 2019): eaax2705. http://dx.doi.org/10.1126/sciadv.aax2705.
Der volle Inhalt der QuelleOlenieva, V. D., D. I. Lytvyn, A. I. Yemets und 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 (09.09.2018): 162–68. http://dx.doi.org/10.7124/feeo.v22.942.
Der volle Inhalt der QuelleSadoul, Karin, und Saadi Khochbin. „The growing landscape of tubulin acetylation: lysine 40 and many more“. Biochemical Journal 473, Nr. 13 (28.06.2016): 1859–68. http://dx.doi.org/10.1042/bcj20160172.
Der volle Inhalt der QuelleTomas-Roig, Jordi, Shyam Ramasamy, Diana Zbarsky, Ursula Havemann-Reinecke und 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, Nr. 9 (21.09.2022): e0274352. http://dx.doi.org/10.1371/journal.pone.0274352.
Der volle Inhalt der QuelleXie, Xi, Ruibao Ren, Bao yuan Zhang und Ping Liu. „Suppression of Microtubule Acetylation Mediates Theanti-Leukemic Effect of CDK9 Inhibition“. Blood 142, Supplement 1 (28.11.2023): 5772. http://dx.doi.org/10.1182/blood-2023-187901.
Der volle Inhalt der QuelleAguilar, Andrea, Lars Becker, Thomas Tedeschi, Stefan Heller, Carlo Iomini und Maxence V. Nachury. „α-Tubulin K40 acetylation is required for contact inhibition of proliferation and cell–substrate adhesion“. Molecular Biology of the Cell 25, Nr. 12 (15.06.2014): 1854–66. http://dx.doi.org/10.1091/mbc.e13-10-0609.
Der volle Inhalt der QuelleKalebic, Nereo, Concepcion Martinez, Emerald Perlas, Philip Hublitz, Daniel Bilbao-Cortes, Karol Fiedorczuk, Annapaola Andolfo und Paul A. Heppenstall. „Tubulin Acetyltransferase αTAT1 Destabilizes Microtubules Independently of Its Acetylation Activity“. Molecular and Cellular Biology 33, Nr. 6 (28.12.2012): 1114–23. http://dx.doi.org/10.1128/mcb.01044-12.
Der volle Inhalt der QuelleRahimi, Amir Mohammad, Mingfang Cai, Irem Kılıҫ, Zahra Basir Kazerouni, Constanza Tapia Contreras und Sigrid Hoyer-Fender. „Expression of α-Tubulin Acetyltransferase 1 and Tubulin Acetylation as Selective Forces in Cell Competition“. Cells 10, Nr. 2 (14.02.2021): 390. http://dx.doi.org/10.3390/cells10020390.
Der volle Inhalt der QuelleDorsch, Schuldt, Remedios, Schinkel, Jong, Michels, Kuster, Brundel und Velden. „Protein Quality Control Activation and Microtubule Remodeling in Hypertrophic Cardiomyopathy“. Cells 8, Nr. 7 (18.07.2019): 741. http://dx.doi.org/10.3390/cells8070741.
Der volle Inhalt der QuelleAslan, Joseph E., Kevin G. Phillips, Laura D. Healy, Asako Itakura, Jiaqing Pang und 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, Nr. 12 (15.12.2013): C1230—C1239. http://dx.doi.org/10.1152/ajpcell.00053.2013.
Der volle Inhalt der QuelleCoombes, Courtney, Ami Yamamoto, Mark McClellan, Taylor A. Reid, Melissa Plooster, G. W. Gant Luxton, Joshua Alper, Jonathon Howard und Melissa K. Gardner. „Mechanism of microtubule lumen entry for the α-tubulin acetyltransferase enzyme αTAT1“. Proceedings of the National Academy of Sciences 113, Nr. 46 (01.11.2016): E7176—E7184. http://dx.doi.org/10.1073/pnas.1605397113.
Der volle Inhalt der QuelleLabisso, 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, Nr. 9 (11.09.2018): 175. http://dx.doi.org/10.3390/brainsci8090175.
Der volle Inhalt der QuelleOthman, Ahmad, Marcus Winogradzki, Shreya Patel, Waddell Holmes, Alan Blank und Jitesh Pratap. „The Role of Runx2 in Microtubule Acetylation in Bone Metastatic Breast Cancer Cells“. Cancers 14, Nr. 14 (15.07.2022): 3436. http://dx.doi.org/10.3390/cancers14143436.
Der volle Inhalt der QuelleYu, Jinyan, Zhongsen Ma, Sreerama Shetty, Mengshi Ma und 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, Nr. 1 (01.07.2016): L39—L47. http://dx.doi.org/10.1152/ajplung.00051.2016.
Der volle Inhalt der QuelleLiu, Pengfei, Shengwei Zhang, Jingyi Ma, Dongning Jin, Yali Qin und 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, Nr. 9 (15.09.2022): e1010856. http://dx.doi.org/10.1371/journal.ppat.1010856.
Der volle Inhalt der QuelleLuo, J., S. Megee und I. Dobrinski. „288 THE EXPRESSION PATTERN OF ACETYLATED ALPHA-TUBULIN IS CONSERVED IN PORCINE AND MURINE SPERMATOGONIAL STEM CELLS“. Reproduction, Fertility and Development 20, Nr. 1 (2008): 223. http://dx.doi.org/10.1071/rdv20n1ab288.
Der volle Inhalt der QuelleSun, 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, Nr. 30 (23.07.2021): e2100230118. http://dx.doi.org/10.1073/pnas.2100230118.
Der volle Inhalt der QuelleDelgado, Inês L. S., João Gonçalves, Rita Fernandes, Sara Zúquete, Afonso P. Basto, Alexandre Leitão, Helena Soares und Sofia Nolasco. „Balancing Act: Tubulin Glutamylation and Microtubule Dynamics in Toxoplasma gondii“. Microorganisms 12, Nr. 3 (28.02.2024): 488. http://dx.doi.org/10.3390/microorganisms12030488.
Der volle Inhalt der QuelleStoner, Michael W., Dharendra Thapa, Manling Zhang, Gregory A. Gibson, Michael J. Calderon, Claudette M. St. Croix und Iain Scott. „α-Lipoic acid promotes α-tubulin hyperacetylation and blocks the turnover of mitochondria through mitophagy“. Biochemical Journal 473, Nr. 12 (10.06.2016): 1821–30. http://dx.doi.org/10.1042/bcj20160281.
Der volle Inhalt der QuelleShi, Lang, Zhixia Song, Chenglong Li, Fangjing Deng, Yao Xia, Jing Huang, Xiongfei Wu und Jiefu Zhu. „HDAC6 Inhibition Alleviates Ischemia- and Cisplatin-Induced Acute Kidney Injury by Promoting Autophagy“. Cells 11, Nr. 24 (07.12.2022): 3951. http://dx.doi.org/10.3390/cells11243951.
Der volle Inhalt der QuelleCreppe, Catherine, und 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.
Der volle Inhalt der QuelleHowes, Stuart C., Gregory M. Alushin, Toshinobu Shida, Maxence V. Nachury und Eva Nogales. „Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure“. Molecular Biology of the Cell 25, Nr. 2 (15.01.2014): 257–66. http://dx.doi.org/10.1091/mbc.e13-07-0387.
Der volle Inhalt der QuelleSharma, Chiranjeev, Yong Jin Oh, Byoungduck Park, Sooyeun Lee, Chul-Ho Jeong, Sangkil Lee, Ji Hae Seo und Young Ho Seo. „Development of Thiazolidinedione-Based HDAC6 Inhibitors to Overcome Methamphetamine Addiction“. International Journal of Molecular Sciences 20, Nr. 24 (09.12.2019): 6213. http://dx.doi.org/10.3390/ijms20246213.
Der volle Inhalt der QuellePatel, Shreya, Marcus Winogradzki, Ahmad Othman, Waddell Holmes und Jitesh Pratap. „Abstract 270: The novel control mechanism of the tubulin code and vesicular trafficking in breast cancer bone metastatic cells“. Cancer Research 82, Nr. 12_Supplement (15.06.2022): 270. http://dx.doi.org/10.1158/1538-7445.am2022-270.
Der volle Inhalt der QuelleHu, Yi. „Post-translational modification of cytoskeleton regulates anti-tumor cytotoxicity in γδ T cells“. Journal of Immunology 204, Nr. 1_Supplement (01.05.2020): 88.19. http://dx.doi.org/10.4049/jimmunol.204.supp.88.19.
Der volle Inhalt der QuelleEshun-Wilson, Lisa, Rui Zhang, Didier Portran, Maxence V. Nachury, Daniel B. Toso, Thomas Löhr, Michele Vendruscolo, Massimiliano Bonomi, James S. Fraser und Eva Nogales. „Effects of α-tubulin acetylation on microtubule structure and stability“. Proceedings of the National Academy of Sciences 116, Nr. 21 (09.05.2019): 10366–71. http://dx.doi.org/10.1073/pnas.1900441116.
Der volle Inhalt der QuelleSolinger, Jachen A., Roberta Paolinelli, Holger Klöß, Francesco Berlanda Scorza, Stefano Marchesi, Ursula Sauder, Dai Mitsushima, Fabrizio Capuani, Stephen R. Stürzenbaum und Giuseppe Cassata. „The Caenorhabditis elegans Elongator Complex Regulates Neuronal α-tubulin Acetylation“. PLoS Genetics 6, Nr. 1 (22.01.2010): e1000820. http://dx.doi.org/10.1371/journal.pgen.1000820.
Der volle Inhalt der QuelleKim, Byeong-Seong, Taegwan Yoon und Jee-Yin Ahn. „Id2 regulates α-tubulin acetylation by Sirt2, promoting axon growth“. IBRO Reports 6 (September 2019): S471. http://dx.doi.org/10.1016/j.ibror.2019.07.1484.
Der volle Inhalt der QuelleKim, Go-Woon, Lin Li, Mohammad Ghorbani, Linya You und 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, Nr. 48 (25.11.2016): 25279. http://dx.doi.org/10.1074/jbc.a113.464792.
Der volle Inhalt der QuelleKim, Go-Woon, Lin Li, Mohammad Gorbani, Linya You und 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, Nr. 28 (28.05.2013): 20334–50. http://dx.doi.org/10.1074/jbc.m113.464792.
Der volle Inhalt der QuelleStemberger, 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, Nr. 9 (27.04.2023): 1266. http://dx.doi.org/10.3390/cells12091266.
Der volle Inhalt der QuellePongrakhananon, Varisa, Hiroko Saito, Sylvain Hiver, Takaya Abe, Go Shioi, Wenxiang Meng und Masatoshi Takeichi. „CAMSAP3 maintains neuronal polarity through regulation of microtubule stability“. Proceedings of the National Academy of Sciences 115, Nr. 39 (06.09.2018): 9750–55. http://dx.doi.org/10.1073/pnas.1803875115.
Der volle Inhalt der QuelleValenzuela-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, Nr. 11 (November 2005): 5445–54. http://dx.doi.org/10.1091/mbc.e05-04-0354.
Der volle Inhalt der QuelleAdamakis, Ioannis-Dimosthenis S., Emmanuel Panteris und Eleftherios P. Eleftheriou. „Tubulin Acetylation Mediates Bisphenol A Effects on the Microtubule Arrays of Allium cepa and Triticum turgidum“. Biomolecules 9, Nr. 5 (11.05.2019): 185. http://dx.doi.org/10.3390/biom9050185.
Der volle Inhalt der QuelleCarbajal, Agustín, María E. Chesta, C. Gastón Bisig und Carlos A. Arce. „A novel method for purification of polymerizable tubulin with a high content of the acetylated isotype“. Biochemical Journal 449, Nr. 3 (09.01.2013): 643–48. http://dx.doi.org/10.1042/bj20121439.
Der volle Inhalt der QuelleQu, 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, Nr. 8 (01.05.2019): 471–82. http://dx.doi.org/10.1093/molehr/gaz023.
Der volle Inhalt der QuelleCueva, Juan G., Jen Hsin, Kerwyn Casey Huang und Miriam B. Goodman. „Posttranslational Acetylation of α-Tubulin Constrains Protofilament Number in Native Microtubules“. Current Biology 22, Nr. 12 (Juni 2012): 1066–74. http://dx.doi.org/10.1016/j.cub.2012.05.012.
Der volle Inhalt der QuelleOhkawa, Noriaki, Shunichiro Sugisaki, Eri Tokunaga, Kazuko Fujitani, Mitsutoshi Setou und Kaoru Inokuchi. „ARD1-NAT1 complex regulates neuronal dendritic arborization through α-tubulin acetylation“. Neuroscience Research 58 (Januar 2007): S88. http://dx.doi.org/10.1016/j.neures.2007.06.1080.
Der volle Inhalt der QuelleLi, Wande, Yinzhi Zhao und Iih-Nan Chou. „Nickel (Ni2+) Enhancement of α-Tubulin Acetylation in Cultured 3T3 Cells“. Toxicology and Applied Pharmacology 140, Nr. 2 (Oktober 1996): 461–70. http://dx.doi.org/10.1006/taap.1996.0243.
Der volle Inhalt der QuelleRyu, Na Mi, und Jung Min Kim. „The role of the α-tubulin acetyltransferase αTAT1 in the DNA damage response“. Journal of Cell Science 133, Nr. 17 (11.08.2020): jcs246702. http://dx.doi.org/10.1242/jcs.246702.
Der volle Inhalt der QuelleSanto, 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, Nr. 21 (18.11.2011): 2912. http://dx.doi.org/10.1182/blood.v118.21.2912.2912.
Der volle Inhalt der QuelleRead, M., T. Sherwin, S. P. Holloway, K. Gull und 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, Nr. 3 (April 1993): 223–32. http://dx.doi.org/10.1017/s0031182000075041.
Der volle Inhalt der QuelleShimazu, Tadahiro, Sueharu Horinouchi und Minoru Yoshida. „Multiple Histone Deacetylases and the CREB-binding Protein Regulate Pre-mRNA 3′-End Processing“. Journal of Biological Chemistry 282, Nr. 7 (17.12.2006): 4470–78. http://dx.doi.org/10.1074/jbc.m609745200.
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